NOVEL ENDOGLUCANASES

Abstract: An enzyme preparation consisting essentially of an enzyme having cellulolytic activity and comprising a first amino acid sequence of 14 residues having the sequence Thr Arg X3 X4 Asp Cys Cys X8 X9 X10 Cys X12 Trp X14, in which X3 and X4 independently is Trp, Tyr or Phe; X8 is Arg, Lys or His; each of X9, X10, X12 and X13 is any of the 20 naturally occurring amino acid residues; and a second amino acid sequence of 5 residues having the sequence Trp Cys Cys XX4 Cys, in which XX4 is any of the 20 naturally occurring amino acid residues with the proviso that, in the first amino acid sequence, (i) when X12 is Ser, then X14 is not Ser, and (ii) when X12 is Gly, then X14 is not Ala; performs excellently in detergent, laundering, textile and papermaking pulp applications.

Description: NOVEL ENDOGLUCANASES The present invention relates to novel enzyme preparations comprising an enzyme exhibiting endoglucanase activity which performs very good in indus¬ trial applications such as laundry compositions, for biopolishing of newly manufactured textiles, for provid- ing an abraded look of cellulosic fabric or garment, and for treatment of paper pulp. Further, the invention relates to DNA constructs encoding such enzymes, a method for providing a gene encoding for such enzymes, a method of producing the enzymes, enzyme preparations containing such enzymes, and the use of these enzymes for a number of industrial applications. BACKGROUND OF THE INVENTION Cellulases or cellulytic enzymes are enzymes involved in hydrolyses of cellulose. In the hydrolysis of native cel¬ lulose, it is known that there are three major types of cellulase enzymes involved, namely cellobiohydrolase (l,4-3-D-glucan cellobiohydrolase, EC 3.2.1.91), endo-/3- 1,4-glucanase (endo-l,4-3-D-glucan 4-glucanohydrolase, EC 3.2.1.4) and 3-glucosidase (EC 3.2.1.21). Cellulases are synthesized by a large number of microor- ganisms which include fungi, actinomycetes, myxobacteria and true bacteria but also by plants. Especially endoglucanases of a wide variety of specificities have been identified. A very important industrial use of cellulytic enzymes is the use for treatment of cellulosic textile or fabric, e.g. as ingredients in detergent compositions or fabric softener compositions, for bio-polishing of new fabric (garment finishing) , and for obtaining a "stone-washed" look of cellulose-containing fabric, especially denim, and several methods for such treatment have been sug- gested, e.g. in GB-A-1 368 599, EP-A-0 307 564 and EP-A-0 435 876, WO 91/17243, WO 91/10732, WO 91/17244, PCT/DK95/000108 and PCT/DK95/00132. Another important industrial use of cellulytic enzymes is the use for treatment of paper pulp, e.g. for improving the drainage or for deinking of recycled paper. Especially the endoglucanases (EC No. 3.2.1.4) constitute an interesting group of hydrolases for the mentioned industrial uses. Endoglucanases catalyses endo hydrolysis of l,4-3-D-glycosidic linkages in cellulose, cellulose derivatives (such as carboxy methyl cellulose and hydroxy ethyl cellulose), lichenin, 0-1,4 bonds in mixed j8-l,3 glucans such as cereal 3-D-glucans or xyloglucans and other plant material containing cellulosic parts. The authorized name is endo-l,4-j8-D-glucan 4-glucano hydrolase, but the abbreviated term endoglucanase is used in the present specification. Reference can be made to T.-M. Enveri, "Microbial Cellulases" in W.M. Fogarty, Microbial Enzymes and Biotechnology, Applied Science Pub¬ lishers, p. 183-224 (1983); Methods in Enzymology, (1988) Vol. 160, p. 200-391 (edited by Wood, W.A. and Kellogg, S.T.); Beguin, P., "Molecular Biology of Cellulose Degra¬ dation", Annu. Rev. Microbiol. (1990), Vol. 44, pp. 219- 248; Beguin, P. and Aubert, J-P., "The biological degra¬ dation of cellulose", FEMS Microbiology Reviews .13. (1994) p.25-58; Henrissat, B. , "Cellulases and their interaction with cellulose". Cellulose (1994), Vol. 1, pp. 169-196. Fungal endoglucanases have been described in numerous publications, especially those derived from species as e.g. Fusarium oxysporum , Trichoderma reesei , Trichoderma longibrachiatum , Aspergillus aculeatus , Neocallimastix patriciarum , and e.g. from species of the genera Piromyces, Humicola, Myceliophthora, Geotricum, Penicillium, Irpex. Coprinus . For example, fungal endoglucanases have been described by Sheppard, P.O., et al. , "The use of conserved cellulase family-specific sequences to clone Cellulase ho ologue cDNAs from Fusarium oxysporum, Gene, (1994), Vol. 15, pp. 163-167, Saloheimo, A., et al., "A novel, small endoglucanase gene, egI5 , from Trichoderma reesei iso¬ lated by expression in yeast". Molecular Microbiology (1994), Vol. 13(2), pp. 219-228; van Arsdell, J.N. et al, (1987) , Cloning, characterization, and expression in Saccharomyces cerevisiae of endoglucanase I from Trichoderma reesei , Bio/Technology 5: 60-64; Penttila, M. et al., (1986), "Homology between cellulase genes of Trichoderma reesei : complete nucleotide sequence of the endoglucanase I gene", Gene 45:253-263; Saloheimo, M. et al, (1988) , "EGIII, a new endoglucanase from Trichoderma reesei : the characterization of both gene and enzyme", Gene 63:11-21; Gonzales, R. , et al., "Cloning, sequence analysis and yeast expression of the egll gene from Trichoderma longibrachiatum", Appl. Microbiol. Biotechnol., (1992), Vol. 38, pp. 370-375; Ooi, T. et al. "Cloning and sequence analysis of a cDNA for cellulase (FI-CMCase) from Aspergillus aculeatus" , Curr. Genet., (1990), Vol. 18, pp. 217-222; Ooi, T. et al, "Complete nucleotide sequence of a gene coding for Aspergillus aculeatus cellulase (FI-CMCase)", Nucleic Acids Research, (1990), Vol. 18, No. 19, p. 5884; Xue, G. et al. , "Clon¬ ing and expression of multiple cellulase cDNAs from the anaerobic rumen fungus Neocallimastix patriciarum in E. coli" , J. Gen. Microbiol., (1992), Vol. 138, pp. 1413- 1420; Xue, G. et al., "A novel polysaccharide hydrolase cDNA (celD) from Neocallimastix patriciarum encoding three multi-functional catalytical domains with high endoglucanase, cellobiohydrolase and xylanase activ¬ ities", J. Gen. Microbiol., (1992), Vol. 138, pp. 2397- 2403; Zhou, L. et al. , "Intronless celB from the anaerobic fungus Neocallimastix patriciarum encodes a modular family A endoglucanase", Biochem. J. , (1994), Vol. 297, pp. 359-364; Dalbøge, H. and Heldt-Hansen, H.P., "A novel method for efficient expression cloning of fungal enzyme genes", Mol. Gen. Genet., (1994), Vol. 243, pp. 253-260; Ali, B.R.S. et al., "Cellulases and hemicellulases of the anaerobic fungus Piromyces consti¬ tute a multiprotein cellulose-binding complex and are encoded by multigene families", FEMS Microbiol. Lett., (1995), Vol. 125, No. 1, pp. 15-21. Further, the DNA Data Bank of Japan (DDBJ database publicly available at Internet) comprises two DNA sequences cloned from Penicillium janthinellum encoding endoglucanases (cloned by A. Koch and G. Mernitz, respectively) and a DNA sequence cloned from Humicola grisea var. thermoidea encoding an endoglucanase (cloned by T. Uozumi) . Two endoglucanases from Macrophomina phaseolina have been cloned and sequenced, see Wang, H.Y. and Jones, R.W. : "Cloning, characterization and functional expression of an endoglucanase-encoding gene from the phytopathogenic fungus Macrophomina phaseolina" in Gene, 158:125-128, 1995, and Wang, H.Y. and Jones, R.W. : "A unique endoglucanase-encoding gene cloned from the phytopathogenic fungus Macrophomina phaseolina" in Applied And Environmental Microbiology, 61:2004-2006, 1995. One of these endoglucanases shows high homology to the egl3 endoglucanase from the fungus Trichoderma reesei , the other shows homology to the egll from the microbial phytopathogen Pseudomonas solanacearum indicat¬ ing that both endoglucanases belong to family 5 of glycosyl hydrolases (B. Henrissat, Biochem J 280:309-316 (1991)). Filament-specific expression of a cellulase gene in the dimorphic fungus Ustilago maydis is disclosed in Schauwecker, F. et al. (1995). WO 91/17243 (Novo Nordisk A/S) discloses a cellulase pre¬ paration consisting of a homogenous endoglucanase compo¬ nent immunoreactive with an antibody raised against a highly purified 43 kDa endoglucanase derived from Humicola insolens , DSM 1800; WO 91/17244 (Novo Nordisk A/S) discloses a new (hemi)cellulose degrading enzyme, such as an endoglucanase, a cellobiohydrolase or a β- glucosidase, which may be derived from fungi other than Trichoderma and Phanerochaete; WO 93/20193 discloses an endoglucanase derivable from Aspergillus aculeatus ; WO 94/21801 (Genencor Inc.) concerns a cellulase system iso¬ lated from Trichoderma longibrachiatum exhibiting endoglucanase activity; WO 94/26880 (Gist Brocades N.V.) discloses an isolated mixture of cellulose degrading enzymes, which preferable are obtained from Trichoderma , Aspergillus or Disporotrichum, comprising endoglucanase, cellobiohydrolase, and xyloglucanase activity; and WO 95/02043 (Novo Nordisk A/S) describes an enzyme with endoglucanase activity derived from Trichoderma harzianum , which can be used for a number of purposes including e . g . degradation or modification of plant cell walls. It is also known that cellulases may or may not have a cellulose binding domain (a CBD) . The CBD enhances the binding of the enzyme to a cellulose-containing fiber and increases the efficacy of the catalytic active part of the enzyme. There is an ever existing need for providing novel cellulase enzyme preparations which may be used for applications where cellulase, preferably an endoglucanase, activity is desirable. The object of the present invention is to provide novel enzyme preparations having substantial cellulytic activ¬ ity at acid, neutral or alkaline conditions and improved performance in paper pulp processing, textile treatment, laundry processes or in animal feed; preferably novel cellulases, more preferably we11-performing endoglucana¬ ses, which are contemplated to be producible or produced by recombinant techniques. SUMMARY OF THE INVENTION Surprisingly, it has been found that a group of endoglucanases having certain unique characteristics per¬ form very good in those industrial applications for which endoglucanases are conventionally used. These unique characteristics can be described in terms of conserved regions of the amino acid sequence of the enzyme protein and the inventors have found that cellulytic enzymes, i.e. enzymes exhibiting cellulytic activity, having cer¬ tain conserved regions are very effective e.g. in the treatment of laundry, in the treatment of newly manufac- tured textile, in the treatment of papermaking pulp. Accordingly, in its first aspect the present invention relates to an enzyme preparation consisting essentially of an enzyme having cellulytic activity and comprising a first amino acid sequence consisting of 14 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp Xaa 1 2 3 4 5 6 7 8 9 10 11 12 13 14 and a second amino acid sequence consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, 12 and 14, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues with the provisos that, in the first amino acid sequence, (i) when the amino residue in position 12 is Ser, then the amino acid residue in position 14 is not Ser, and (ii) when the amino residue in position 12 is Gly, then the amino acid residue in position 14 is not Ala. This surprising finding of clearly recognisable conserved regions, in spite of rather prominent variations found within well-performing endoglucanase enzymes, is a result of studies of a number of fungal DNA sequences encoding for specific amino acid sequences of enzymes having sig¬ nificant cellulytic, especially endoglucanase, activ¬ ities. Based on this finding, a novel molecular method taylored to screen specifically for genomic DNA or cDNA characterised by encoding the enzymes of the invention has been developed. As tools for this three sets of degenerated primers were constructed. Accordingly, in its second aspect, the invention relates to a method for providing a gene encoding for cellulytic enzymes having the above conserved regions. By using this method, i.e. the set of primers for a PCR screening on genomic DNA, it was surprisingly found that DNA encoding for said enzymes can be found from a broad range of fungi, belonging to taxonomically very different organisms and inhabiting ecologically very different niches. Further, by using this method it has been possible to find DNA sequences encoding for the core regions (cata- lytically active regions or domains) of said enzymes without any attached cellulose binding domain (CBD) which core regions of enzymes would not have been selected by using conventional performance based screening approaches. The inventors have verified experimentally that the linking of a CBD region to a core region enzyme (comprising the catalytically active region or domain of the enzyme) of the present invention results in a sig¬ nificantly improved performance, e.g. a fifty times higher performance, of the multiple domain enzyme. Accordingly, the present invention provides novel cellulases, especially endoglucanases, having improved performance in industial applications, either in their native form, or homo- or heterologously produced. In further aspects, the present invention relates to novel cellulytic enzyme preparations which are derivable from taxonomically specific phyli, classes, orders, families, genera, and species; e.g. from Basidiomycotous Hymenomycetes , Zygomycota, Chytridiomycota ; or from the classes Discomycetes, Loculoascomycetes. Plectomyceteε; Archaeascomycetes , Hernias corny cetes or from the orders Di- aportaleε, Xylariales, Trichosphaeriales, Phyllachorales ; or from the families Nectriaeae, Sordariaceae. Chaetomiaceae , Ceratostomaceae, Lasiosphaeriaceae ; or from the genera Cylindrocarpon, Gliocladium, Volutella, Scytalidium, Acremonium , or from the species Fusarium lycopersici , Fusarium passiflora, Fusarium solani, Fusarium anguioides, Fusarium poae, Humicola nigrescens , Humicola grisea , especially such consisting essentially of an enzyme comprising an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. More specifically, the enzyme preparation of the invention is preferably obtainable from the taxonomically specific phyli, classes, orders, families, genera, and species mentioned above which all produce endoglucanases comprising a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. In yet further aspects, the present invention provides DNA constructs comprising a DNA sequence encoding an en¬ zyme exhibiting endoglucanase activity, which DNA sequence comprises the DNA sequence shown in SEQ ID Nos. 1, 4, 6, 8, 10, 12, 16, and 19, respectively, or analogues thereof. The present invention also relates to a recombinant expression vector comprising a DNA construct of the invention; to a cell comprising a DNA construct or a recombinant expression vector of the invention; to a method of producing an enzyme, e.g a recombinant enzyme, of the invention; to a method of providing colour clari- fication of laundry by using the enzyme of the invention; to a laundry composition comprising the enzyme of the invention; to uses of the enzyme of the invention for degradation or modification of plant material, e.g. cell walls, for treatment of fabric, textile or garment, for treatment of paper pulp; and to an enzyme preparation which is enriched in an enzyme of the present invention. THE DRAWINGS Figure 1 is an alignment of the deduced encoded amino acid sequences of Acrejπoniujπ sp. (I) , Volutella colletotrichoides , Crinipellis scabella, Acremonium sp. (II) , Myceliophthora thermophila, Thielavia terrestris, Macrophomina phaseolina . The Pileup program (Feng and Doolittle, 1987) (GCG package, version 8.0) was used to create the best alignment. Identical residues in at least four sequences (boxed) are indicated around the corre¬ sponding amino acids. Figure 2 Figure 2a,b,c illustrates the taxonomic classification within the Fungal Kingdom of all the microorganisms dis¬ closed herein as being capable of producing said enzyme preparations and enzymes of the invention. The taxonomic classification used herein builds primarily on the system used in the :NIH Data Base (Entrez, version spring 1996) available on World Wide Web: (http://www3.ncbi.nlm.nih.gov/htbin/ef/entrezTAX) . Regarding classification of organisms which are not included in the Entrez data base the following generally available and world wide accepted reference books have been used: For Ascomyceteε : Eriksson, O.E. & Hawksworth, D.L.: Systema Ascomycetum vol 12 (1993) . For Basidiomycetes: Jϋlich, W. : Higher Taxa of Basidiomycetes, Bibliotheca Mycologia 85, 485pp (1981) . For Zygo ycetes : O'Donnell, K. : Zygomycetes in culture. University of Georgia, US, 257pp (1979) . General mycological reference books : Hawksworth, D.L., Kirk, P.M., Sutton, B.C. and Pegler, D.N. : Dictionary of the fungi. International Mycological Institute, 616pp (1995) ; Von Arx, J.A. : The genera of fungi sporulating in culture, 424pp (1981). The taxonomic implacement of the genus Humicola has untill recently remained unclear. However, studies of 18SRNA of a wide selection of Sordariales has given strong indications of referring Humicola to the order Sordariales (Taylor, Clausen & Oxenbøll, unpublished) . Further these data suggests Humicola along with Scytalid- ium to be only rather distantly related to the families Sordariaceae, Chaetomiaceae, Ceratostomataceae, and Lasiosphaeriaceae. In accordance with the above Humicola and Scytalidium are here placed within the order Sordariales, with unclassified Family. Figure 3 is an alignment of the deduced partial amino acid sequences derived from a selection of 26 of the 46 microorganisms described in Example 5. DETAILED DESCRIPTION OF THE INVENTION In the present context, the term "the 20 naturally occuring amino acid residues" denotes the 20 amino acid residues usually found in proteins and conventionally known as alanine (Ala or A) , valine (Val or V) , leucine (Leu or L) , isoleucine (lie or I), proline (Pro or P) , phenylalanine (Phe or F) , tryptophan (Trp or W) , methionine (Met or M) , glycine (Gly or G) , serine (Ser or S) , threonine (Thr or T) , cysteine (Cys or C) , tyrosine (Tyr or Y) , asparagine (Asn or N) , glutamine (Gin or Q) , aspartic acid (Asp or D) , glutamic acid (Glu or E) , lysine (Lys or K) , arginine (Arg or R) , and histidine (His or H) . According to the present invention there is provided novel well-performing endoglucanases comprising conserved amino acid sequence regions, especially a first amino acid sequence consisting of 14 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp Xaa 1 2 3 4 5 6 7 8 9 10 11 12 13 14 and a second amino acid sequence consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, 12 and 14, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues with the provisos that, in the first amino acid sequence, (i) when the amino residue in position 12 is Ser, then the amino acid residue in position 14 is not Ser, and (ii) when the amino residue in position 12 is Gly, then the amino acid residue in position 14 is not Ala. Preferably, the enzyme of the invention is of microbial origin, i.e. obtainable from a microorganism such as a fungus. In a preferred embodiment, the amino acid residue in position 9 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group consisting of proline and threonine. In another preferred embodiment, the amino acid residue in position 10 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably serine. In yet another preferred embodiment, the amino acid resi- due in position 12 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cy¬ steine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group con- sisting of alanine and glycine. In yet another preferred embodiment, the amino acid resi- due in position 14 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cy¬ steine, asparagine, glutamine, tyrosine, serine, methionine, tryptophan, glutamic acid and aspartic acid, preferably from the group consisting of proline, threonine, serine, alanine, glutamic acid and aspartic acid. Preferably, the amino acid residue in position 4 of the second sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine, tryptophan, glutamic acid and aspartic acid, more preferably from the group con¬ sisting of alanine, glycine, and glutamine. Examples of more preferred embodiments are such wherein, in the first sequence, the amino acid residue in position 3 is tyrosine; or the amino acid residue in position 4 is tryptophan; or the amino acid residue in position 8 is lysine. In an especially preferred embodiment, the enzyme of the invention has a first sequence comprising the amino acid sequence Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Ala Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 , or the amino acid sequence Thr Arg Tyr Trp Asp Cys Cys Lys Thr Ser Cys Ala Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 , or the amino acid sequence Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Gly Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 . In a second aspect, the present invention provides a method for finding and cloning of such an enzyme which encoding such an enzyme which method comprises hybridization, e.g. PCR amplification, under standard conditions with an oligonucleotide derived from any of the conserved regions, illustrated in Fig.l. A useful oligonucleotide comprises a nucleotide sequence encoding at least a pentapeptide comprised in a peptide selected from the group consisting of a. Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp Xaa 1 2 3 4 5 6 7 8 9 10 11 12 13 14 the amino acid in position 3 or 4 being Trp, Tyr or Phe; the amino acid in postion 8 being Arg, Lys or His; he amino acid in position 9, 10, 12 and 14, respectively, being any of the 20 naturally occurring amino acid resi¬ dues ; and b. Trp Cys Cys Xaa Cys Tyr 1 2 3 4 5 6 the amino acid in position 4 being any of the 20 natural¬ ly occurring amino acid residues ; and c. Xaa Pro Gly Gly Gly Xaa Gly Xaa Phe 1 2 3 4 5 6 7 8 9 the amino acid in position 1 being Met or lie; the amino acid in position 6 and 8, respectively, being Leu, lie or Val; and d. Gly Cys Xaa Xaa Arg Xaa Asp Trp Xaa 1 2 3 4 5 6 7 8 9 the amino acid in position 3 being any of the 20 natural¬ ly occurring amino acid residues; the amino acid in position 4 and 6, respectively, being Trp, Tyr or Phe; and the amino acid in position 9 being Phe or Met; The useful oligonucleotides also comprises nucleotide sequences complementary to the sequences mentioned. In a preferred embodiment of the method of the invention, the oligonucleotide corresponds to a PCR primer selected from the PCR primers sense: 5'-CCCCAAGCTTACI A / c GITA c / τ TGGGA c / τ TG c / τ TG c / τ AA A / α A / c C-3' antisense 1: 5'- CTAGTCTAGATA A / 0 CAIGC A / G CA A / 0 CACC -3' ; antisense 2: CTAGTCTAGAAAIA A /o/ τ ICCIA A / c /°ICCICCICCIGG -3' ; and antisense 3: 5 ' - CTAGTCTAGAIAACCA A / 0 TCA A / G A / T AIC°/ T CC-3 . In a third aspect, the present invention provides an enzyme preparation which essentially consists of an enzyme having cellulytic activity and having the conserved regions found by the inventors, i.e. which com¬ prises a peptide consisting of 7 amino acid residues ha- ving the following sequence Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. This enzyme is obtainable from a strain belonging to Basidiomycotous Hymenomycetes (see Fig.2 ) , more preferably to the group consisting of the orders Agarica- les, Auriculariales, and Aphyllophorales, even more preferably to the group consisting of the families Exidiaceae, Tricholomataceae, Coprinaceae, Schizophyllaceae, Bjerkanderaceae and Polyporaceae , especially to the group consisting of the genera Exidia, Crinipellis, Fomes, Panaeolus, Trameteε, Schizophyllum, and Spongipellis . Specific examples are endoglucanases obtainable from a strain belonging to the group consisting of the species Exidia glandulosa, Crinipellis scabella, Fomeε fomentarius, and Spongipellis sp. , more specific examples being Exidia glandulosa, CBS 277.96, Crinipellis scabella, CBS 280.96, Fomes fomentarius, CBS 276.96, and Spongipellis sp. , CBS 283.96. Exidia glandulosa was deposited at Centraalbureau voor Schimmelcultures, Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands, on 12 March, 1996, under the deposition number CBS 277.96; Crinipellis scabella was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 280.96, Fomeε fomentariuε was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 276.96, and Spongipellis sp. was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 283.96; all deposited under the Budapest Treaty. The enzyme preparation of the invention is also obtain¬ able from a strain belonging to Chytridiomycota, preferably from a strain belonging to the class of Chytridiomyceteε , more preferably belonging to the group consisting of the order Spizellomycetaleε , even more preferably to the family Spizellomycetaceae , especially belonging to the genus Rhizophlyctiε . A specific example is a strain belonging to the species Rhizophlyctiε rosea , more specifically to Rhizophlyctiε roεea , CBS 282.96. Rhizophlyctiε rosea was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 282.96; under the Budapest Treaty. The enzyme preparation of the invention is also obtain¬ able from a strain belonging to Zygomycota , preferably belonging to the class Zygomycetes , more preferably to the order Mucorales , even more preferably to the group of families consisting of Mucoraceae and Thamnidiaceae , especially belonging to the group consisting of the ge¬ nera Rhizomucor, Phycomyces and Chaetostylum . Specific examples are strains belonging to the genera Rhizomucor pusillus, Phycomyces nitens , and Chaetostylum fresenii more specifically to Rhizomucor pusillus, IFO 4578, and Phycomyces nitens , IFO 4814 and Chaetostylum fresenii , NRRL 2305. Further, the enzyme preparation of the invention is also obtainable from a strain belonging to the group consist¬ ing of Ar chaeas corny cetes, Discomyceteε , Hemiascomycetes , Loculoascomycetes , and Plectomyceteε , preferably belonging to the group consisting of the orders Pezizales, Rhytismataleε, Dothidealeε, and Eurotialeε . Especially, the enzyme is obtainable from a strain belonging the the group consisting of the families Cucurbitariaceae , Ascobolaceae, Rhytismataceae, and Trichocomaceae, preferably belonging the the group con¬ sisting of the genera Diplodia, Microsphaeropsiε , Ulospora, Macrophomina, Ascobolus, Saccoboluε, Penicil- lium, and Thermomyces . Specific examples are enzymes obtainable from a strain belonging the the group consist- ing of the species Diplodia gossypina, Microsphaeropεis sp. , Ulospora bilgramii, Aureobasidium εp . , Macrophomina phaseolina, Ascobolus stictoideε, Saccoboluε dilutelluε, Peziza, Penicillium verruculoεum, Penicillium chryεogenum, and Thermomyceε verrucosuε; more specifically Diplodia goεεypina, CBS 274 .96, Ulospora bilgramii, NKBC 1444, Macrophomina phaεeolina, CBS 281 .96, Saccoboluε dilutellus, CBS 275.96, Penicillium verruculosum, ATCC 62396, Penicillium chrysogenum, ATCC 9480, and Thermomyces verrucosus , CBS 285.96. Diplodia gossypina was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 274.96, Macrophomina phaseolina was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 281.96, Saccoboluε dilutelluε was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 275.96; Thermomyceε verrucosus was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 285.96; all under the Budapest Treaty. Yet further, the enzyme is obtainable from a strain belonging to the group consisting of the orders Dia- portales, Xylariales, Trichosphaeriales and Phyllachorales, preferably from a strain belonging to the group consisting of the families Xylariaceae, Valεaceae, and Phyllachoraceae , more preferably belonging to the ge¬ nera Diaporthe, Colletotrichum, Nigroεpora, Xylaria, Nodulisporum and Poronia . Specific examples are the species Diaporthe syngeneεia, Colletotrichum lagenarium, Xylaria hypoxylon, Nigroεpora εp. , Nodulisporum sp . , and Poronia punctata, more specifically Diaporthe syngeneεia, CBS 278.96, Colletotrichum lagenarium, ATCC 52609, Nigroεpora εp. , CBS 272 .96, Xylaria hypoxylon, CBS 284 .96. Diaporthe εyngeneεia was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 278.96, Nigroεpora εp. was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 272.96, Xylaria hypoxylon was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 284.96; all under the Budapest Treaty. The enzyme is also obtainable from the unidentified fungal, mitosporic, coleomycetous deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition numbers CBS 270.96, CBS 271.96 and CBS 273.96, respectively, under the Budapest Treaty. The enzyme is also obtainable from a strain belonging to the group consisting of the genera Cylindrocarpon, Gliocladium, Nectria, Volutella, Sordaria, Scytalidium, Thielavia, Syspastospora, Cladorrhinum, Chaetomium, Myce- liphthora and Acremonium, especially from a strain belon¬ ging to the group consisting of the species Cylin- drocarpon sp. , Nectria pinea, Volutella colletotrichoides, Sordaria fimicola, Sordaria macrospora, Thielavia terrestris, Thielavia thermophila, Syspastospora boninensis, Cladorrhinum foecundiεεimum, Chaetomium murorum, Chaetomium vireεcenε, Chaetomium brasiliensis, Chaetomium cunicolorum, Myceliophthora thermophila, Gliocladium catenulatum, Scytalidium thermophila, and Acremonium sp. , more specifically from Nectria pinea, CBS 279.96, Volutella colletotrichoideε, CBS 400 .58, Sordaria fimicola, ATCC 52644, Sordaria macrospora, ATCC 60255, Thielavia terrestriε, NRRL 8126, Thielavia thermophila, CCBS 174 .70, Chaetomium murorum, CBS 163 .52, Chaetomium vireεcenε, CBS 547. 75, Chaetomium brasiliensis, CBS 122 .65, Chaetomium cunicolorum, CBS 799.83 , Syspastospora boninensis, NKBC 1515, Cladorrhinum foecundisεimum, ATCC 62373, Myceliophthora thermophila, CBS 117.65, Scytalidium thermophila, ATCC 28085, Gliocladium catenulatum, ATCC 10523, and Acremonium εp . , CBS 478.94. Nectria pinea was deposited at Centraalbureau voor Schimmelcultures on 12 March, 1996, under the deposition number CBS 279.96, and Acremonium εp. was deposited in 28 September 1994 under the deposition number CBS 478.94, both according to the Budapest Treaty. The enzyme is also obtainable from a strain belonging to the group consisting of the species Fusarium solani, Fusarium anguioides, Fusarium poae , Fusarium oxysporum ssp. lycopersici, Fusarium oxysporum ssp. passiflora, Humicola nigrescens and Humicola grisea , especially Fusarium oxysporum ssp lycopersici, CBS 645.78, Fusarium oxysporum ssp passiflora, CBS 744 . 79, Fusarium solani, IMI 107.511, Fusarium anguioides, IFO 4467, Fusarium poae, ATCC 60883, Humicola nigrescenε , CBS 819.73 and Humicola grisea , ATCC 22726. It is to be noted that Humi¬ cola grisea is different from Humicola grisea var. thermoidea . In a preferred embodiment, the enzyme preparation of the invention is derived from the disclosed classes, orders, families, genera and species and essentially consists of an enzyme comprising a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. Preferably, the amino acid residue in position 9 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, more preferably from the group consisting of proline and threonine; the amino acid residue in position 10 of the first sequence which is selected from the group consist¬ ing of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably serine; the amino acid residue in position 12 of the first sequence is selected from the group consist¬ ing of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group consisting of alanine and glycine; and the amino acid residue in position 4 of the second sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine, tryptophan, glutamic acid and aspartic acid, more preferably from the group con¬ sisting of alanine, glycine, and glutamine. In further aspects, the present invention provides a DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SE ID No. 1, 4, 6, 8, 10, 12, 16, or 19, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyces cereviεiae DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia COli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively; or b) an analogue of the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16, or 19, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 9770, DSM 10082, DSM 10080, DSM 10081, Escherichia COli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively, which i) is homologous with the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16, or 19, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia coli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively, ii) hybridizes with the same oligonucleotide probe as the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16, or 19, respectively, or the DNA sequ¬ ence obtainable from the plasmid in Saccharomyceε cerevisiae DSM 9770, DSM 10082, DSM 10080, DSM 10081, Escherichia coli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively, iii) encodes a polypeptide which is homologous with the polypeptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16, or 19, respectively, or the DNA sequ¬ ence obtainable from the plasmid in Saccharomyces cerevisiae DSM 9770, DSM 10082, DSM 10080, DSM 10081, Escherichia coli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively, iv) encodes a polypeptide which is immunologically re¬ active with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 1, 4, 6, 8, 10, 12, 16, or 19, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyceε cereviεiae DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia coli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively. Escherichia coli DSM 10512 was deposited under the Buda- pest Treaty on 2 February, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10511 was deposited under the Buda- pest Treaty on 2 February, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10571 was deposited under the Buda- pest Treaty on 6 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10576 was deposited under the Buda- pest Treaty on 12 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10583 was deposited under the Buda- pest Treaty on 13 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10584 was deposited under the Buda- pest Treaty on 13 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany). Escherichia coli DSM 10585 was deposited under the Buda- pest Treaty on 13 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10586 was deposited under the Buda¬ pest Treaty on 13 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10587 was deposited under the Buda¬ pest Treaty on 13 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Escherichia coli DSM 10588 was deposited under the Buda¬ pest Treaty on 13 March, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Saccharomyces cerevisiae DSM 9770 was deposited under the Budapest Treaty on 24 February, 1995, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Saccharomyces cerevisiae DSM 10082 was deposited under the Budapest Treaty on 30 June, 1995, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Saccharomyces cerevisiae DSM 10080 was deposited under the Budapest Treaty on 30 June, 1995, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . Saccharomyces cerevisiae DSM 10081 was deposited under the Budapest Treaty on 30 June, 1995, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) . The DNA construct of the invention relating to SEQ ID No. 1 can be isolated from or produced on the basis of a DNA library of a strain of Myceliophthora, in particular a strain of M. thermophila , especially M. thermophila , CBS 117.65. The DNA constructs of the invention relating to SEQ ID Nos. 4 and 6 can be isolated from or produced on the basis of a DNA library of a strain of Acremonium, especially Acremonium sp. , CBS 478.94. The DNA construct of the invention relating to SEQ ID No. 8 can be isolated from or produced on the basis of a DNA library of a strain of Thielavia in particular a strain of Thielavia terrestris, especially Thielavia terrestris, NRRL 8126. The DNA construct of the invention relating to SEQ ID No. 10 can be isolated from or produced on the basis of a DNA library of a strain of Macrophomina, in particular a strain of M. phaseolina, especially M . phaseolina , CBS 281.96. The DNA construct of the invention relating to SEQ ID No. 12 can be isolated from or produced on the basis of a DNA library of a strain of Crinipellis, in particular a strain of C. scabella , especially C. scabella , CBS 280.96. The DNA construct of the invention relating to SEQ ID No. 19 can be isolated from or produced on the basis of a DNA library of a strain of Sordaria, in particular a strain of Sordaria fimicola . In the present context, the "analogue" of the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16 or 19, respectively, is intended to indicate any DNA sequence encoding an enzyme exhibiting endoglucanase activity, which has any or all of the properties i)-iv). The analogous DNA sequence a) may be isolated from another or related (e.g. the same) organism producing the enzyme with endoglucanase activity on the basis of the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16 or 19, respectively, e.g. using the procedures described herein; the homologue may be an allelic variant of the DNA sequence comprising the DNA sequences shown herein, i.e. an alternative form of a gene that arises through mutation; mutations can be silent (no change in the encoded enzyme) or may encode enzymes having altered amino acid sequence; the homologue of the present DNA sequence may also be a genus or spe¬ cies homologue, i.e. encoding an enzyme with a similar activity derived from another species, b) may be constructed on the basis of the DNA sequences Shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16 or 19, respectively, e.g. by introduction of nucleotide substitutions which do not give rise to another amino acid sequence of the endoglucanase encoded by the DNA sequence, but which correspond to the codon usage of the host organism intended for production of the enzyme, or by introduction of nucleotide substitutions which may give rise to a different amino acid sequence. However, in the latter case amino acid changes are preferably of a minor nature, that is conservative amino acid substitu¬ tions that do not significantly affect the folding or activity of the protein, small deletions, typically of one to about 30 amino acids; small amino- or carboxyl- terminal extensions, such as an amino-terminal methionine residue, a small linker peptide of up to about 20-25 residues, or a small extension that facilitates purifica¬ tion, such as a poly-histidine tract, an antigenic epitope or a binding domain. See in general Ford et al., Protein Expression and Purification 2 : 95-107, 1991. Examples of conservative substitutions are within the group of basic amino acids (such as arginine, lysine, histidine) , acidic amino acids (such as glutamic acid and aspartic acid) , polar amino acids (such as glutamine and asparagine) , hydrophobic amino acids (such as leucine, isoleucine, valine) , aromatic amino acids (such as phenylalanine, tryptophan, tyrosine) and small amino acids (such as glycine, alanine, serine, threonine, methionine) . It will be apparent to persons skilled in the art that such substitutions can be made outside the regions criti¬ cal to the function of the molecule and still result in an active polypeptide. Amino acids essential to the activity of the polypeptide encoded by the DNA construct of the invention, and therefore preferably not subject to substitution, may be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, Science 244. 1081-1085, 1989). In the latter technique mutations are introduced at every residue in the mol¬ ecule, and the resultant mutant molecules are tested for biological (i.e. endoglucanase) activity to identify amino acid residues that are critical to the activity of the molecule. Sites of substrate-enzyme interaction can also be determined by analysis of crystal structure as determined by such techniques as nuclear magnetic reson¬ ance, crystallography or photoaffinity labeling. See, for example, de Vos et al., Science 255: 306-312, 1992; Smith et al., J. Mol. Biol. 224: 899-904, 1992; Wlodaver et al., FEBS Lett. 309: 59-64, 1992. The endoglucanase encoded by the DNA sequence of the DNA construct of the invention may comprise a cellulose bind¬ ing domain (CBD) existing as an integral part of the encoded enzyme, or a CBD from another origin may be introduced into the endoglucanase enzyme thus creating an enzyme hybride. In this context, the term "cellulose- binding domain" is intended to be understood as defined by Peter Tomme et al. "Cellulose-Binding Domains: Classi¬ fication and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Michael H. Penner (Eds.), ACS Symposium Series, No. 618, 1996. This definition classifies more than 120 cellulose-binding domains (CBDs) into 10 families (I-X) , and it demon¬ strates that CBDs are found in various enzymes such as cellulases, xylanases, mannanases, arabinofuranosidases, acetyl esterases and chitinases. CBDs have also been found in algae, e.g., the red alga Porphyra purpurea as a non-hydrolytic polysaccharide-binding protein, for refer¬ ence see Peter Tomme et al., supra. However, most of the CBDs are from cellulases and xylanases. CBDs are found at the N or C termini of proteins or are internal. Enzyme hybrids are known in the art, see e.g. WO 90/00609 and WO 95/16782, and may be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain ligated, with or without a linker, to a DNA sequence encoding the enzyme of interest and growing the host cell to express the fused gene. Enzyme hybrids may be described by the following formula: CBD - MR - X, wherein CBD is the N-terminal or the C-terminal region of an amino acid sequence corresponding to at least the cellulose-binding domain; MR is the middle region (the linker) , and may be a bond, or a short linking group preferably of from about 2 to about 100 carbon atoms, more preferably of from 2 to 40 carbon atoms; or is preferably from about 2 to about 100 amino acids, more preferably of from 2 to 40 amino acids; and X is an N- terminal or C-terminal region of a polypeptide encoded by the DNA sequence of the invention. The homology referred to in i) above is determined as the degree of identity between the two sequences indicating a derivation of the first sequence from the second. The homology may suitably be determined by means of computer programs known in the art such as GAP provided in the GCG program package (Needleman, S.B. and Wunsch, CD., Jour¬ nal of Molecular Biology, _UL: 443-453, 1970) . Using GAP with the following settings for DNA sequence comparison: GAP creation penalty of 5.0 and GAP extension penalty of 0.3, the coding region of the DNA sequence exhibits a degree of identity preferably of at least 60%, more preferably at least 65%, more preferably at least 70%, even more preferably at least 80%, especially at least 90%, with the coding region of the DNA sequence shown in SEQ ID No.l, 4, 6, 8, 10, 12, or 16, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, Escherichia COli , DSM 10512, DSM 10511, DSM 10571, or DSM 10576, respectively. The hybridization referred to in ii) above is intended to indicate that the analogous DNA sequence hybridizes to the same probe as the DNA sequence encoding the endoglucanase enzyme under certain specified conditions which are described in detail in the Materials and Methods section hereinafter. The oligonucleotide probe to be used is the DNA sequence corresponding to the endoglucanase encoding part of the DNA sequence shown in SEQ ID NO 1, 4, 6, 8, 10, 12, or 16 respectively, or the DNA sequence obtainable from the plasmid in Saccharomyceε cerevisiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia coli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively. The homology referred to in iii) above is determined as the degree of identity between the two sequences indicat¬ ing a derivation of the first sequence from the second. The homology may suitably be determined by means of com¬ puter programs known in the art such as GAP provided in the GCG program package (Needleman, S.B. and Wunsch, CD., Journal of Molecular Biology, 48.: 443-453, 1970). Using GAP with the following settings for polypeptide sequence comparison: GAP creation penalty of 3.0 and GAP extension penalty of 0.1, the polypeptide encoded by an analogous DNA sequence exhibits a degree of identity pre¬ ferably of at least 55%, more preferably at least 60%, more preferably at least 65%, even more preferably at least 70%, more preferably at least 80%, especially at least 90%, with the enzyme encoded by a DNA construct comprising the DNA sequence shown in SEQ ID No.l, 4, 6, 8, 10, 12, 16 or 19, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyceε cereviεiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia COli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively. In connection with property iv) above it is intended to indicate an endoglucanase encoded by a DNA sequence iso¬ lated from strain Saccharomyceε cereviεiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia coli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively, and produced in a host organism transformed with said DNA sequence or the corresponding endoglucanase naturally produced by Myceliophthora thermophila, Acremonium εp. , Thielavia terrestriε, Macrophomina phaεeolina, Crinipelliε scabella, Volutella colletotrichoideε , or Sordaria fimicola , respectively. The immunological reac¬ tivity may be determined by the method described in the Materials and Methods section below. In further aspects the invention relates to an expression vector harbouring a DNA construct of the invention, a cell comprising the DNA construct or expression vector and a method of producing an enzyme exhibiting endoglucanase activity which method comprises culturing said cell under conditions permitting the production of the enzyme, and recovering the enzyme from the culture. In a still further aspect the invention relates to an enzyme exhibiting endoglucanase activity, which enzyme a) is encoded by a DNA construct of the invention b) produced by the method of the invention, and/or c) is immunologically reactive with an antibody raised against a purified endoglucanase encoded by the DNA sequence shown in SEQ ID No.l, 4, 6, 8, 10, 12, or 16, respectively, or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, Escherichia coli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively. The endoglucanase mentioned in c) above may be encoded by the DNA sequence isolated from the strain Saccharomyces cerevisiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, Eεcherichia coli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively, and produced in a host organism transformed with said DNA sequence or the corresponding endoglucanase naturally produced by Myceliophthora thermophila, Acremonium sp. , Thielavia terrestriε, Macrophomina phaseolina, Crinipellis scabella, Volutella colletotrichoides or Sordaria fimicola , respectively. Generally, in the present context the term "enzyme" is understood to include a mature protein or a precursor form thereof as well to a functional fragment thereof which essentially has the activity of the full-length enzyme. Furthermore, the term "enzyme" is intended to include homologues of said enzyme. Homologues of the present enzyme may have one or more amino acid substitutions, deletions or additions. These changes are preferably of a minor nature, that is conser- vative amino acid substitutions that do not significantly affect the folding or activity of the protein, small deletions, typically of one to about 30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue, a small linker peptide of up to about 20-25 residues, or a small extension that facilitates purification, such as a poly-histidine tract, an antigenic epitope or a binding domain. See in general Ford et al. , Protein Expression and Purification 2.: 95- 107, 1991. Examples of conservative substitutions are within the group of basic amino acids (such as arginine, lysine, histidine) , acidic amino acids (such as glutamic acid and aspartic acid) , polar amino acids (such as glutamine and asparagine) , hydrophobic amino acids (such as leucine, isoleucine, valine) , aromatic amino acids (such as phenylalanine, tryptophan, tyrosine) and small amino acids (such as glycine, alanine, serine, threonine, methionine) . It will be apparent to persons skilled in the art that such substitutions can be made outside the regions criti¬ cal to the function of the molecule and still result in an active enzyme. Amino acids essential to the activity of the enzyme of the invention, and therefore preferably not subject to substitution, may be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham, 1989) . In the latter technique mutations are introduced at every residue in the molecule, and the resultant mutant molecules are tested for cellulytic activity to identify amino acid residues that are critical to the activity of the molecule. Sites of ligand-receptor interaction can also be determined by analysis of crystal structure as determined by such techniques as nuclear magnetic resonance, crystallography or photoaffinity labelling. See, for example, de Vos et al., 1992; Smith et al., 1992. Wlodaver et al., 1992. The homologue may be an allelic variant, i.e. an alterna¬ tive form of a gene that arises through mutation, or an altered enzyme encoded by the mutated gene, but having substantially the same activity as the enzyme of the invention. Hence mutations can be silent (no change in the encoded enzyme) or may encode enzymes having altered amino acid sequence. The homologue of the present enzyme may also be a genus or species homologue, i.e. an enzyme with a similar activity derived from another species. A homologue of the enzyme may be isolated by using the procedures described herein. Molecular screening and cloning by polymerase chain reaction fPCR) Molecular screening for DNA sequences of the invention may be carried out by polymerase chain reaction (PCR) using genomic DNA or double-stranded cDNA isolated from a suitable source, such as any of the herein mentioned organisms, and synthetic oligonucleotide primers prepared on the basis of the DNA sequences or the amino acid sequences disclosed herein. For instance, suitable oligonucleotide primers may be the primers described in the Materials and Methods section. In accordance with well-known procedures, the PCR fragment generated in the molecular screening may be isolated and subcloned into a suitable vector. The PCR fragment may be used for screening DNA libraries by e.g. colony or plaque hybridization. Expression cloning in veast The DNA sequence of the invention encoding an enzyme exhibiting endoglucanase activity may be isolated by a general method involving cloning, in suitable vectors, a DNA library from a suitable source, such as any of the herein mentioned organisms transforming suitable yeast host cells with said vectors, culturing the host cells under suitable conditions to express any enzyme of interest encoded by a clone in the DNA library, screening for positive clones by determining any endoglucanase activity of the enzyme produced by such clones, and isolating the enzyme encoding DNA from such clones. The general method is further disclosed in WO 94/14953 the contents of which are hereby incorporated by reference. A more detailed description of the screening method is given in Example 1 below. The DNA sequence coding for the enzyme may for instance be isolated by screening a cDNA library of Macrophomina phaseolina, Crinipellis scabella, Sordaria fimicola or Volutella colletotrichoides , and selecting for clones ex¬ pressing the appropriate enzyme activity (i.e. endoglucanase activity) or from Eεcherichia coli DSM 10512 deposited under the Budapest Treaty on 2 February, 1996, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) , or from Eεcherichia coli DSM 10511 deposited under the Budapest Treaty on 2 February, 1996, at DSM, or from Escherichia coli DSM 10576, deposited under the Budapest Treaty on 12 March, 1996, at DSM; or from Escherichia coli DSM 10571 deposited under the Budapest Treaty on 6 March, 1996, at DSM; or by screening a cDNA library of Myceliphthora thermophila, CBS 117.65, Acremonium sp. , CBS 478.94, or Thielavia terrestris , NRRL 8126, and selecting for clones expres¬ sing the appropriate enzyme activity (i.e. endoglucanase activity) or from Saccharomyces cerevisiae DSM 9770 deposited under the Budapest Treaty on 24 February, 1995, at DSM (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 16, D-38124 Braunschweig, Germany) , or from Saccharomyces cerevisiae DSM 10082 deposited under the Budapest Treaty on 30 June, 1995, at DSM, from Saccharomyceε cerevisiae DSM 10080 deposited under the Budapest Treaty on 30 June, 1995, or from Saccharomyces cereviεiae DSM 10081 deposited under the Budapest Treaty on 30 June, 1995, at DSM. The appropriate DNA sequence may then be isolated from the clone by standard procedures, e.g. as described in Example 1. Nucleic acid construct As used herein the term "nucleic acid construct" is intended to indicate any nucleic acid molecule of cDNA, genomic DNA, synthetic DNA or RNA origin. The term "construct" is intended to indicate a nucleic acid segment which may be single- or double-stranded, and which may be based on a complete or partial naturally occurring nucleotide sequence encoding an enzyme of interest. The construct may optionally contain other nucleic acid segments. The nucleic acid construct encoding the enzyme of the invention may suitably be of genomic or cDNA origin, for instance obtained by preparing a genomic or cDNA library and screening for DNA sequences coding for all or part of the enzyme by hybridization using synthetic oligonucleotide probes in accordance with standard techniques (cf. Sambrook et al., 1989). The nucleic acid construct encoding the enzyme may also be prepared synthetically by established standard methods, e.g. the phosphoa idite method described by Beaucage and Caruthers, (1981) , or the method described by Matthes et al., (1984). According to the phospho- amidite method, oligonucleotides are synthesized, e.g. in an automatic DNA synthesizer, purified, annealed, ligated and cloned in suitable vectors. Furthermore, the nucleic acid construct may be of mixed synthetic and genomic, mixed synthetic and cDNA or mixed genomic and cDNA origin prepared by ligating fragments of synthetic, genomic or cDNA origin (as appropriate) , the fragments corresponding to various parts of the entire nucleic acid construct, in accordance with standard tech- niques. The nucleic acid construct may also be prepared by polymerase chain reaction using specific primers, for instance as described in US 4,683,202 or Saiki et al., (1988). The nucleic acid construct is preferably a DNA construct which term will be used exclusively in this specification and claims. Recombinant vector A recombinant vector comprising a DNA construct encoding the enzyme of the invention may be any vector which may conveniently be subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which it is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated. The vector is preferably an expression vector in which the DNA sequence encoding the enzyme of the invention is operably linked to additional segments required for transcription of the DNA. In general, the expression vector is derived from plasmid or viral DNA, or may contain elements of both. The term, "operably linked" indicates that the segments are arranged so that they function in concert for their intended purposes, e.g. transcription initiates in a promoter and proceeds through the DNA sequence coding for the enzyme. The promoter may be any DNA sequence which shows transcriptional activity in the host cell of choice and may be derived from genes encoding proteins either homologous or heterologous to the host cell. Examples of suitable promoters for use in yeast host cells include promoters from yeast glycolytic genes (Hitzeman et al., J. Biol. Che . 255 (1980), 12073 - 12080; Alber and Kawasaki, J. Mol. Appl. Gen. (1982), 419 - 434) or alcohol dehydrogenase genes (Young et al., in Genetic Engineering of Microorganisms for Chemicals (Hollaender et al, eds.). Plenum Press, New York, 1982), or the TPI1 (US 4,599,311) or ADH2-4C (Russell et al., Nature 304 (1983), 652 - 654) promoters. Examples of suitable promoters for use in filamentous fungus host cells are, for instance, the ADH3 promoter (McKnight et al., The EMBO J. 4 (1985), 2093 - 2099) or the tpiA promoter. Examples of other useful promoters are those derived from the gene encoding A . oryzae TAKA amylase, Rhizomucor miehei aspartic proteinase, A. niger neutral α-amylase, A. niger acid stable α-amylase, A. niger or A. aw amor i glucoamylase (gluA) , Rhizomucor miehei lipase, A. oryzae alkaline protease, A. oryzae triose phosphate isomerase or A. nidulanε acetamidase. Preferred are the TAKA-amylase and gluA promoters. Examples of suitable promoters for use in bacterial host cells include the promoter of the Bacilluε stearothermophilus maltogenic amylase gene, the Bacillus licheniformis alpha-amylase gene, the Bacillus amyloliquefaciens BAN amylase gene, the Bacillus εubtiliε alkaline protease gen, or the Bacilluε pumiluε xylosidase gene, or by the phage Lambda P R or P L promoters or the E. coli lac, trp or tac promoters. The DNA sequence encoding the enzyme of the invention may also, if necessary, be operably connected to a suitable terminator. The recombinant vector of the invention may further comprise a DNA sequence enabling the vector to replicate in the host cell in question. The vector may also comprise a selectable marker, e.g. a gene the product of which complements a defect in the host cell, such as the gene coding for dihydrofolate reductase (DHFR) or the Schizoεaccharomyceε pombe TPI gene (described by P.R. Russell, Gene 40, 1985, pp. 125- 130) . For filamentous fungi, selectable markers include amdS. pyrG. a_r_gB, niaD. sC. To direct an enzyme of the present invention into the secretory pathway of the host cells, a secretory signal sequence (also known as a leader sequence, prepro sequence or pre sequence) may be provided in the recombinant vector. The secretory signal sequence is joined to the DNA sequence encoding the enzyme in the correct reading frame. Secretory signal sequences are commonly positioned 5' to the DNA sequence encoding the enzyme. The secretory signal sequence may be that normally associated with the enzyme or may be from a gene encoding another secreted protein. For secretion from yeast cells, the secretory signal sequence may encode any signal peptide which ensures efficient direction of the expressed enzyme into the secretory pathway of the cell. The signal peptide may be naturally occurring signal peptide, or a functional part thereof, or it may be a synthetic peptide. Suitable signal peptides have been found to be the -factor signal peptide (cf. US 4,870,008), the signal peptide of mouse salivary amylase (cf. 0. Hagenbuchle et al., Nature 289. 1981, pp. 643-646), a modified carboxypeptidase signal peptide (cf. L.A. Vails et al.. Cell 48. 1987, pp. 887- 897) , the yeast BAR1 signal peptide (cf. WO 87/02670) , or the yeast aspartic protease 3 (YAP3) signal peptide (cf. M. Egel-Mitani et al., Yeast 6, 1990, pp. 127-137). For efficient secretion in yeast, a sequence encoding a leader peptide may also be inserted downstream of the signal sequence and upstream of the DNA sequence encoding the enzyme. The function of the leader peptide is to allow the expressed enzyme to be directed from the endoplasmic reticulum to the Golgi apparatus and further to a secretory vesicle for secretion into the culture medium (i.e. exportation of the enzyme across the cell wall or at least through the cellular membrane into the periplasmic space of the yeast cell) . The leader peptide may be the yeast α-factor leader (the use of which is described in e.g. US 4,546,082, EP 16 201, EP 123 294, EP 123 544 and EP 163 529) . Alternatively, the leader peptide may be a synthetic leader peptide, which is to say a leader peptide not found in nature. Synthetic leader peptides may, for instance, be constructed as described in WO 89/02463 or WO 92/11378. For use in filamentous fungi, the signal peptide may conveniently be derived from a gene encoding an Aspergillus sp. amylase or glucoamylase, a gene encoding a Rhizomucor miehei lipase or protease, a Humicola lanuginosa lipase. The signal peptide is preferably derived from a gene encoding A. oryzae TAKA amylase, A. niger neutral α-amylase, A. niger acid-stable amylase, or A. niger glucoamylase. The procedures used to ligate the DNA sequences coding for the present enzyme, the promoter and optionally the terminator and/or secretory signal sequence, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to persons skilled in the art (cf., for instance, Sambrook et al., op.cit.) . Host cells The DNA sequence encoding the present enzyme introduced into the host cell may be either homologous or heterologous to the host in question. If homologous to the host cell, i.e. produced by the host cell in nature, it will typically be operably connected to another promoter sequence or, if applicable, another secretory signal sequence and/or terminator sequence than in its natural environment. The term "homologous" is intended to include a cDNA sequence encoding an enzyme native to the host organism in question. The term "heterologous" is intended to include a DNA sequence not expressed by the host cell in nature. Thus, the DNA sequence may be from another organism, or it may be a synthetic sequence. The host cell into which the DNA construct or the recombinant vector of the invention is introduced may be any cell which is capable of producing the present enzyme and includes bacteria, yeast, fungi and higher eukaryotic cells. Examples of bacterial host cells which, on cultivation, are capable of producing the enzyme of the invention are gram-positive bacteria such as strains of Bacilluε , such as strains of B . subtilis, B . licheniformis, B . lentus, B . brevis, B . stearothermophilus, B . alkalophilus, B . amyloliquefaciens, B . coagulans, B . circulanε, B . lautuε , B . megatherium or B . thuringiensis , or strains of Streptomyces , such as S. lividans or S. murinuε , or gram-negative bacteria such as Echerichia coli . The transformation of the bacteria may be effected by protoplast transformation or by using competent cells in a manner known per se (cf. Sambrook et al., supra) . When expressing the enzyme in bacteria such as E. coli , the enzyme may be retained in the cytoplasm, typically as insoluble granules (known as inclusion bodies) , or may be directed to the periplasmic space by a bacterial secretion sequence. In the former case, the cells are lysed and the granules are recovered and denatured after which the enzyme is refolded by diluting the denaturing agent. In the latter case, the enzyme may be recovered from the periplasmic space by disrupting the cells, e.g. by sonication or osmotic shock, to release the contents of the periplasmic space and recovering the enzyme. Examples of suitable yeasts cells include cells of Saccharomyceε spp. or Schizoεaccharomyceε spp. , in particular strains of Saccharomyces cerevisiae or Saccharomyces fcluyveri. Methods for transforming yeast cells with heterologous DNA and producing heterologous enzymes therefrom are described, e.g. in US 4,599,311, US 4,931,373, US 4,870,008, 5,037,743, and US 4,845,075, all of which are hereby incorporated by reference. Transformed cells are selected by a phenotype determined by a selectable marker, commonly drug resistance or the ability to grow in the absence of a particular nutrient, e.g. leucine. A preferred vector for use in yeast is the POT1 vector disclosed in US 4,931,373. The DNA sequence encoding the enzyme of the invention may be preceded by a signal sequence and optionally a leader sequence , e.g. as described above. Further examples of suitable yeast cells are strains of Kluyveromyces , such as K. lactiε , Hansenula , e . g. H. polymorpha , or Pichia , e. g. P. pastoris (cf. Gleeson et al., J. Gen. Microbiol. 132. 1986, pp. 3459-3465; US 4,882,279). Examples of other fungal cells are cells of filamentous fungi, e.g. Aspergillus spp., Neurospora spp., Fusarium spp. or Trichoderma spp. , in particular strains of A. oryzae , A . nidulanε , A. niger, or Fuεarium graminearum . The use of Aspergillus spp. for the expression of pro- teins is described in, e.g., EP 272 277, EP 230 023. The transformation of F. oxysporum may, for instance, be carried out as described by Malardier et al., 1989, Gene 78: 147-156. When a filamentous fungus is used as the host cell, it may be transformed with the DNA construct of the invention, conveniently by integrating the DNA construct in the host chromosome to obtain a recombinant host cell. This integration is generally considered to be an advantage as the DNA sequence is more likely to be stably maintained in the cell. Integration of the DNA constructs into the host chromosome may be performed according to conventional methods, e.g. by homologous or heterologous recombination. The transformed or transfected host cell described above is then cultured in a suitable nutrient medium under conditions permitting the expression of the present enzyme, after which the resulting enzyme is recovered from the culture. The medium used to culture the cells may be any conventional medium suitable for growing the host cells, such as minimal or complex media containing appropriate supplements. Suitable media are available from commercial suppliers or may be prepared according to published recipes (e.g. in catalogues of the American Type Culture Collection) . The enzyme produced by the cells may then be recovered from the culture medium by conventional procedures including separating the host cells from the medium by centrifugation or filtration, precipitating the proteinaceous components of the supernatant or filtrate by means of a salt, e.g. ammonium sulphate, purification by a variety of chromatographic procedures, e.g. ion exchange chromatography, gel filtration chromatography, affinity chromatography, or the like, dependent on the type of enzyme in question. In a still further aspect, the present invention relates to a method of producing an enzyme according to the invention, wherein a suitable host cell transformed with a DNA sequence encoding the enzyme is cultured under conditions permitting the production of the enzyme, and the resulting enzyme is recovered from the culture. Enzyme Screening driven by taxonomy as well as ecolo y: A powerful tool like the molecular screening disclosed herein, designed to detect and select said type of interesting enzymes, can still not stand on its own. In order to maximize the chances of making interesting discoveries the molecular screening approach was in the present investigation combined with careful selection of which fungi to screen. The selection was done through a thorough insight in the identification of fungi, in taxono ical classification and in phylogenetic relationships. A taxonomic hot spot for production of cellulytic enzymes can further only be fully explored if also the ecological approach is included. Thorough knowledge about the adaptation to various substrates (especially saprotrophic, necrotrophic or biotrophic degradation of plant materials) are prerequisites for designing an intelligent screening and for managing a successful selection of strains and ecological niches to be searc¬ hed. Both the taxonomy and the ecological approach disclosed herein aim at maximizing discovery of said enzymes in the molecular screening program. However, still several hundreds (or if all preliminary work is included) several thousand fungi have been brought in culture in order to detect the 53 hits of said type of cellulytic enzyme here reported. The screening and cloning may be carried out using the following: MATERIALS AND METHODS List of organisms: Saccharomyces cerevisiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, or Escherichia coli , DSM 10512, DSM 10511, DSM 10571, DSM 10576, respectively, containing the plasmid comprising the full length DNA sequence, coding for the endoglucanase of the invention, in the shuttle vector pYES 2.0. Escherichia coli DSM 10583, 10584, 10585, 10586, 10587, and 10588. Diplodia gossypina Cooke Deposit of Strain, Ace No: CBS 274.96 Classification: Ascomycota, Loculoascomycetes, Dothideales, Cucurbitariaceae Ulospora bilgramii (Hawksw. et al .) Hawksw. et al . Ace No of strain: NKBC 1444, Nippon University, (Prof. Tubaki collection) Classification: Ascomycota, Loculoascomycetes, Dothideales, (family unclassified) Microsphaeropsis εp. Isolated from: Leaf of Camellia japonica (Theaceae, Guttiferales) , grown in Kunming Botanical garden, Yunnan Province, China Classification: Ascomycota, Loculoascomycetes, Dothideales, (family unclassified) Macrophomina phaεeolina (Taεεi) Goidannich Syn: Rhizoctonia bataticola Deposit of Strain, Ace No.:CBS 281.96 Isolated from seed of Glycine max (Leguminosa) , cv CMM 60, grown in Thailand, 1990 Classification: Ascomycota, Discomycetes, Rhytismat les, Rhytismataceae Aεcoboluε εtictoideuε Speg. Isolated from goose dung, Svalbard, Norway Classification: Ascomycota, Discomycetes, Pezizales, Ascobolaceae Saccoboluε dilutelluε (Fuck . ) Sacc. Deposit of strain: Ace No CBS 275.96 Classification: Ascomycota, Discomycetes, Pezizales, Ascobolaceae Penicillium verruculosum Peyronel Ex on Ace No of species: ATCC 62396 Classification: Ascomycota, Plectomycetes, Eurotiales, Trichocomaceae Penicillium chrysogenum Thorn Ace No of Strain: ATCC 9480 Classification: Ascomycota, Plectomycetes, Eurotiales, Trichocomaceae Thermomyces verrucosus Pugh et al Deposit of Strain, Ace No.: CBS 285.96 Classification: Ascomycota, Plectomycetes, Eurotiales, (family unclassified; affiliation based on 18S RNA, sequencing and homologies) Xylaria hypoxylon L . ex Greville Deposit of Strain, Ace No: CBS 284.96 Classification: Ascomycota, Pyrenomycetes, Xylariales, Xylariaceae Poronia punctata (Fr.ex L .) Fr. Classification: Ascomycota, Pyrenomycetes, Xylariales, Xylariaceae Nodulisporum sp Isolated from leaf of Camellia reticulata (Theaceae, Guttiferales) , grown in Kunming Botanical Garden, Yunnan Province, China Classification: Ascomycota, Pyrenomycetes, Xylariales, Xylariaceae Cylindrocarpon sp Isolated from marine sample, the Bahamas Classification: Ascomycota, Pyrenomycetes, Hypocreales (unclassified) Acremonium sp Deposit of Strain, Ace. No.: CBS 478.94 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Fusarium anguioides Sherbakoff Ace No of strain: IFO 4467 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Fusarium poae (Peck) Wr. Ex on Ace No of species: ATCC 60883 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Fusarium solani (Mart . ) Sacc.emnd.Snyd & Hans . Ace No of strain: IMI 107.511 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Fusarium oxysporum ssp lycopersici (Sacc . ) Snyd . & Hans . Ace No of strain: CBS 645.78 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Fusarium oxyεporum εsp pasεiflora Ace No of strain: CBS 744.79 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Gliocladium catenulatum Gillman & Abbott Ace. No. of strain: CBS 227.48 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Hypocreaceae Nectria pinea Dingley Deposit of Strain, Ace. No. CBS 279.96 Classification: Ascomycota, Pyrenomycetes, Hypocreales, Nectriaceae Volutella colletotrichoides Ace No of Strain: CBS 400.58 Classification: Ascomycota, Pyrenomycetes, Hypocreales (unclassified) Sordaria macrospora Auerswald Ex on Ace No of species: ATCC 60255 Classification: Ascomycota, Pyrenomycetes, Sordariales, Sordariaceae Sordaria fimicola (Roberge) Cesati et De Notariε Ex on Ace. No. for the species: ATCC 52644 Isolated from dung by H.Dissing, ISP, KU, Denmark Classification: Ascomycota, Pyrenomycetes, Sordariales, Sordariaceae Humicola grisea Traeen ex on Ace No for the species: ATCC 22726 Source: Hatfield Polytechnic Classification: Ascomycota, Pyrenomycetes, Sordariales, (fam. unclassified) Humicola nigreεcenε Omvik Ace No of strain: CBS 819.73 Classification: Ascomycota, Pyrenomycetes, Sordariales, (fam. unclassified) Scytalidium thermophilum (Cooney et E erεon) Austwick Ace No of strain: ATCC 28085 Classification: Ascomycota, Pyrenomycetes, Sordariales, (fam. unclassified) Thielavia thermophila Fergus et Sinden (syn Corynascus thermophilus) Ace No of strain: CBS 174.70, IMI 145.136 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Isolated from Mushroom compost Thielavia terrestris (Appinis) Malloch et Cain Ace No of strain: NRRL8126 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Cladorrhinum foecundiεεimum Saccardo et Marchal Ex on Ace No of species: ATCC 62373 Classification: Ascomycota, Pyrenomycetes, Sordariales, Lasiosphaeriaceae Isolated from leaf of Selandin sp. (Compositaceae, Asterales) , Dallas Mountain, Jamaica Syspastospora boninensiε Ace No of strain: NKBC 1515 (Nippon University, profe Tubaki Collection) Classification: Ascomycota, Pyrenomycetes, Sordariales, Cerastomataceae Chaetomium cuniculorum Fuckel Ace. No. of strain: CBS 799.83 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Chaetomium braεilienεe Batiεta et Potual Ace No of strain: CBS 122.65 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Chaetomium murorum Cor da Ace No of strain: CBS 163.52 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Chaetomium vireεcenε (von Arx) Udagawa Ace.No. of strain: CBS 547.75 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Myceliophthora thermophila (Apiniε) Oorεchot Deposit of Strain, Ace No:CBS 117.65 Classification: Ascomycota, Pyrenomycetes, Sordariales, Chaetomiaceae Nigroεpora εp Deposit of strain, Ace No: CBS 272.96 Isolated from leaf of Artocarpus altilis, Moraceae, Urticales grown in Christiana, Jamaica Classification: Ascomycota, Pyrenomycetes, Trichosphaeriales, (family unclassified) Nigroεpora sp Isolated from leaf of Pinus yuannanensis, Botanical Garden, Kuning, Yunnan. Classification: Ascomycota, Pyrenomycetes, Trichosphaeriales, Abietaceae, Pinales. Diaporthe syngeneεia Deposit of strain, Ace No: CBS 278.96 Classification: Ascomycota, Pyrenomycetes, Diaporthales, Valsaceae Colletotrichum lagenarium (Passerini) Elliε et Halεted syn Glomerella cingulata var orbiculare Jenkins et Winstead Ex on ace No of species: ATCC 52609 Classification: Ascomycota, Pyrenomycetes, Phyllaehorales Exidia glandulosa Fr. Deposit of Strain, Ace No: CBS 277.96 Classification: Basidiomycota, Hymenomycetes, Auriculariales, Exidiaceae Crinipellis scabella (Alb. &Schw. :Fr. )Murr Deposit of strain: Ace No CBS 280.96 Classification: Basidiomycota, Hymenomycetes, Agaricales, Panaeolus retirugiε (Fr. ) Gill . Ace.No. of strain: CBS 275.47 Classification: Basidiomycota, Hymenomycetes, Agaricales, Coprinaceae Fomeε fomentariuε (L. ) Fr. Deposit of strain: Ace No. CBS 276.96 Classification: Basidiomycota, Hymenomycetes, Aphyllophorales, Fomitaceae Spongipelliε εp. Deposit of Strain: Ace No CBS 283.96 Classification: Basidiomycota, Hymenomycetes, Aphyllophorales, Bjerkanderaceae (identified and affiliated taxonomically by 18S sequence and homology) Trameteε εanguinea (Fr. ) Lloyd syn: Polyporus sanguineus; Pyenoporus sanguineus (L.:Fr.) Murrill Ace No of strain: AKU 5062 (Kyoto University Culture Collection) Classification: Basidiomycota, Aphyllophorales, Polyporaceae Schizophyllum commune Fr Ace. No. of species: ATCC 38548 Classification: Basidiomycota, Aphyllophorales, Schizophyllaceae Rhizophlyctis rosea (de Bary & Wor) Fischer Deposit of Strain: Ace No.: CBS 282.96 Classification: Chytridiomycota, Chytridiomycetes, Spizellomycetales, Spizellomycetaceae Rhizomucor puεilluε (Lindt) Schipper syn: Mucor pusillus Ace No of strain: IFO 4578 Ex on Ace No of species: ATCC 46883 Classification: Zygomycota, Zygomycetes, Mucorales, Mucoraceae Phycomyceε nitens (Kunze) van Tieghem & Le Monnier Ace No of strain: IFO 4814 Ex on Ace No of species: ATCC 16327 Classification: Zygomycota, Zygomycetes, Mucorales, Mucoraceae Chaetostylum freεenii van Tieghem & Le Monnier syn. Helicostylum fresenii Ace No of strain NRRL 2305 Classification: Zygomycota, Zygomycetes, Mucorales, Thamnidiaceae Unclassified: Trichothecium roseum Ace No of strain: IFO 5372 Coniothecium sp Endophyte, isolated from leaf of unidentifed higher plant, growing in Kunming, Yunnan, China Unclassified and Un-identified: Deposit of strain, Ace No.: CBS 271.96 Isolated from leaf of Artocarpus altilis (Moraceae, Urticales) , grown in Christiana, Jamaica Deposit of strain, Ace No.: CBS 273.96 Isolated from leaf of Pimenta dioica (Myrtaceae, Myrtales) grown in Dallas Mountain, Jamaica Deposit of strain: CBS 270.96 Isolated from leaf of Pseudocalymma alliaceum (Bignoniaceae, Solanales) growing in Dallas Mountain, Jamaica Other strains: Eεcherichia coli MC1061 and DH10B. Yeast strain: The Saccharomyceε cereviεiae strain used was W3124 (MATcr; ura 3-52; leu 2-3, 112; his 3-D200; pep 4-1137; prcl::HIS3; prbl: : LEU2; cir+) . Plasmids: The Aspergillus expression vector pHD414 is a derivative of the plasmid p775 (described in EP 238 023) . The construction of pHD414 is further described in WO 93/11249. pYES 2.0 (Invitrogen) pA2C477, pA2C193, pA2C357, pA2C371, pA2C385, pA2C475, pA2C488, pA2C502 (See example 1, 2, 3 and 4). Isolation of the DNA sequence shown in SEQ ID No. 1, 4 , 6 8 10, 12, 16, or 19 respectively: The full length DNA sequence, comprising the cDNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, 16 or 19, respectively, coding for the endoglucanase of the invention, can be obtained from the deposited organism S . cerevisiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, E . COli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively, by extraction of plasmid DNA by methods known in the art (Sambrook et al. (1989) Molecular cloning: A laboratory manual, Cold Spring Harbor lab., Cold Spring Harbor, NY) . PCR primers for molecular screening of cellulases of the present invention: The four degenerate, deoxyinosine-containing oligonucleotide primers (sense; s and antisense; asl, as2 and as3) corresponding to four highly conserved amino acid regions found in the deduced amino acid sequences of Thielavia terrestriε cellulase, Myceliophthora thermophilum cellulase, and two cellulases from Acremonium sp. The residues are numbered according to the Myceliophthora thermophilum sequence. The deoxyinosines are depicted by an I in the primer sequences, and the restriction sites are underlined. Molecular screening by polymerase chain reaction (PCR) : In vitro amplification of genomic DNA and double-stranded CDNA. Directional, double-stranded cDNA was synthesized from 5 μg of poly(A) + RNA as described below. Genomic DNA was isolated according to Yelton et al . Approximately 10 to 20 ng of double-stranded, cellulase-induced cDNA or 100 to 200 ng of genomic DNA from a selection of fungal strains was PCR amplified in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 mM MgCl 2 , 0.01 % (w/v) gelatin) containing 200 μK of each dNTP and 100 pmol of each degenerate primer in three combinations: 1) sense, 5 ' -CCCCAAGCTTACI A / c GITA c / τ TGGGA c / τ TG c / τ TG c / τ AA A / 0 A / c C-3 ' antisense 1 , 5 ' - CTAGTCTAGATA A / α CAIGC A / G CA A / G CACC -3 ' ; or 2 ) sense , 5 ' - CCCCAAGCTTACI A / c GITA c / τ TGGGA c / τ TG c / τ TG c / τ AA A / Q A / c C-3 ' antisense 2 , CTAGTCTAGAAAIA A / α / τ ICCIA A / c /°ICCICCICCIGG -3 ' ; or 3) sense, 5'- CCCCAAGCTTACI A / c GITA c / τ TGGGA c / τ TG c / τ TG c / τ AA A / 0 A / c C-3' antisense 3, 5'- CTAGTCTAGAIAACCA A / 0 TCA A / 0 A / T AIC G / T CC -3; a DNA thermal cycler (Landgraf, Germany) and 2.5 units of Taq polymerase (Perkin-Elmer, Cetus, USA) . Thirty cycles of PCR were performed using a cycle profile of denaturation at 94 °C for 1 min, annealing at 64 °C for 2 min, and extension at 72 β C for 3 min. Ten-μl aliquots of the amplification products were analyzed by electrophoresis in 3 % agarose gels (NuSieve, FMC) with Haelll-digested ΦX174 RF DNA as a size marker. Direct sequencing of the PCR products. Eighty-μl aliquots of the PCR products were purified using the QIAquick PCR purification kit (Qiagen, USA) according to the manufacturer's instructions. The nucleotide sequences of the amplified PCR fragments were determined directly on the purified PCR products by the dideoxy chain-termination method, using 50-150 ng template, the Taq deoxy-terminal cycle sequencing kit (Perkin-Elmer, USA) , fluorescent labeled terminators and 5 pmol of the sense primer: 5'- CCCCAAGCTTACI A / C GITA C / T TGGGA C / T T- G c / τ TG c / τ AA A / 0 A / c C-3 ' . Analysis of the sequence data were performed according to Devereux et al . Cloning by polymerase chain reaction (PCR) : Subcloning of PCR fragments. Twentyfive-μl aliquots of the PCR products generated as described above were electrophoresed in 0.8 % low gelling temperature agarose (SeaPlaque GTG, FMC) gels, the relevant fragments were excised from the gels, and recovered by agarase treatment by adding 0.1 vol of 10 x agarase buffer (New England Biolabs) and 2 units per 100 μl molten agarose to the sample, followed by incubation at 45 °C for 1.5 h. The sample was phenol and chloroform extracted, and precipitated by addition of 2 vols of 96 % EtOH and 0.1 of 3 M NaAc, pH 5.2. The PCR fragments were recovered by centrifugation, washed in 70 % EtOH, dried and resuspended in 20 μl of restriction enzyme buffer (10 mM Tris-HCl, 10 mM MgC12, 50 mM NaCl, 1 mM DTT). The fragments were digested with Hindlll and XJbal, phenol and chloroform extracted, recovered by precipitation with 2 vols of 96 % EtOH and 0.1 of 3 M NaAc, pH 5.2, and subcloned into Hindlll/XJal-cleaved pYES 2.0 vector. Screening of cDNA libraries and characterization of the positive clones. cDNA libraries in S. cerevisiae or E. coli, constructed as described below, were screened by colony hybridization (Sambrook, 1989) using the corresponding random-primed (Feinberg and Vogelstein) 32 P-labeled (>1 x 10 9 cpm/μg) PCR products as probes. The hybridizations were carried out in 2 x SSC (Sambrook, 1989), 5 x Denhardt's solution (Sambrook, 1989), 0.5 % (w/v) SDS, 100 μg/ml denatured salmon sperm DNA for 20 h at 65 β C followed by washes in 5 x SSC at 25°C (2 x 15 min), 2 x SSC, 0.5 % SDS at 65°C (30 min), 0.2 x SSC, 0.5 % SDS at 65°C (30 min) and finally in 5 x SSC ( 2 x 15 min) at 25°C The positive cDNA clones were characterized by sequencing the ends of the cDNA inserts with pYES 2.0 polylinker primers (Invitrogen, USA) , and by determining the nucleotide seuence of the longest cDNA from both strands by the dideoxy chain termination method (Sanger et al.) using fluorescent labeled terminators. Qiagen purified plasmid DNA (Qiagen, USA) was sequenced with the Taq deoxy terminal cycle sequencing kit (Perkin Elmer, USA) and either pYES 2.0 polylinker primers (Invitrogen, USA) or synthetic oligonucleotide primers using an Applied Biosystems 373A automated sequencer according to the manufacturers instructions. Analysis of the sequence data was performed according to Devereux et al . Extraction of total RNA was performed with guanidinium thiocyanate followed by ultracentrifugation through a 5.7 M CsCl cushion, and isolation of poly(A) + RNA was carried out by oligo(dT)-cellulose affinity chromatography using the procedures described in WO 94/14953. cDNA synthesis: Double-stranded cDNA was synthesized from 5 μg poly(A) + RNA by the RNase H method (Gubler and Hoffman (1983) Gene 25:263-269, Sambrook et al. (1989) Molecular cloning: A laboratory manual, Cold Spring Harbor lab., Cold Spring Harbor, NY) using the hair-pin modification developed by F. S. Hagen (pers. comm.). The poly(A) + RNA (5 μg in 5 μl of DEPC-treated water) was heated at 70°C for 8 min. in a pre-siliconized, RNase- free Eppendorph tube, quenched on ice and combined in a final volume of 50 μl with reverse transcriptase buffer (50 mM Tris-Cl, pH 8.3, 75 mM KC1, 3 mM MgCl 2 , 10 mM DTT, Bethesda Research Laboratories) containing 1 mM of dATP, dGTP and dTTP and 0.5 mM 5-methyl-dCTP (Pharmacia) , 40 units human placental ribonuclease inhibitor (RNasin, Promega) , 1.45 μg of oligo(dT), 8 -Not I primer (Pharmacia) and 1000 units Superscript II RNase H reverse transcriptase (Bethesda Research Laboratories) . First- strand cDNA was synthesized by incubating the reaction mixture at 45°C for 1 hour. After synthesis, the mRNA:cDNA hybrid mixture was gelfiltrated through a MicroSpin S-400 HR (Pharmacia) spin column according to the manufacturer's instructions. After the gelfiltration, the hybrids were diluted in 250 μl second strand buffer (20 mM Tris-Cl, pH 7.4, 90 mM KC1, 4.6 mM MgCl 2 , 10 mM (NH 4 ) 2 S0 4 , 0.16 mM 0NAD+) containing 200 μM of each dNTP, 60 units E . coli DNA polymerase I (Pharmacia), 5.25 units RNase H (Promega) and 15 units E . coli DNA ligase (Boehringer Mannheim) . Second strand cDNA synthesis was performed by incubating the reaction tube at 16°C for 2 hours and additional 15 min. at 25°C The reaction was stopped by addition of EDTA to a final concentration of 20 mM followed by phenol and chloroform extractions. Mung bean nuclease treatment: The double-stranded cDNA was precipitated at -20°C for 12 hours by addition of 2 vols 96% EtOH, 0.2 vol 10 M NH 4 Ac, recovered by centrifugation, washed in 70% EtOH, dried and resuspended in 30 μl Mung bean nuclease buffer (30 mM NaAc, pH 4.6, 300 mM NaCl, 1 mM ZnS0 4 , 0.35 mM DTT, 2% glycerol) containing 25 units Mung bean nuclease (Pharmacia) . The single-stranded hair-pin DNA was clipped by incubating the reaction at 30 β C for 30 min., followed by addition of 70 μl 10 mM Tris-Cl, pH 7.5, 1 mM EDTA, phenol extraction and precipitation with 2 vols of 96% EtOH and 0.1 vol 3 M NaAc, pH 5.2 on ice for 30 min. Blunt-ending with T4 DNA polymerase: The double-stranded cDNAs were recovered by centrifugation and blunt-ended in 30 μl T4 DNA polymerase buffer (20 mM Tris-acetate, pH 7.9, 10 mM MgAc, 50 mM KAc, 1 mM DTT) containing 0.5 mM of each dNTP and 5 units T4 DNA polymerase (New England Biolabs) by incubating the reaction mixture at 16°C for 1 hour. The reaction was stopped by addition of EDTA to a final concentration of 20 mM, followed by phenol and chloroform extractions, and precipitation for 12 hours at -20°C by adding 2 vols 96% EtOH and 0.1 vol 3 M NaAc pH 5.2. Adaptor ligation. Not I digestion and size selection: After the fill-in reaction the cDNAs were recovered by centrifugation, washed in 70% EtOH and dried. The cDNA pellet was resuspended in 25 μl ligation buffer (30 mM Tris-Cl, pH 7.8, 10 mM MgCl 2 , 10 mM DTT, 0.5 mM ATP) containing 2.5 μg non-palindromic BstXI adaptors (Invitrogen) and 30 units T4 ligase (Promega) and incubated at 16°C for 12 hours. The reaction was stopped by heating at 65°C for 20 min. and then cooling on ice for 5 min. The adapted cDNA was digested with Not I restriction enzyme by addition of 20 μl water, 5 μl lOx Not I restriction enzyme buffer (New England Biolabs) and 50 units Not I (New England Biolabs) , followed by incubation for 2.5 hours at 37°C. The reaction was stopped by heating at 65°C for 10 min. The cDNAs were size-fractionated by gel electrophoresis on a 0.8% SeaPlaque GTG low melting temperature agarose gel (FMC) in lx TBE to separate unligated adaptors and small cDNAs. The cDNA was size-selected with a cut-off at 0.7 kb and rescued from the gel by use of 3-Agarase (New England Biolabs) according to the manufacturer's instructions and precipitated for 12 hours at -20 β C by adding 2 vols 96% EtOH and 0.1 vol 3 M NaAc pH 5.2. Construction of libraries: The directional, size-selected cDNA was recovered by centrifugation, washed in 70% EtOH, dried and resuspended in 30 μl 10 mM Tris-Cl, pH 7.5, 1 mM EDTA. The cDNAs were desalted by gelfiltration through a MicroSpin S-300 HR (Pharmacia) spin column according to the manufacturer's instructions. Three test ligations were carried out in 10 μl ligation buffer (30 mM Tris-Cl, pH 7.8, 10 mM MgCl 2 , 10 mM DTT, 0.5 mM ATP) containing 5 μl double-stranded cDNA (reaction tubes #1 and #2) , 15 units T4 ligase (Promega) and 30 ng (tube #1) , 40 ng (tube #2) and 40 ng (tube #3, the vector background control) of BstXI-NotI cleaved pYES 2.0 vector. The ligation reactions were performed by incubation at 16°C for 12 hours, heating at 70°C for 20 min. and addition of 10 μl water to each tube. 1 μl of each ligation mixture was electroporated into 40 μl electrocompetent E. coli DH10B cells (Bethesda research Laboratories) as described (Sambrook et al. (1989) Molecular cloning: A laboratory manual, Cold Spring Harbor lab., Cold Spring Harbor, NY). Using the optimal conditions a library was established in E. coli consisting of pools. Each pool was made by spreading transformed E. coli on LB+ampicillin agar plates giving 15.000-30.000 colonies/plate after incubation at 37°C for 24 hours. 20 ml LB+ampicillin was added to the plate and the cells were suspended herein. The cell suspension was shaked in a 50 ml tube for 1 hour at 37°C Plasmid DNA was isolated from the cells according to the manufacturer's instructions using QIAGEN plasmid kit and stored at -20°C 1 μl aliquots of purified plasmid DNA (100 ng/μl) from individual pools were transformed into S . cerevisiae W3124 by electroporation (Becker and Guarante (1991) Methods Enzymol. 194:182-187) and the transformants were plated on SC agar containing 2% glucose and incubated at 30 β C Identification of positive colonies: After 3-5 days of growth, the agar plates were replica plated onto a set of SC + galactose-uracil agar plates containing 0.1% AZCL HE cellulose. These plates were incubated for 3-7 days at 30°C Endoglucanase positive colonies were identified as colonies surrounded by a blue halo. Cells from enzyme-positive colonies were spread for single colony isolation on agar, and an enzyme-producing single colony was selected for each of the endoglucanase- producing colonies identified. Characterization of positive clones: The positive clones were obtained as single colonies, the cDNA inserts were amplified directly from the yeast colony using biotinylated polylinker primers, purified by magnetic beads (Dynabead M-280, Dynal) system and characterized individually by sequencing the 5'-end of each cDNA clone using the chain-termination method (Sanger et al. (1977) Proc. Natl. Acad. Sci. U.S.A. 74:5463-5467) and the Sequenase system (United States Biochemical) . The nucleotide sequence was determined of the longest cDNA from both strands by the dideoxy chain termination method (Sanger et al.) using fluorescent labeled terminators. Plasmid DNA was rescued by transformation into E . coli as described below. Qiagen purified plasmid DNA (Qiagen, USA) was sequenced with the Taq deoxy terminal cycle sequencing kit (Perkin Elmer, USA) and either pYES 2.0 polylinker primers (Invitrogen, USA) or synthetic oligonucleotide primers using an Applied Biosystems 373A automated sequencer according to the manufacturers instructions. Analysis of the sequence data was performed according to Devereux et al . Isolation of a cDNA gene for expression in Aspergillus: An endoglucanase-producing yeast colony was inoculated into 20 ml YPD broth in a 50 ml glass test tube. The tube was shaken for 2 days at 30°C The cells were harvested by centrifugation for 10 min. at 3000 rpm. DNA was isolated according to WO 94/14953 and dissolved in 50 μl water. The DNA was transformed into E . coli by standard procedures. Plasmid DNA was isolated from E . coli using standard procedures, and analyzed by restriction enzyme analysis. The cDNA insert was excised using appropriate restriction enzymes and ligated into an Aspergillus expression vector. Transformation of Aspergillus oryzae or Aspergillus niger Protoplasts may be prepared as described in WO 95/02043, p. 16, line 21 - page 17, line 12, which is hereby incorporated by reference. 100 μl of protoplast suspension is mixed with 5-25 μg of the appropriate DNA in 10 μl of STC (1.2 M sorbitol, 10 mM Tris-HCl, pH = 7.5, 10 mM CaCl 2 ) . Protoplasts are mixed with p3SR2 (an A . nidulans amdS gene carrying plasmid) . The mixture is left at room temperature for 25 minutes. 0.2 ml of 60% PEG 4000 (BDH 29576), 10 mM CaCl 2 and 10 mM Tris-HCl, pH 7.5 is added and carefully mixed (twice) and finally 0.85 ml of the same solution is added and carefully mixed. The mixture is left at room temperature for 25 minutes, spun at 2500 g for 15 minutes and the pellet is resuspended in 2 ml of 1.2 M sorbitol. After one more sedimentation the protoplasts are spread on minimal plates (Cove, Biochem. Biophys. Acta 113 (1966) 51-56) containing 1.0 M sucrose, pH 7.0, 10 mM acetamide as nitrogen source and 20 mM CsCl to inhibit background growth. After incubation for 4-7 days at 37°C spores are picked and spread for single colonies. This procedure is repeated and spores of a single colony after the second reisolation is stored as a defined transformant. Test of A. oryzae transformants Each of the transformants were inoculated in 10 ml YPM and propagated. After 2-5 days of incubation at 37°C, 10 ml supernatant was removed. The endoglucanase activity was identified by AZCL HE cellulose as described above. Hybridization conditions (to be used in evaluating property ii) of the DNA construct of the invention) : Suitable conditions for determining hybridization between a nucleotide probe and a homologous DNA or RNA sequence involves presoaking of the filter containing the DNA fragments or RNA to hybridize in 5 x SSC (standard saline citrate) for 10 min, and prehybridization of the filter in a solution of 5 x SSC (Sambrook et al. 1989), 5 x Denhardt's solution (Sambrook et al. 1989), 0.5 % SDS and 100 μg/ml of denatured sonicated salmon sperm DNA (Sambrook et al. 1989) , followed by hybridization in the same solution containing a random-primed (Feinberg, A. P. and Vogelstein, B. (1983) Anal. Biochem . 132:6-13), 3 P- dCTP-labeled (specific activity > 1 x 10 9 cpm/μg ) probe for 12 hours at ca. 45°C. The filter is then washed two times for 30 minutes in 2 x SSC, 0.5 % SDS at preferably not higher than 50°C, more preferably not higher than 55°C, more preferably not higher than 60°C, more preferably not higher than 65°C, even more preferably not higher than 70°C, especially not higher than 75°C. The nucleotide probe to be used in the hybridization is the DNA sequence corresponding to the endoglucanase encoding part of the DNA sequence shown in SEQ ID No. 1, 4, 6, 8, 10, 12, or 16, resepctively, and/or the DNA sequence obtainable from the plasmid in S . cereviεiae , DSM 9770, DSM 10082, DSM 10080, DSM 10081, E. COli , DSM 10512, DSM 10511, DSM 10571 or DSM 10576, respectively. Immunological cross-reactivity: Antibodies to be used in determining immunological cross-reactivity may be prepared by use of a purified cellulase. More specifically, antiserum against the cellulase of the invention may be raised by immunizing rabbits (or other rodents) according to the procedure described by N. Axelsen et al. in: A Manual of Quantitative Immunoelec- trophoresis. Blackwell Scientific Publications, 1973, Chapter 23, or A. Johnstone and R. Thorpe, Immunochemistry in Practice. Blackwell Scientific Publications, 1982 (more specifically pp. 27-31) . Purified immunoglobulins may be obtained from the anti- sera, for example by salt precipitation ((NH 4 ) 2 S0 4 ) , followed by dialysis and ion exchange chromatography, e.g. on DEAE-Sephadex. Immunochemical characterization of proteins may be done either by Outcherlony double- diffusion analysis (O. Ouchterlony in: Handbook of Experimental Immunology (D.M. Weir, Ed.), Blackwell Scientific Publications, 1967, pp. 655-706) , by crossed immunoelectrophoresis (N. Axelsen et al.. supra. Chapters 3 and 4) , or by rocket immunoelectrophoresis (N. Axelsen et al.. Chapter 2) . Media YPD: 10 g yeast extract, 20 g peptone, H 2 0 to 900 ml. Autoclaved, 100 ml 20% glucose (sterile filtered) added. YPM: 10 g yeast extract, 20 g peptone, H 2 0 to 900 ml. Autoclaved, 100 ml 20% maltodextrin (sterile filtered) added. 10 x Basal salt: 75 g yeast nitrogen base, 113 g succinic acid, 68 g NaOH, H 2 0 ad 1000 ml, sterile filtered. SC-URA: 100 ml 10 x Basal salt, 28 ml 20% casamino acids without vitamins, 10 ml 1% tryptophan, H 2 0 ad 900 ml, autoclaved, 3.6 ml 5% threonine and 100 ml 20% glucose or 20% galactose added. SC-URA agar: SC-URA, 20 g/1 agar added. PD agar: 39g potato dextrose agar, DIFCO 0013; add deionized water up to 1000ml; autoclave (121°C for 15-20 min) . PC agar: Potatoes and carrots (grinded, 20 g of each) and water, added up to 1000ml, are boiled for 1 hr; agar (20g/l of Merck 1614) ; autoclave (121°C for 20 min) PC liquid broth: as PC agar but without the Agar PD liquid broth: 24g potato dextrose broth, Difco 0549, deionized water up to 1000ml; autoclave (121°C for 15-20 min) PC and PD liquid broth with cellulose: add 30 g Solcafloc (Dicacel available from Dicalite-Europe-Nord, 9000 Gent, Belgium) per 1000ml PB-9 liquid broth: 12 g Rofec (Roquette 101-0441) and 24 g glucose are added to 1000ml water; pH is adjusted to 5.5; 5ml mineral oil and 5 g CaCo 3 are added per 1000ml. autoclave (121°C for 40 min) YPG liquid broth: 4g yeast extract (Difco 0127) , lg KH 2 P0 4 (Merck4873), 0.5g MgS0 4 .7H20 Merck 5886, 15g Dextrose, Roquette 101-0441, 0.1ml Pluronic (101-3088); deionized water up to 1000ml; autoclave (20min at 121°C) Dilute salt solution (DS) : Make up two stock solutions: P-stock: 13 . 61g KH 2 P0 4 ; 13 . 21g (NH 4 ) 2P0 4 , 17 . 42g KH 2 P0 4 ; deionized water up to 100ml Ca/Mg stock: 7 . 35g CaCl 2 , 2H 2 0 , 10 . 17g MgCl 2 , 6H 2 0 , deionized water up to 100ml; pH adjusted to 7.0; autoclaving (121°C; 20min) Mix 0..5ml P-stock with 0.1ml Ca/Mg stock add deionized water up to 1000ml AZCL HE cellulose (Megazyme, Australia) . Uses During washing and wearing, dyestuff from dyed fabrics or garment will conventionally bleed from the fabric which then looks faded and worn. Removal of surface fibers from the fabric will partly restore the original colours and looks of the fabric. By the term "colour clarification", as used herein, is meant the partly restoration of the initial colours of fabric or garment throughout multiple washing cycles. The term "de-pilling" denotes removing of pills from the fabric surface. The term "soaking liquor" denotes an aqueous liquor in which laundry may be immersed prior to being subjected to a conventional washing process. The soaking liquor may contain one or more ingredients conventionally used in a washing or laundering process. The term "washing liquor" denotes an aqueous liquor in which laundry is subjected to a washing process, i.e. usually a combined chemical and mechanical action either manually or in a washing machine. Conventionally, the washing liquor is an aqueous solution of a powder or liquid detergent composition. The term "rinsing liquor" denotes an aqueous liquor in which laundry is immersed and treated, conventionally immediately after being subjected to a washing process, in order to rinse the laundry, i.e. essentially remove the detergent solution from the laundry. The rinsing liquor may contain a fabric conditioning or softening composition. The laundry subjected to the method of the present inven¬ tion may be conventional washable laundry. Preferably, the major part of the laundry is sewn or unsewn fabrics, including knits, wovens, denims, yarns, and toweling, made from cotton, cotton blends or natural or manmade cellulosics (e.g. originating from xylan-containing cel¬ lulose fibers such as from wood pulp) or blends thereof. Examples of blends are blends of cotton or rayon/viscose with one or more companion material such as wool, syn¬ thetic fibers (e.g. polyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyvinylidene chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers) , and cellulose-containing fibers (e.g. rayon/viscose, ramie, flax/linen, jute, cellulose acetate fibers, lyocell) . Detergent Compositions According to one aspect of the present invention, the present endoglucanases may typically be components of a detergent composition. As such, they may be included in the detergent composition in the form of a non-dusting granulate, a stabilized liquid, or protected enzymes. Non-dusting granulates may be produced, e.g., as dis¬ closed in US 4,106,991 and 4,661,452 (both to Novo Industri A/S) and may optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethyleneglycol, PEG) with mean molecular weights of 1000 to 20000; ethoxylated nonylphenols having from 16 to 50 ethylene oxide units; ethoxylated fatty alcohols in which the alcohol contains from 12 to 20 carbon atoms and in which there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono- and di- and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluid bed techniques are given in patent GB 1483591. Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods. Other enzyme stabilizers are well known in the art. Protected enzymes may be prepared according to the method disclosed in EP 238,216. The detergent composition of the invention may be in any convenient form, e.g. as powder, granules, paste or liquid. A liquid detergent may be aqueous, typically con¬ taining up to 70% water and 0-30% organic solvent, or nonaqueous. The detergent composition comprises one or more surf¬ actants, each of which may be anionic, nonionic, cationic, or zwitterionic. The detergent will usually contain 0-50% of anionic surfactant such as linear alkylbenzenesulfonate (LAS) , alpha-olefinsulfonate (AOS) , alkyl sulfate (fatty alcohol sulfate) (AS) , alcohol ethoxysulfate (AEOS or AES) , secondary alkanesulfonates (SAS) , alpha-sulfo fatty acid methyl esters, alkyl- or alkenylsuccinic acid, or soap. It may also contain 0-40% of nonionic surfactant such as alcohol ethoxylate (AEO or AE) , carboxylated alcohol ethoxylates, nonylphenol ethoxylate, alkylpolyglycoside, alkyldi ethylamine oxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, or polyhydroxy alkyl fatty acid amide (e.g. as described in WO 92/06154) . The detergent composition may additionally comprise one or more other enzymes such as amylase, lipase, cutinase, protease, peroxidase, and oxidase, e.g. laccase. The detergent may contain 1-65% of a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, citrate, nitrilotriacetic acid (NTA) , ethylenediaminetetraacetic acid (EDTA) , diethylenetriaminepentaacetic acid (DTMPA) , alkyl- or alkenylsuccinic acid, soluble silicates or layered silicates (e.g. SKS-6 from Hoechst) . The detergent may also be unbuilt, i.e. essentially free of detergent builder. The detergent may comprise one or more polymers. Examples are carboxymethylcellulose (CMC) , poly(vinylpyrrolidone) (PVP) , polyethyleneglycol (PEG) , poly(vinyl alcohol) (PVA) , polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers. The detergent may contain a bleaching system which may comprise a H 2 0 2 source such as perborate or percarbonate which may be combined with a peracid-forming bleach activator such as tetraacetylethylenediamine (TAED) or nonanoyloxybenzenesulfonate (NOBS) . Alternatively, the bleaching system may comprise peroxyacids of, e.g., the amide, i ide, or sulfone type. The enzymes of the detergent composition of the invention may be stabilized using conventional stabilizing agents, e.g. a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative such as, e.g., an aromatic borate ester, and the composition may be formulated as described in, e.g., WO 92/19709 and WO 92/19708. The detergent may also contain other conventional deter¬ gent ingredients such as, e.g., fabric conditioners in¬ cluding clays, foam boosters, suds suppressors, anti- corrosion agents, soil-suspending agents, anti-soil- redeposition agents, dyes, bactericides, optical brighteners, or perfume. The pH (measured in aqueous solution at use concentra¬ tion) will usually be neutral or alkaline, e.g. in the range of 7-11. Particular forms of detergent compositions within the scope of the invention include: 1) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 2) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 3) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 4) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 5) An aqueous liquid detergent composition comprising 6) An aqueous structured liquid detergent composition comprising 7) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 8) A detergent composition formulated as a granulate comprising 9) A detergent composition formulated as a granulate comprising 10) An aqueous liquid detergent composition comprising 11) An aqueous liquid detergent composition comprising 12) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 13) Detergent formulations as described in 1) - 12) wherein all or part of the linear alkylbenzenesulfonate is replaced by (C 12 -C 18 ) alkyl sulfate. 14) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 15) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 16) Detergent formulations as described in 1) - 15) which contain a stabilized or encapsulated peracid, either as an additional component or as a substitute for already specified bleach systems. 17) Detergent compositions as described in 1) , 3) , 7) , 9) and 12) wherein perborate is replaced by percarbonate. 18) Detergent compositions as described in 1), 3), 7), 9) , 12) , 14) and 15) which additionally contain a manganese catalyst. The manganese catalyst may, e.g., be one of the compounds described in "Efficient manganese catalysts for low-temperature bleaching", Nature 369, 1994, pp. 637-639. 19) Detergent composition formulated as a nonaqueous detergent liquid comprising a liquid nonionic surfactant such as, e.g., linear alkoxylated primary alcohol, a builder system (e.g. phosphate), enzyme and alkali. The detergent may also comprise anionic surfactant and/or a bleach system. The endoglucanase may be incorporated in concentrations conventionally employed in detergents. It is at present contemplated that, in the laundry composition of the in- vention, the cellulase may be added in an amount corre¬ sponding to 0.0001-10 mg (calculated as pure enzyme protein) of cellulase per liter of wash liquor. According to yet another aspect of the present invention, endoglucanase may typically be a component of a fabric conditioning or softener composition. Examples of conven¬ tional softener compositions are disclosed in e.g. EP 0 233 910. Textile applications In another embodiment, the present invention relates to use of the endoglucanase of the invention in the bio- polishing process. Bio-Polishing is a specific treatment of the yarn surface which improves fabric quality with respect to handle and appearance without loss of fabric wettability. The most important effects of Bio-Polishing can be characterized by less fuzz and pilling, increased gloss/luster, improved fabric handle, increased durable softness and altered water absorbency. Bio-Polishing usually takes place in the wet processing of the manufacture of knitted and woven fabrics. Wet processing comprises such steps as e.g. desizing, scouring, bleaching, washing, dying/printing and finishing. During each of these steps, the fabric is more or less subjected to mechanical action. In general, after the textiles have been knitted or woven, the fabric proceeds to a desizing stage, followed by a scouring stage, etc. Desizing is the act of removing size from textiles. Prior to weaving on mechanical looms, warp yarns are often coated with size starch or starch derivatives in order to increase their tensile strength. After weaving, the size coating must be removed before further processing the fabric in order to ensure a homogeneous and wash-proof result. It is known that in order to achieve the effects of Bio- Polishing, a combination of cellulytic and mechanical action is required. It is also known that "super- softness" is achievable when the treatment with a cellulase is combined with a conventional treatment with softening agents. It is contemplated that use of the endoglucanase of the invention for bio-polishing of cellulosic fabrics is advantageous, e.g. a more thorough polishing can be achieved. Bio-polishing may be obtained by applying the method described e.g. in wo 93/20278. Stone-washing It is known to provide a "stone-washed" look (localized abrasion of the colour) in dyed fabric, especially in denim fabric or jeans, either by washing the denim or jeans made from such fabric in the presence of pumice stones to provide the desired localized lightening of the colour of the fabric or by treating the fabric enzymatically, in particular with cellulytic enzymes. The treatment with an endoglucanase of the present invention may be carried out either alone such as disclosed in US 4,832,864, together with a smaller amount of pumice than required in the traditional process, or together with perlite such as disclosed in WO 95/09225. Pulp and paper applications In the papermaking pulp industry, the endoglucanase of the present invention may be applied advantageously e.g. as follows: - For debarking: pretreatment with the endoglucanase may degrade the cambium layer prior to debarking in mechanical drums resulting in advantageous energy savings. - For defibration: treatment of a material containing cellulosic fibers with the endoglucanase prior to refin¬ ing or beating may result in reduction of the energy consumption due to the hydrolysing effect of the cellulase on the interfibre surfaces. Use of the endoglucanase may result in improved energy savings as compared to the use of known enzymes, since it is believed that the enzyme composition of the invention may possess a higher ability to penetrate fibre walls. - For fibre modification, i.e. improvement of fibre prop¬ erties where partial hydrolysis across the fibre wall is needed which requires deeper penetrating enzymes (e.g. in order to make coarse fibers more flexible) . Deep treatment of fibers has so far not been possible for high yield pulps e.g. mechanical pulps or mixtures of recycled pulps. This has been ascribed to the nature of the fibre wall structure that prevents the passage of enzyme molecules due to physical restriction of the pore matrix of the fibre wall. It is contemplated that the present endoglucanase is capable of penetrating into the fibre wall. - For drainage improvement. The drainability of papermaking pulps may be improved by treatment of the pulp with hydrolysing enzymes, e.g. cellulases. Use of The treatment of lignocellulosic pulp may, e.g., be performed as described in WO 91/14819, WO 91/14822, WO 92/17573 and WO 92/18688. Degradation of plant material In yet another embodiment, the present invention relates to use of the endoglucanase and/or enzyme preparation according to the invention for degradation of plant material e.g. cell walls. It is contemplated that the novel endoglucanase and/or enzyme preparation of the invention is useful in the pre- paration of wine, fruit or vegetable juice in order to increase yield. Endoglucanases according to the invention may also be applied for enzymatic hydrolysis of various plant cell-wall derived materials or waste materials, e.g. agricultural residues such as wheat-straw, corn cobs, whole corn plants, nut shells, grass, vegetable hulls, bean hulls, spent grains, sugar beet pulp, and the like. The plant material may be degraded in order to improve different kinds of processing, facilitate purification or extraction of other components like purification of beta-glucan or beta-glucan oligomers from cereals, improve the feed value, decrease the water binding capacity, improve the degradability in waste water plants, improve the conversion of e.g. grass and corn to ensilage, etc. The following examples illustrate the invention. EXAMPLE 1 Cellulytic enzymes from 4 fungi, belonging to 3 families under two orders within the Ascomycetes were detected by expression cloning; corresponding DNA sequences were determined; the enzymes heterologously expressed, and produced by liquid fermentation, characterized and demonstrated to give good performance in colour clarifi¬ cation assays. Isolate CBS 117.65, CBS 478.94, NRRL 8126, and ATCC 10523 were grown in shake flask cultures on cellulose enriched potato dextrose broth, incubated for 5 days at 26°C (shaking conditions, 150 rpm) . A. Cloning and expression of an endoglucanase from Myceliophthora thermophila, Acremonium sp. , and Thielavia terrestris and Volutella colletotrichoides mRNA was isolated from Myceliophthora thermophila, Acremonium sp. , Thielavia terrestris and Volutella colletotrichoides , respectively, grown in a cellulose- containing fermentation medium with agitation to ensure sufficient aeration. Mycelia were harvested after 3-5 days' growth, immediately frozen in liquid nitrogen and stored at -80°C Libraries from Myceliophthora thermophila, Acremonium sp. , Thielavia terrestris and Volutella colletotrichoides , respectively, each consisting of approx. 10 6 individual clones were constructed in E . coli as described with a vector background of 1%. Plasmid DNA from some of the pools from each library was transformed into yeast, and 50-100 plates containing 250- 400 yeast colonies were obtained from each pool. Endoglucanase-positive colonies were identified and isolated on SC-agar plates with the AZCL HE cellulose assay. cDNA inserts were amplified directly from the yeast colonies and characterized as described in the Materials and Methods section above. The DNA sequence of the cDNA encoding the endoglucanase from Myceliophthora thermophila is shown in SEQ ID No. 1 and the corresponding amino acid sequence is also shown in SEQ ID No. 1. The cDNA is obtainable from the plasmid in DSM 9770. The DNA sequence of the cDNA encoding the endoglucanase from Acremonium sp . is shown in SEQ ID No. 4 and the corresponding amino acid sequence is shown in SEQ ID No. 5. The cDNA is obtainable from the plasmid in DSM 10082. The DNA sequence of the cDNA encoding the endoglucanase from Thielavia terreεtriε is shown in SEQ ID No. 8 and the corresponding amino acid sequence is shown in SEQ ID No. 9. The cDNA is obtainable from the plasmid in DSM 10081. The DNA sequence of the cDNA encoding the endoglucanase from Volutella colletotrichoideε is shown in SEQ ID No. 16 and the corresponding amino acid sequence is shown in SEQ ID No. 17. The cDNA is obtainable from the plasmid in DSM 10571. Total DNA was isolated from a yeast colony and plasmid DNA was rescued by transformation of E. coli as described above. In order to express the endoglucanases in Aspergillus , the DNA was digested with appropriate restriction enzymes, size fractionated on gel, and a fragment corresponding to the endoglucanase gene from Myceliophthora thermophila, Acremonium sp . , Thielavia terreεtriε and Volutella colletotrichoides, respectively, was purified. The genes were subsequently ligated to pHD414, digested with appropriate restriction enzymes, resulting in the plasmids pA2C193, pA2C357, pA2C385 and pA2C488, respectively. After amplification of the DNA in E. coli the plasmids were transformed into Aspergillus oryzae as described above. Test of A. oryzae transformants Each of the transformants were tested for endoglucanase activity as described above. Some of the transformants had endoglucanase activity which was significantly larger than the Aspergillus oryzae background. This demonstrates efficient expression of the endoglucanases in Aspergillus oryzae . The transformants with the highest endoglucanase activity were selected and inoculated in a 500 ml shake flask with YPM media. After 3-5 days of fermentation with sufficient agitation to ensure good aeration, the culture broth was centrifuged for 10 minutes at 2000 g and the supernatant recovered. B. Determination of endoglucanase activity The cellulytic activity of the endoglucanase may be determined relative to an analytical standard and expressed in the unit S-CEVU. Cellulytic enzymes hydrolyse CMC, thereby decreasing the viscosity of the incubation mixture. The resulting reduction in viscosity may be determined by a vibration viscosimeter (e.g. MIVI 3000 from Sofraser, France) . Determination of the cellulytic activity, measured in terms of S-CEVU, may be determined according to the analysis method AF 301.1 which is available from the Applicant upon request. The S-CEVU assay quantifies the amount of catalytic activity present in the sample by measuring the ability of the sample to reduce the viscosity of a solution of carboxy-methylcellulose (CMC) . The assay is carried out at 40°C, pH 7.5 using a relative enzyme standard for reducing the viscosity of the CMC substrate. Assay for determination of endoglucanase activity in terms of SAVI units using phosphoric-acid swollen cellu- lose (PASC) : Definition: 1 SAVI-U is the amount of enzyme which forms an amount of reducing carbohydrates equivalent to 1 μmol of glucose per minute. Assay condition: Enzyme solution: 0,5 ml 4 g/1 PASC in 0,1 M Buffer: 2.0 ml 20 min, 40 °C Sensitivity: Max 0.1 SAVIU/ml = approx. 1 S-CEVU/ml (CMC viscosity) Min 0.01 SAVIU/ml = approx. 0.1 S-CEVU/ml Determination of formation of reducing sugars: The reducing groups assay was performed according to Lever, M. A new reaction for colormetric determination of carbohydrates. Anal. Biochem. 1972. Vol 47 (273-279). Reagent mixture was prepared by mixing 1,5 gram p- hydroxybenzoic-acide hydracide (PHBAH) with 5 gram sodium tartrate in 100 ml 2 % sodium hydroxide. Substrate: PASC stock solution was prepared the following way using ice cold acetone and phosphoric acid. 5 gram of cellulose (Avicel * ) was moistered with water, and 150 ml ice cold 85% ortho-phosphoric acid was added. The mixture was placed in ice bath under slow stirring for 1 hr. Then 100 ml ice cold acetone was added with stirring. The slurry was transferred to a Buchner filter with pyrex sintered disc number 3 and then washed three times with 100 ml ice cold acetone, and sucked as dry as possible after each wash. Finally, the filter cake was washed twice with 500 ml water, sucked as dry as possible after each wash. The PASC was mixed with deionized water to a total volume of 300 ml, blended to homogeneity (using the Ultra Turrax Homogenizer) and stored in refrigerator (up to one month) . Substrate equilibration with buffer: 20 gram phosphoric acid swollen cellulose PASC stock solution was centrifu- ged for 20 min at 5000 rpm. , the supernatant was poured of; the sediment was resuspended in 30 ml of buffer and centrifuged for 20 min. at 5000 rpm., the supernatant was poured of, and the sediment was resuspended in buffer to a total of 60 g corresponding to a substrate concentra¬ tion of 5 g cellulose/litre. Buffer for pH 8,5 determination: 0.1 M Barbital. Buffer for pH 10 determination: 0.1 M Glycine. Procedure: 1. Dilution of enzyme samples The enzyme solution is diluted in the same buffer as the substrate. 2. Enzyme reaction The substrate in buffer solution is preheated for 5 min. at 40 * C (2 ml) . Then the enzyme solution (diluted to between 0.2 and 1 S- CEVU/ml) 0,5 ml is added and mixed for 5 sec. Enzymes blanks are obtained by adding the stop reagent before enzyme solution. Incubate for 20 min. at 40 * C The reaction is stopped by adding 0.5 ml 2% NaOH solution and mixing for 5 sec. The samples are centrifuged for 20 min. at 5000 rpm. 1 ml supernatant is mixed with 0.5 ml PHBAH reagent and boiled for 10 min. The test tubes are cooled in a ice water bath. 3. Determination of reducing end groups: The absorbancy at 410 nm is measured using a spectrophotometer. Blanks are prepared by adding sodium hydroxide before adding enzyme solution. A standard glucose curve was obtained by using glucose concentrations of 5, 10, 15 and 25 mg/1 in the same buffer and adding PHBAH reagent before boiling. The release of reducing glucose equivalent is calculated using this standard curve. 4. Calculation of catalytic activity: Measure absorbance at 410 nm 1) Standard curve (Glucose) - (H 2 0) vs concentration of glucose 2) Enzyme sample (Sample) - (Blank) Calculate glucose concentration according to a standard curve Activity (SAVIU/ml) : X (mg glucose/1) * Dilution 180.16 (MW of glucose) * 20 (min) C. Purification and characterisation of the endoglucanase from M. thermophila Aspergillus oryzae transformed with pA2C193 was grown on YPM medium for 4 days. The liquid was then centrifuged and sterile filtered. The sample was concentrated by ultrafiltration on AMICON cells using a DOW membrane GR61PP with cut-off 20 kD. The Uf-concentrate was analyzed for S-CEVU/ml and SaviU/ml with the following result: Purification: 2 ml of the UF-concentrate was diluted 5 times to lower the ionic strength and filtered through 0.22 μm disk filter. This sample was applied to a Mono Q * HR5/5 Phar¬ macia column, equilibrated with 50 mM Tris/HCl buffer, pH 7.5, (buffer A) and a flow of 1 ml/min. After wash to baseline, with buffer A, the column was eluted with a Tris/HCl buffer, pH 7.5, containing 1 M NaCl (buffer B) , the elution gradient was 0-50% buffer B in 1 hour. After 36 min. a peak complex showed up, 1 ml fractions were picked up and the first 10 fractions showed cellulase activity on CMC/Agarose/congo-red plates. These fractions were pooled and concentrated, by ultrafiltration on AMICON cells using a DOW membrane GR61PP with cut-off 20 kD, to 3 ml. This sample was applied to a HiLoad 26/60 Superdex 75™ prep grade Pharmacia column, equilibrated with 100 mM Na- Acetate buffer, pH 6.35, and a 1 ml/min flow. After 82 min. a peak showed up, 1 ml fractions were picked up and the first 10 fractions showed cellulase activity on CMC/Agarose/congo-red plates. These fractions were pooled and the following results were obtained: A 280 =0.15 MW(SDS)=22 kD pl=3.5 - 5 Purity on SDS-PAGE =100% S-CEVU/ml=28.5 S-CEVU/A 280 =188 S-CEVU/mg=436 Extinction coefficient=54880 (calculated) Mw(calculated)=22 kD The Extinction coefficient is based on the content of tyrosine, tryptophane and cystein calculated from the sequence of the enclosed SEQ ID No. 1 (the amino acid sequence) . SDS-Page was performed on NOVEX Pre-Cast Gels 4-20% Tris-Glycine Gel 1.0 mm x 10 Well IEF was performed on Pharmacia PAGplate pH 3.5 - 9.5, the activity was visualized by CMC-Congored overlaying. Determination of K M & k..,: k_. and k,,, was determined in the same manner as the determination of SAVI Units at pH 8.5 with a substrate concentration up to 8 g/1. The following results were obtained: k^ 38 per sec. *_. 5 g/1, phosporic acid swollen cellulose, pH 8.5, Specific activity on CMC at pH 7.5: 436 S-CEVU per mg protein. D. Determination of pH and temperature profile of the endoglucanase from M. thermophila The pH profile was determined at the following conditions: Buffers of pH values between 2.5 and 10.0 were made by mixing O.IM Tri-sodium phosphate with O.IM citric acid. Purified endoglucanase was diluted to ensure the assay response to be within the linear range of the assay. The substrate was a 0.4% suspension of AZCL-HE-cellulose (MegaZyme) mixed 1:1 with the citrate/phosphate buffer to a final substrate concentration of 0.2% AZCL-HE- cellulose. 1 ml substrate in Eppendorf® 1.5ml polypropylene tubes were added 10 μl of enzyme solution and incubated for 15 minutes in Eppendorf® temperature controlled Thermomixers before heat-inactivation of enzymes for 20 minutes at 95°C in a separate Thermomixer. The tubes were centrifuged and 200 μl of each supernatant was transferred to a well in a 96 well microtiter plate and OD was measured at 620nm in an ELISA reader (Labsystems Multiskan® MCC/340) . For the pH optimum incubations took place at 30°C. For each pH value, three tubes were added enzyme and incubated before heat-inactivation, whereas one tube (the blank) was added enzyme and heat-inactivated immediately. The mean value of the three incubated samples was calculated and the blank value was substracted. The following pH profile was determined: It is seen that the endoglucanase has more than 60% activity between pH 4.0 and 8.0 and optimal activity at pH 5.0-6.0. Temperature profile: The temperature optimum was determined in the same manner at pH 5.5. The temperatures ranged from 30°C to 80°C For each temperature three incubations were carried out and the mean calculated. Three blanks were produced by immediate heat-inactivation of enzyme and the mean was subtracted from the incubated sample values. It is seen that the endoglucanase has optimal activity at 50-70°C The temperature stability was determined in the same manner at pH 5.5 and 30°C, and, further, the enzyme solu¬ tions were preheated for 1 hour at the actual temperature and cooled on ice. The residual activity is shown below in % of the activity of a non-preheated enzyme sample: E. Color clarification of Myceliophthora cellulase (SEQ ID Mo. 1) Measured as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers Apparatus Terg-o-tometer Liquid volume 100 ml Agitation 150 movements/min with vertical stirrer Rinse time 5 min in tapwater Washing temp 40 * Washing liqour 0.05 M phosphate buffer PH 7.0 Washing time 30 min Repetitions 2 Enzymes Myceliophthora SEQ ID No. IB Dosage 500 and 2500 S-CEVU/1 Textile 2 swatches of aged black 100% cotton 5x6 cm (0.9 gram) Drying Tumble dry Evaluation The light remission is measured by a Datacolor Elrepho Remission spectrophotometer. Remission is calculated as delta L (Hunter Lab- values) . When the surface fibrils and fibers protruding from the yarn are removed by the cellulase, the surface of the black fabric appears darker, and lower L values are obtained. The sample is compared with a blind sample, i washed without enzyme: No cellulase 500 ECU/1 2500 ECU/1 0.00 -1.41 -1.91 Delta L-values compared to blind sample, The data shows that Myceliophthora cellulase without CBD gives good color clarification under the conditions tested. F. Construction of the gene fusions between the endoglucanase from Myceliophthora thermophila and the 43kD endoglucanase from Humicola insolens The purpose of the two constructions was to make derivatives of the endoglucanase from M. thermophila with the linker and CBD from the 43kD endoglucanase from H. insolens (disclosed in WO 91/17243) . The native endoglucanase from M . thermophila do not have a linker and/or a cellulose binding domain, CBD. CM1: Construction 1 consist of the endoglucanase from M.thermophila (225 amino acids) and the 72 C-terminal amino acids from the H. insolens 43kD endoglucanase. CM2: Construction 2 consist of the endoglucanase from M.thermophila (225 amino acids) and the 83 C-terminal amino acids from the H. insolens 43kD endoglucanase. The 43kD endoglucanase cDNA from H. insolens was cloned into pHD414 in such a way that the endoglucanase gene was transcribed from the Taka-promoter. The resulting plasmid was named pCaHj418. In a similar way the cDNA encoding the endoglucanase from M. thermophila was cloned into pHD414 and the resulting plasmid was named pA2C193. Primers: primer 1: 5'- CGGAGCTCACGTCCAAGAGCGGCTGCTCCCGTCCCTCCAGCAGCACCAGCTCTCCGG -3' primer 2: 5' CCGGAGAGCTGGTGCTGCTGGAGGGACGGGAGCAGCCGCTCTTGGACGTGAGCTCCG -3' primer 3: 5'- CGGAGCTCACGTCCAAGAGCGGCTGCTCCCGTAACGACGACGGCAACTTCCCTGCCG -3' primer 4: 5'- CGGCAGGGAAGTTGCCGTCGTCGTTACGGGAGCAGCCGCTCTTGGACGTGAGCTCCG -3' Taka-pro. primer: 5' CAACATCACATCAAGCTCTCC -3' AMG-term. primer: 5' CCCCATCCTTTAACTATAGCG -3' The endoglucanase fusions were constructed by the PCR overlap-extension method as described by Higuchi et al. 1988. Construction 1: Reaction A: The Polymerase Chain Reaction (PCR) was used to amplify the fragment of pCaHj418 between primer 1 and AMG-term. primer (the linker and CBD from the 43kD endoglucanase from H.insolens). Reaction B: PCR amplification of the fragment between Taka-pro. primer and primer 2 in pA2C193, the endoglucanase gene from M.thermophila. Reaction C: The two purified fragments were used in a third PCR in the presence of the primers flanking the total region, i.e. Taka-pro. primer and AMG-term. primer. Construction 2: The same procedure was used where primer 3 and primer 4 had replaced respectively primer 1 and primer 2. The fragment amplified in reaction C was purified, digested with restriction enzymes Xba I and BsstE II. The purified digested fragment was ligated into pA2C193 digested with restriction enzymes Xba I and BsstE II. Competent cells from E. coli strain DH5otF' (New England Biolabs.) were transformed with the ligated plasmid and colonies containing the gene fusion were isolated. The sequence of the cloned part was verified by DNA sequencing. The sequence of the gene in the two constructs are shown in SEQ ID No. 2A and SEQ ID No. 3A. Polymerase Chain Reactions were carried out under standard conditions, as recommended by Perkin-Elmer. Reaction A and B started with 2 min. at 94°C followed by 20 cycles of (30 sec. at 94°C, 30 sec. at 50°C and 1 min. at 72°C) and end with 4 min. at 72 °C Reaction C started with (2 min. at 94°C, 1 min. at 52°C and 2 min. at 72 β C) , followed by 15 cycles of (30 sec. at 94°C, 30 sec. at 52°C and 90 sec. at 72°C) and end with 4 min. at 72°C The two constructs were transformed into Aspergillus ory- zae as described above. G. Purification and characterisation of cloned cellulases vith cellulose binding domains: The cloned product is recovered after fermentation by separation of the extracellular fluid from the production organism. About one gram of cellulase is then highly purified by affinity chromatography using 150 gram of Avicel in a slurry with 20 mm Sodium- phosphate pH 7.5. The Avicel is mixed with the crude fermentation broth which contain total about 1 gram of .cellulase. After mixing at 4 C for 20 min the Avicel enzyme is packed into a column with a dimension of 50 times 200 mm about 400 ml total. The column is washed with the 200 ml buffer, then washed with 0.5 M NaCl in the same buffer until no more protein elutes. Then washed with 500 ml 20 mm Tris pH 8.5. Finally the pure full length enzyme is eluted with 1% triethylamine pH 11.8. The eluted enzyme solution is adjusted to pH 8 and concentrated using a Amicon cell unit with a membrane DOW GR61PP (polypropylene with a cut off of 20 KD) to above 5 mg protein per ml. The purified cellulases were characterised as follow: Mw pi Molar E.280 S-CEVU per SDS-PAGE A.280 Myceliophthora (SEQ ID No.2) 43 kD 4 74.950 135 Acremonium (SEQ ID No.5) 40 kD 5 68.020 185 Thielavia (SEQ ID No.9) 35 kD 4.3 52.470 75 pH N-terminal Termo- Activity stability above 50% DSC Myceliophthora (SEQ ID No.2) 5.0-9.0 Blocked. 80°C Acremonium (SEQ ID No.5) 6.0-9.5 Blocked. 61°C Thielavia (SEQ ID No.9) 5.0-9.0 ASGSG 83°C The purified cellulases was analysed for MW by SDS-PAGE and using standard LMW protein marker kit from Pharmacia the MW was calculated for the cellulases. The MW is apparently higher than the MW of the composition of the coding a in acids and is due to the fact the linker region are O-glycosylated resulting in this higher MW. The pi was determined using a Pharmacia Ampholine PAG plates pH 3.5 to 9.5 and again using a Pharmacia kit with known pi proteins. The molar extinction coefficient was calculated based on the amin acids composition using the known absorbance of Tryptophan, Tyrosine and Cystein. pH activity profile was obtained using CMC substrate, incubation for 20 min at 40° C at a 0.5 pH interval and measuring the formation of reducing sugars. The relative activity at the different pH was calculated and the table contain the interval with more than 50% relative activity has been measured. The N-terminal was determined for the purified cellulase using a Applied Biosystems model 473A sequencer. The protein sequenceer was run according to the manufacturer instructions. Two of the cellulases were blocked, this is due to the N- terminal glutamine which form a pyroglutamate which can not be detected and which block for further sequencing. DSC Differential scanning calometry was done at neutral pH (7.0) using a MicroCalc Inc. MC calorimeter with a constant scan rate and raising the temperature from 20 to 90° at a rate of 90° per hour. Raising antibody. The cellulases from Myceliophthora, Acremonium and Thielavia were used for raising antibody in rabits. 0.1 mg of the purified cellulase in 0.9 % NaCl solution mixed with Freunds adjuvant immediately prior to injection. The rabits were immunized 10 times with one week interval. The immunoglobulin G fraction (IgG) was purified by ammonium sulfate precipitation (25% saturation) . the precipitate was solubilized in water and then dialyzed extensively against sodium acetate buffer (pH 5.0, 50 mM) altering with deionized water. After filtration, the IgG fraction was stabilized with sodium azide (0.01%) . Using immunodiffusion in agar plates all three cellulases form a single immunoprecipitate with its homologous antiserum and no precipitate was seen between the 3 cloned cellulases and the sera raised against the other two cellulases. H-I. Performance of endoglucanase of construction 1 (SEQ ID Mo. 2) measured in buffer as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers Apparatus Terg-o-tometer Liquid volume 100 ml Agitation 150 movements/min (rpm) Rinse time 5 min in tap water Washing temp 40 * C Water Hardness 1 mM CaCl 2 Washing liquor 0.05 M phosphate buffer PH 7.0 Washing time 30 min Repetitions 2 Textile 2 swatches of aged black, 100% cotton 5x6 cm Drying Tumble dry Evaluation: The light remission was measured by a Macbeth Color Eye 7000 Remission spectrophotometer. Remission is calculated as delta L (Hunter Lab-values) . When the surface fibrils and fibers protruding from the yarn were removed by the cellulase, the surface appeared more bright, and lower L values were obtained. Results: The data show that the enzyme of the invention gives very good color clarification under the conditions tested. H-II. Performance of cloned endoglucanase from Thielavia terrestris (SEQ ID Mo.9) in buffer measured as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers Apparatus Terg-o-tometer Liquid volume 100 ml Agitation 150 movements/min with vertical stirrer Rinse time 10 min in tapwater Washing temp 40 * Washing liqour 0.05 M phosphate buffer. pH 7.0 Washing time 30 min Repetitions 2 Textile 2 swatches of aged black cotton 5x6 cm (app. 150 g/m2) Drying : Tumble dry Evaluation : The light remission was measured by a Datacolor Elrepho Remission spectrophotometer. Remission is calculated as delta L (Hunter Lab-values) . When the surface fibrils and fibers protruding from the yarn are removed by the cellulase, the surface of the black fabric appears darker and nicer, and lower L values are obtained. Results: The data show that the cellulase gives good color clarification under the conditions tested. H-III. Performance of endoglucanase of Volutella colletrichoides (SEQ ID Mo. 17) measured in buffer as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers Apparatus Terg-o-tometer Liquid volume 100 ml Agitation 150 movements/min with vertical stirrer Rinse time 5 min in tapwater Washing temp 40 * Washing liqour 0.05 M phosphate buffer PH 7.0 Washing time 30 min Repetitions 2 Dosage 2.5 S-CEVU/ml Textile 2 swatches of aged black 100% cotton 5x6 cm (0.9 gram) Drying : Tumble dry Evaluation: The light remission is measured by a Datacolor Elrepho Remission spectrophotometer. Remission is calculated as delta L (Hunter Lab-values) . When the surface fibrils and fibers protruding from the yarn are removed by the cellulase, the surface of the black fabric appears darker, and lower L values are obtained. The sample is compared with a blind sample, i.e. washed without enzyme: No cellulase With cellulase 0.00 -0.57 Delta L remission values compared to blind sample. The data shows that the Volutella colletrichoides cellulase gives good color clarification under the conditions tested. H-IV. Performance of cloned cellulases from Thielavia terrestris and Acremonium sp. CBS 478.94 in high pH heavy duty detergent measured as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers Evaluation : The light remission is measured by a Datacolor Elrepho Remission spectrophotometer. Remission is calculated as delta L (Hunter Lab-values) . When the surface fibrils and fibers protruding from the yarn are removed by the cellulase, the surface of the black fabric appears darker and nicer, and lower L values are obtained. Different dosages of cloned cellulases from Thielavia terreεtriε (SEQ ID No. 9) and Acremonium εp . CBS 478.94 (SEQ ID No.5), respectively, (denoted A and B, respectively) were tested. Results : The data show that both cellulases gives good color clarification under the conditions tested. H-V. Performance of cellulases cloned from Thielavia terrestris and Acremonium sp. CBS 478.94, and construction 1 (SEQ ID Mo.2) measured as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers Apparatus Terg-o-tometer Liquid volume 150 ml Agitation 150 movements/min with vertical stirrer Rinse time 10 min in tapwater Washing temp 35'C Hardness 1.0 mM CaCl2 0.34 mM MgC12 Washing liqour 2.0 g/1 HDL (neutral, citrate built HDL, with nonionic/anionic weight ra¬ tion > 0.5) PH 7.5 Washing time 30 min Repetitions 2 Textile 2 swatches of aged black cotton 5x6 cm (app. 150 g/m2) 2 swatches of heavy knitted cotton 4x7 cm (app. 600 g/m2) Drying : Tumble dry Evaluation : The light remission is measured by a Datacolor Elrepho Remission spectrophotometer. Remission is calculated as delta L (CIE Lab-values) . When the surface fibrils and fibers protruding from the yarn are removed by the cellulase, the surface of the black fabric appears darker and nicer, and lower L values are obtained. Three different dosages Different dosages of cloned cellulases from Thielavia terrestris (SEQ ID No. 9) and Acremonium sp. CBS 478.94 (SEQ ID No.5) and the construction 1 (SEQ ID No.2), respectively, (denoted A and B and C, respectively) were tested. Results: The data show that all cellulases gives very good color clarification under the conditions tested. I. Application of endoglucanases from Thielavia terre¬ stris, Acremonium sp. and construction 1 (SEQ ID Mo. 2) in denim finishing Experimental Apparatus: Washing machine Wascator FL 120 Liquid volume: 20 L Fabric: 1.1 kg denim fabric, 14 oz 100 % cotton Desizing: 10 min, 55 * C, pH 7 50 ml Aquazyme 120L 2.5 g/1 Phosphate buffer Abrasion: 2 hours; pH and temperature varied according to the following table: Enzyme Activity pH/temp Buffer system SEQ ID No. 2 1400 S-CEVU/g 6/55 * C 2.5 g/1 phosphate buffer No. 9 292 S-CEVU/g 5/65 * C 1 g/1 citrate buffer No. 5 782 S-CEVU/g 7/45 * C 2.5 g/1 phosphate buffer Inactivation: 15 min, 80"C 1 g/1 sodium carbonate Rinses: Three rinse cycles of 5 min in cold tap water Evaluation: Abrasion : The remission from the fabric was determined at 420 nm using a Texflash 2000 as a measure of the abrasion level. The results from the treatment of the denim fabric with different endoglucanases of the invention is shown in the following table: All tested cellulases show excellent performance in denim finishing, although each enzyme is unique in its own way. When applying the enzyme corresponding to SEQ ID No. 2 for denim finishing it is possible to reach a high abrasion level with a minimum of strength loss. When treating denim with the enzyme corresponding to SEQ ifD No. 9, a very high wash down can be reached which leaves the fabric with an almost bleached appearance. Denim finishing with the enzyme corresponding to SEQ ID No. 5 gives a high abrasion level at a low temperature optimum which makes it possible to reduce the processing tempera¬ ture and save energy. J. Use of cloned cellulases from Acremonium sp. and Thie¬ lavia terrestris for Biopolishing of lyocell fibers Lyocell fibers which are sold under the trade name Tencel are spun from wood pulp cellulose in a more environmentally friendly waterbased solvent than is the case for normal viscose production) . However, the fibers have a tendency to fibrillate when they are processed into textiles which is seen on the surface and denoted "fuzz". By using cellulases it is possible to permanently remove the exposed and fuzzy fibers and significantly improve the look of the finished fabric, the treatment generally known as Biopolishing. The endoglucanases of the present invention are especially suited for the removal of Lyocell surface fibers. MATERIALS AND METHODS The textile substrate was either 100 % woven or different kinds of jersey knitted dark blue Tencel. The dark colour and jersey knit was preferred in order to enhance the visual effects which simplifed the evaluation. A woven 70/30 Tencel/Rayon blend was also used to a lesser extent. The assays were either performed in 200 ml scale using a Launder-o-meter or in the 20 1 scale using a Wascator. The treatment time was 60min at 55° C in Wascator and 60- 90 min in LOM. The buffer was 2 g/1 sodium acetate adjusted to pH 5 with acetic acid. The fabric to liquid ratio was 1:10 but in the Launder-o-meter 20 steel balls with a diameter of 14 mm (11 g each) was used to obtain sufficient mechanical abrasion. The biopolishing was immediately followed by inactivation using 2 g/lit sodium carbonate at 80° C for 15 min followed by rinsing in cold water. The results were evaluated using a fuzz note scale from 1 - 5 were 1 is the fibrillated look of the starting material and 5 is a high quality look with no visible fibers on the surface. Since the performance of endocellulases is specific towards a surface treatment the weightloss is below 2 % and is therefore not included in the evaluation. Two cellulases were evaluated: the cellulases cloned from Acremonium sp. (SEQ ID No. 5) and from Thielavia terrestris (SEQ ID No. 9) . The two cellulases are able to defibrillate both Tencel and Tencel blended fabrics. By using an endoglucanase of the invention, only small fibrils are removed rather than whole fibers such as is the case when using acid cellulase mixtures from Trichoderma . The strength loss of the treated fabric is threrefore kept at a minimum when using endoglucanases of the present invention. The following dosages gave a superior defibrillation, i.e. fuzz note 4 or above: 15 S-CEVU/g fabric of cellulase from Acremonium sp (SEQ ID No. 5) ; and 10 S-CEVU/g fabric of cellulase from Thelavia terrestriε (SEQ ID No.9) . EXAMPLE 2 λ new cellulytic enzyme was by expression cloning as well as by PCR cloning detected to be produced by a plant pat¬ hogen, isolated from soy bean seeds and identified as Ma- crophomina phaseolina. Production of biomass for PCR and expression cloning procedures: Isolate CBS 281.96 was grown in shake flask cultures on cellulose enriched potato dextrose broth, incubated for 5 days at 260C (shaking conditions: 150 rpm) . λ. Cloning and expression of an endoglucanase from Macrophomina phaseolina mRNA was isolated from Macrophomina phaseolina , grown in a cellulose-containing fermentation medium with agitation to ensure sufficient aeration. Mycelia were harvested after 3-5 days' growth, immediately frozen in liquid nitrogen and stored at -80°C A library from Macrophomina phaseolina , consisting of approx. 10 6 individual clones was constructed in E. coli as described with a vector background of 1%. Plasmid DNA from some of the pools was transformed into yeast, and 50-100 plates containing 250-400 yeast colonies were obtained from each pool. Endoglucanase-positive colonies were identified and isolated on SC-agar plates with the AZCL HE cellulose assay. cDNA inserts were amplified directly from the yeast colonies and characterized as described in the Materials and Methods section above. The DNA sequence of the cDNA encoding the endoglucanase is shown in SEQ ID No. 10 and the corresponding amino acid sequence is shown in SEQ ID No. 11. The cDNA is obtainable from the plasmid in DSM 10512. Total DNA was isolated from a yeast colony and plasmid DNA was rescued by transformation of ϋ". coli as described above. In order to express the endoglucanse in Aspergillus , the DNA was digested with appropriate restriction enzymes, size fractionated on gel, and a fragment corresponding to the endoglucanase gene was purified. The gene was subsequently ligated to pHD414, digested with appropriate restriction enzymes, resulting in the plasmid pA2C477. After amplification of the DNA in E . coli the plasmid was transformed into Aspergillus oryzae as described above. Screening of the cDNA library by hybridization and characterization of the positive clones. Approximately 6000 colony forming units (c.f.u.) from the Macrophomina phaseolina cDNA library in E. coli was screened by colony hybridization using a random-primed 32 P-labeled PCR product from M. phaseolina as probe. The PCR product was generated as described in the Materials and methods section. The positive cDNA clones were characterized by sequencing the ends of the cDNA inserts, and by determining the nucleotide seuence of the longest cDNA from both strands. The DNA sequence of the cDNA encoding the endoglucanase is shown in SEQ ID No. 10 and the corresponding amino acid sequence is shown in SEQ ID No. 11. B. Construction of gene fusion between the endoglucanase from Macrophomina phaseolina and the 43 kD endoglucanase from Humicola insolens One construction was prepared in order to make a derivative of the endoglucanase from M . phaseolina with the linker and CBD from the 43 kD endoglucanase from H . insolens (disclosed in WO 91/17243) . The native endoglucanase from M . phaseolina does not have a linker and/or a cellulose binding domain, CBD. The construction consists of the endoglucanase from M . phaseolina (223 amino acids) and the 72 C-terminal amino acids from the H. insolenε 43 kD endoglucanase. The 43 kD endoglucanase cDNA from H . inεolenε is cloned into pHD414 in such a way that the endoglucanase gene is transcribed from the Taka-promoter. The resulting plasmid is named pCaHj418. The cDNA encoding the endoglucanase from M . phaεeolina is cloned into pYES2.0 as a BstX I/Not I fragment and the resulting plasmid is named pClC477. Primers: primer l: 5'- GGTCGCCCGGACTGGCTGTTCCCGTACCCCCTCCAGCAGCACCAGCTCTCCGG -3' primer 2: 5' CCGGAGAGCTGGTGCTGCTGGAGGGGGTACGGGAACAGCCAGTCCGGGCGACC -3' PYES2.0 F.HT primer: 5' CGGACTACTAGCAGCTGTAATACG -3' AMG-term. primer: 5' CCCCATCCTTTAACTATAGCG -3' The endoglucanase fusion is constructed by the PCR overlap-extension method as described by Higuchi et al. 1988. Reaction A: The Polymerase Chain Reaction (PCR) is used to amplify the fragment of pCaHj418 between primer 1 and AMG-term. primer (the linker and CBD from the 43 kD endoglucanase from H. insolens) . Reaction B: PCR amplification of the fragment between PYES2.0 F.HT primer and primer 2 in pClC477, the endoglucanase gene from M . phaseolina . Reaction C: The two purified fragments are used in a third PCR in the presence of the primers flanking the total region, i.e. pYES2.0 F.HT primer and AMG-term. primer. The fragment amplified in reaction C is purified, digested with restriction enzymes, e.g. Xba I and BamH I. The purified digested fragment is ligated into pHD414 digested with restriction enzymes, e.g. Xba I and BamH I. Competent cells from E . coli strain DH5αF' (New England Biolabs) are transformed with the ligated plasmid and colonies containing the gene fusion are isolated. The sequence of the cloned part was verified by DNA sequen- cing. Polymerase Chain Reactions are carried out under standard conditions, as recommended by Perkin-Elmer. Reaction A and B start with 2 min. at 94°C followed by 20 cycles of (30 sec. at 94°C, 30 sec. at 52°C and 1 min. at 72 β C) and ends with 4 min. at 72 °C Reaction C starts with (2 min. at 94°C, 1 min. at 52°C and 2 min. at 72°C) , followed by 20 cycles of (30 sec. at 94°C, 30 sec. at 52°C and 90 sec. at 72°C) and ends with 4 min. at 72 β C The construct may be transformed into Aspergillus oryzae as described above. EXAMPLE 3 Cloning and expression of an endoglucanase from Acremonium sp. and Sordaria fimicola Production of biomass for expression cloning procedures: Isolates CBS 478.94 and ATCC 52644, respectively, were grown in shake flask cultures on cellulose enriched pota¬ to dextrose broth, incubated for 5 days at 260C (shaking conditions: 150 rpm) . mRNA was isolated from Acremonium sp. , CBS 478.94, and Sordaria fimicola , ATCC 52644, respectively, grown in a cellulose-containing fermentation medium with agitation to ensure sufficient aeration. Mycelia were harvested after 3-5 days' growth, immediately frozen in liquid nitrogen and stored at -80°C Libraries from Acremonium sp. , and Sordaria fimicola , respectively, each consisting of approx. 10 6 individual clones were constructed in E . coli as described with a vector background of 1%. Plasmid DNA from some of the pools from each library was transformed into yeast, and 50-100 plates containing 250- 400 yeast colonies were obtained from each pool. Endoglucanase-positive colonies were identified and isolated on SC-agar plates with the AZCL HE cellulose assay. cDNA inserts were amplified directly from the yeast colonies and characterized as described in the Materials and Methods section above. The DNA sequence of the cDNA encoding the endoglucanase from Acremonium sp. is shown in SEQ ID No. 6 and the corresponding amino acid sequence is shown in SEQ ID No.7. The cDNA is obtainable from the plasmid in DSM 10080. The partial DNA sequence of the cDNA encoding the endoglucanase from Sordaria fimicola is shown in SEQ ID No. 19 (Nucleotide sequence of the 5'-end of the cDNA) and the corresponding amino acid sequence is shown in SEQ ID No. 20. The cDNA is obtainable from the plasmid in DSM 10576. Total DNA was isolated from a yeast colony and plasmid DNA was rescued by transformation of E. coli as described above. In order to express the endoglucanase in Aspergillus , the DNA was digested with appropriate restriction enzymes, size fractionated on gel, and a fragment corresponding to the endoglucanase gene from Acremonium sp. and Sordaria fimicola , respectively, was purified. The genes were subsequently ligated to pHD414, digested with appropriate restriction enzymes, resulting in the plasmids pA2C371 and pA2C502, respectively. After amplification of the DNA in E. coli the plasmids were transformed into Aspergilluε oryzae as described above. EXAMPLE 4 A. Cloning by PCR an endoglucanase from Crinipellis sca¬ bella. CBS 280.96 Isolate CBS 280.96 was grown in static flask cultures, holding wheat bran medium (per flask: 300g wheat bran added 450 ml salt solution) , incubated for 6 days at 26C. After incubation the wheat bran was extracted with destilled water (300ml per flask) and the extract tested for endoglucanase activity (0.1% AZCL-HE-Cellulose (megazyme) in 1% agarose (Litex agarose, Medinova) . Activity was observed on the plates holding pH of 3.0, 7.0 and 9.5. mRNA was isolated from Crinipellis scabella grown as describe above. Mycelia were harvested after 3-5 days' growth, immediately frozen in liquid nitrogen and stored at -80°C A library from Crinipellis scabella , consisting of approx. 10 6 individual clones was constructed in E. coli as described with a vector background of 1%. Approximately 10 000 colony forming units (c.f.u.) from the Crinipellis scabella cDNA library in E. coli was screened by colony hybridization using a random-primed 3 P-labeled PCR product from C. scabella as probe. The PCR product was generated as described in the Materials and methods section. The positive cDNA clones were characterized by sequencing the ends of the cDNA inserts, and by determining the nucleotide seuence of the longest cDNA from both strands. The DNA sequence of the cDNA encoding the endoglucanase is shown in SEQ ID No. 12 and the corresponding amino acid sequence is shown in SEQ ID No. 13. The cDNA is obtainable from the plasmid in DSM 10511. Total DNA was isolated from a yeast colony and plasmid DNA was rescued by transformation of E. coli as described above. In order to express the endoglucanse in Aspergillus, the DNA was digested with appropriate restriction enzymes, size fractionated on gel, and a fragment corresponding to the endoglucanase gene was purified. The gene was subsequently ligated to pHD414, digested with appropriate restriction enzymes, resulting in the plasmid pA2C475. After amplification of the DNA in E. coli the plasmid was transformed into Aspergillus oryzae as described above. Construction of two gene fusions between the endoglucanase from Crinipellis scabella and the linker/CBD region of the 43 kDa endoglucanase from Humicola insolens. The native endoglucanase from Crinipellis scabella neit¬ her has a linker nor a cellulose binding domain (CBD) . In addition, the full-length cDNA contains an ATG start codon upstream from the endoglucanase encoding open reading frame (ORF) , presumably resulting in scrambled translation initiation upon heterologous expression of the cDNA, such as in the yeast Saccharomyces cereviεiae and the filamentous fungus Aspergillus oryzae . Thus, two gene fusions between the endoglucanase from Crinipellis scabella and the linker/CBD region of the 43kD endoglucanase from Humicola insolens (disclosed in WO 91/17243) has been constructed using splicing by overlap extension (SOE) (Horton et al, 1989) . Construction 1 consists of the cDNA encoding the 226-re- sidue endoglucanase from C. scabella fused by PCR with the 3'-end cDNA of H . insolenε coding for the linker and CBD region (72 amino acids) at the COOH-terminus of the H. insolens 43kD endoglucanase. The second hybrid construct is identical to the abovementioned gene fusion, except that the first five residues from the putative signal peptide have been deleted by PCR resulting in a shorter signal, which starts with the second in-frame ATG start codon. Plasmid constructs The plasmid pClC475 contains the full-length cDNA from C. scabella , cloned into BstXI/Notl-cut yeast expression vector pYES 2.0, the plasmid pClC144 contains the full-length cDNA from H . insolens , cloned into the BstXI site of pYES 2.0. Splicing by overlap extension Two PCR fragments encoding the core region of the endog- lucanase from C. scabella were generated in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 mM MgCl 2 , 0.01 % gelatin; containing 200 μK each dNTP) , using 50-100 ng of PC1C475 as template, and 250 pmol of the reverse primer (5'-GACCGGAGAGCTGGTGCTGCTGGAGGGTTTACGAACACAGCCCGAGATATTAG TG- 3') in two combinations with 300-350 pmol of each forward primer (forward no. 1 5'- CCCCAAGCTTGACTTGGAACCAATGGTCCATCC-3' , forward no. 2 5'- CCCCAAGCTTCCATCCAAACATGCTTAAAACGCTCG- 3' ) , a DNA thermal cycler (Landgraf, Germany) and 2.5 units of Taq polymerase (Perkin-Elmer, Cetus, USA) . Thirty cycles of PCR were performed using a cycle profile of denaturation at 94 °C for 1 min, annealing at 55 °C for 2 min, and extension at 72 °C for 3 min. The PCR fragment coding for the linker and CBD of the endoglucanase of H . insolenε was generated in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 mM MgCl 2 , 0.01 % gelatin; containing 200 μM each dNTP) using 100 ng of the pClC144 template, 250 pmol forward primer (5'-CACTAATATCTCGGGC- TGTGTTCGTAAACCCTCCAGCAGCACCA-GCTCTCCGGTC-3' ) , 250 pmol of the pYES 2.0 reverse primer (5'-GGGCGTGAATGTAAGCGTGACATA-3') a DNA thermal cycler (Landgraf, Germany) and 2.5 units of Taq polymerase (Perkin-Elmer, USA) . Thirty cycles of PCR were performed as above. The PCR products were electrophoresed in 0.7 % low gelling temperature agarose gels (SeaPlaque, FMC) , the fragments of interest were excised from the gel and recovered by treatment with agarase (New England Biolabs, USA) according to the manufacturer's instructions, followed by phenol extraction and ethanol precipitation at - 20 °C for 12 h by adding 2 vols of 96 % EtOH and 0.1 vol of 3M NaAc. The recombinant hybrid genes between the endoglucanase from Crinipelliε scabella and the linker/CBD region of the 43 kD endoglucanase from Humicola insolenε were generated by combining the overlapping PCR fragments from above (ca. 50 ng of each template) in two combinations in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 mM MgCl 2 , 0.01 % gelatin; containing 200 μM each dNTP). The SOE reaction was carried out using the DNA thermal cycler (Landgraf, Germany) and 2.5 units of Taq polymerase (Perkin-Elmer, Cetus, USA) . Two cycles of PCR were performed using a cycle profile of denaturation at 94 °C for 1 min, annealing at 55 °C for 2 min, and extension at 72 °C for 3 min, the reaction was stopped, 250 pmol of each end-primer (forward no. 1 5'-CCCCAAGCTTGACTTGGAACCAATGGTCCATCC-3 ' , forward no. 2 5'-CCCCAAGCTTCCATCCAAACATGCTTAAAACGCTCG-3' . reverse primer 5'-GGGCGTGAATGTAAGCGTGACATA-3 ') was added to the reaction mixture, and an additional 30 cycles of PCR were performed using a cycle profile of denaturation at 94 °C for 1 min, annealing at 55 °C for 2 min, and extension at 72 °C for 3 min. Construction of the expression cassettes for heterologous expression in Aspergillus oryzae The PCR-generated, recombinant fragments were electrophoresed in a 0.7 % low gelling temperature agarose gel (SeaPlaque, FMC) , the fragments of interest were excised from the gel and recovered by treatment with agarase (New England Biolabs, USA) according to the manufacturer's instructions, followed by phenol extraction and ethanol precipitation at - 20 °C for 12 h. The DNA fragments were digested to completion with Hindlll and Xbal, and ligated into Hindlll/Xbal-cleaved pHD414 vector followed by electroporation of the constructs into E. coli DH10B cells according to the manufacturer's instructions (Life Technologies, USA). The nucleotide sequence of the resulting gene fusions were determined from both strands as described in the Materials and methods section, SEQ ID no. 14A and 15A. The constructs may be transformed into A . oryzae as described. EXAMPLE 5 PCR facilitated detection of said type of cellulytic en¬ zyme from 46 filamentous and monocentric fungi, representing 32 genera, from 23 families, belonging to 15 orders of 7 classes, covering all in all all four groups of the true Fungi: Ascomycetous, Basidiomycetous, Chytri- dio ycetous and Zygomycetous fungi 5.1 Materials 1.Diplodia gossypina Cooke Deposit of Strain, Ace No: CBS 274.96 2.Ulospora bilgramii (Hawksw. et al.) Hawksw. et al, Ace No of strain: NKBC 1444, 3. Microsphaeropsis sp 4. Ascobolus stictoideus Speg. Ace No of strain: Q026 (Novo Nordisk collection) Isolated from goose dung, Svalbard, Norway 5. Saccobolus dilutellus (Fuck) Sacc. Deposit of strain: Ace No CBS 275.96 6. Penicillium verruculosum Peyronel Ex on Ace No of species: ATCC 62396 7. Penicillium chrysogenum Thorn Ace No of Strain: ATCC 9480 8. Thermomyces verrucosus Pugh et al Deposit of Strain, Ace No.: CBS 285.96 9. Xylaria hypoxylon L. ex Greville Deposit of Strain, Ace No: CBS 284.96 10. Poronia punctata (Fr.ex L.) Fr. Ref:A.Munk: Danish Pyrenomycetes, Dansk Botanisk Arkiv, Voll7,l 1957 11. Nodulisporum sp Isolated from leaf of Camellia reticulata (Theaceae, Guttiferales) , Kunming Botanical Garden, Yunnan Province, China 12. Cylindrocarpon sp Isolated from marine sample, the Bahamas 13. Fusarium anguioides Sherbakoff Ace No of strain: IFO 4467 14. Fusarium poae (Peck) Wr. Ex on Ace No of species: ATCC 60883 15. Fusarium solani (Mart.)Sacc.emnd.Snyd & Hans. Ace No of strain: IMI 107.511 16. Fusarium oxysporum ssp lycopersici (Sacc.)Snyd. & Hans. Ace No of strain: CBS 645.78 17. Fusarium oxysporum ssp passiflora Ace No of strain: CBS 744.79 18. Gliocladium catenulatum Gillman & Abbott Ace. No. of strain: ATCC 10523 19. Nectria pinea Dingley Deposit of Strain, Ace. No. CBS 279.96 20. Sordaria macrospora Auerswald Ex on Ace No of species: ATCC 60255 21. Humicola grisea Traeen ex on Ace No for the species: ATCC 22726 22. Humicola nigrescens O vik Ace No of strain: CBS 819.73 23. Scytalidium thermophilum (Cooney et Emerson) Austwick Ace No of strain: ATCC 28085 24. Thielavia thermophila Fergus et Sinden (syn Corynascus thermophilus) ACC No Of strain: CBS 174.70, IMI 145.136 25. Cladorrhinum foeeundissimum Saecardo et Marchal Ex on Ace No of species: ATCC 62373 26. Syspastospora boninensis Ace No of strain: NKBC 1515 (Nippon University, profe Tubaki Collection) 27. Chaetomium cuniculorum Fuckel Ace. No. of strain: CBS 799.83 28. Chaetomium brasiliense Batista et Potual Ace No of strain: CBS 122.65 29. Chaetomium murorum Corda Ace No of strain: CBS 163.52 30. Chaetomium virescens (von Arx) Udagawa Ace.No. of strain: CBS 547.75 31. Nigrospora sp Deposit of strain. Ace No: CBS 272.96 32. Nigrospora sp Isolated from: 33. Diaporthe syngenesia Deposit of strain. Ace No: CBS 278.96 34. Colletotrichum lagenarium (Passerini) Ellis et Halsted syn Glomerella cingulata var orbiculare Jenkins et Winstead Ex on ace No of species: ATCC 52609 35. Exidia glandulosa Fr. Deposit of Strain, Ace No: CBS 277.96 36. Fomes fomentarius (L.) Fr. Deposit of strain: Ace No. CBS 276.96 37. Spongipellis (?) Deposit of Strain: Ace No CBS 283.96 38. Rhizophlyctis rosea (de Bary & Wor) Fischer Deposit of Strain: Ace No.: CBS 282.96 39. Rhizomucor pusillus (Lindt) Schipper syn: Mucor pusillus Ace No of strain: IFO 4578 40. Phycomyces nitens (Kunze) van Tieghem & Le Monnier Ace No of strain: IFO 4814 41 Chaetostylum fresenii van Tieghem & Le Monnier syn. Helicostylum fresenii Ace No of strain NRRL 2305 42. Trichothecium roseum. Ace No of strain: IFO 5372 43. Coniothecium sp Endophyte, isolated from leaf of flowering plant, Kunming , Yunnan, China 44. Deposit of strain. Ace No.: CBS 271.96 Coelomyeete, Isolated from leaf of Artoearpus altilis (Moraceae, Urticales) , Christiana, Jamaica 45. Deposit of strain. Ace No.: CBS 273.96 Coelomyeete, isolated from leaf of Pimenta dioica (Myrtaceae, Myrtales) , Dallas Mountain, Jamaica 46. Deposit of strain: CBS 270.96 Coelomyeete, isolated from leaf of Pseudocalymma alliaceum (Bignoniaeeae, Solanales) growing in Dallas Mountain, Jamaica 5.2 Procedure Maintenance of strains and production of biomass: The strains were maintained on agar in petrie dishes (9cm) or on slants (see list of Media: PCA and PDA) . 44 of the strains were grown in shake flasks under the following growth conditions: general fungal media as PC, PD and PB 9 or YPG (see list of media) ; incubation time from 3 to 9 days; temperature 26°C; rpm between 150 and 175 . Strain No 14 (F.poae) was grown on wheat bran for 15 days (26°C; static) . Strain No 38 was grown in dilute salt solution (DS/2) , added 1 cm 2 pieces of autoclaved filter paper. Activity test: Activity was tested on 0.1% AZCL-HE-Cellulose (Megazyme) plates (14 cm Petrie dishes) , made up in 1% agarose (HSB, Litex Agarose, Medinova) . All tests were done in triplicate, viz. AZCL-HE-Cellulose dissolved in three buffers, adjusted to pH 3, 7 or 9.5 (using various proportions of the following two ingredients Citric acid monohydrat, Merck art. No 100244 (21.0 g) dissolved in water, making a total of 1000 ml; 0.1M tri-Sodium dodeca- brohydrate, Merck art.no. 6578 (38 g) , dissolved in wa- ter, making a total of 1000 ml. The mixing is done immidiately before use. Harvesting of Biomass: The biomass was harvested by filtering (mesh adjusted to the growth of the fungus, the finest used for fungi which have highly sporulating mycelium as e.g. Fusarium spp.). The biomass on the filter was scraped into a sterile plastic bag and immidiately frozen (by submerging into liquid nitrogen) . 5. 3 Results I. Using the PCR screening and amplification techniques described in Materials and Methods the following partial cDNA sequences were obtained: Saccobolus dilutellus (Fuck) Sacc, CBS 275.96: SEQ ID No. 21 (and the deduced amino acid sequence in SEQ ID No. 22); Thermomyces verrucosus, CBS 285.96: SEQ ID No. 23 (and the deduced amino acid sequence in SEQ ID No. 24) ; Xylaria hypoxylon, CBS 284.96: SEQ ID No. 25 (and the deduced amino acid sequence in SEQ ID No. 26) ; Fusarium oxysporum ssp lycopersici, CBS 645.78: SEQ ID No. 27 (and the deduced amino acid sequence in SEQ ID No. 28) ; Nectria pinea, CBS 279.96: SEQ ID No. 29 (and the deduced amino acid sequence in SEQ ID No. 30) ; Humicola grisea, ATCC 22726: SEQ ID No. 31 (and the deduced amino acid sequence in SEQ ID No. 32) ; Humicola nigrescens, CBS 819.73: SEQ ID No. 33 (and the deduced amino acid sequence in SEQ ID No. 34) ; Cladorrhinum foeeundissimum, ATCC 62373: SEQ ID No. 35 (and the deduced amino acid sequence in SEQ ID No. 36) ; Syspastospora boninensis, NKBC 1515: SEQ ID No. 37 (and the deduced amino acid sequence in SEQ ID No. 38) ; Nigrospora sp. , CBS 272.96: SEQ ID No. 39 (and the deduced amino acid sequence in SEQ ID No. 40) ; Chaetostylum fresenii: SEQ ID No. 41 (and the deduced amino acid sequence in SEQ ID No. 42) ; Exidia glandulosa, CBS 277.96: SEQ ID No. 43 (and the deduced amino acid sequence in SEQ ID No. 44) ; Coniothecium sp. : SEQ ID No. 45 (and the deduced amino acid sequence in SEQ ID No. 46) ; Deposition No. CBS 271.96: SEQ ID No. 47 (and the deduced amino acid sequence in SEQ ID No. 48) ; Deposition No. CBS 270.96: SEQ ID No. 49 (and the deduced amino acid sequence in SEQ ID No. 50) ; Diplodia gossypina, CBS 274.96: SEQ ID No. 51 (and the deduced amino acid sequence in SEQ ID No. 52) ; Ulospora bilgramii, NKBC 1444: SEQ ID No. 53 (and the deduced amino acid sequence in SEQ ID No. 54) ; Penicillium verruculosum, ATCC 62396: SEQ ID No. 55 (and the deduced amino acid sequence in SEQ ID No. 56); Poronia punctata: SEQ ID No. 57 (and the deduced amino acid sequence in SEQ ID No. 58) ; Fusarium anguioides, IFO 4467: SEQ ID No. 59 (and the deduced amino acid sequence in SEQ ID No. 60) ; Thielavia thermophila, CBS 174.70: SEQ ID No. 61 (and the deduced amino acid sequence in SEQ ID No. 62) ; Chaetomium cuniculorum, CBS 799.83: SEQ ID No. 63 (and the deduced amino acid sequence in SEQ ID No. 64) ; Chaetomium virescens: SEQ ID No. 65 (and the deduced amino acid sequence in SEQ ID No. 66) ; Colletotrichum lagenarium: SEQ ID No. 67 (and the deduced amino acid sequence in SEQ ID No. 68) ; Phycomyces nitens: SEQ ID No. 69 (and the deduced amino acid sequence in SEQ ID No. 70) ; and Trichothecium roseum: SEQ ID No. 71 (and the deduced amino acid sequence in SEQ ID No. 72) ; II. Using the PCR screening and amplification techniques described in Materials and Methods partial cDNA encoding partially for the enzyme of the invention was obtained and the plasmid was deposited according to the Budapest Treaty: Eεcherichia coli , DSM 10583, deposition date 13 March, 1996; cDNA from Trichothecium roseum; Eεcherichia coli , DSM 10584, deposition date 13 March, 1996; cDNA from Syspastospora boninensis; Escherichia coli , DSM 10585, deposition date 13 March, 1996; cDNA from Cheatomium murorum Escherichia coli , DSM 10587, deposition date 13 March, 1996; cDNA from Sordaria fimicola; Escherichia coli , DSM 10588, deposition date 13 March, 1996; cDNA from the unidentified strain CBS 273.96; Escherichia coli , DSM 10586, deposition date 13 March, 1996; cDNA from Spongipellis sp. Color clarification of crude supernatants During normal wash the fabric will often fade. However, the fabric appearance is improved and the original colours are much better preserved or maintained if the fabric is washed with a cellulase giving color clarification. Color clarification is measured as removal of surface fibrils and fibers protruding from the yarn of a textile containing cellulosic fibers. Apparatus Terg-o-tometer Liquid volume 100 ml Agitation 150 movements/min with vertical stirrer Rinse time 5 min in tapwater Washing temp 40 * Washing liqour 0.05 M phosphate buffer PH 7.0 Washing time 30 min Repetitions 2 Enzymes Crude supernatants from the strains shown below. Dosage Two dosages from : 200, 500, 1000 or 2500 S-CEVU/1 Textile 2 swatches of aged black 100% cotton 5x6 cm (0.9 gram) Drying : Tumble dry Evaluation: The light remission is measured by a Datacolor Elrepho Remission spectrophotometer. Remission is calculated as 5 delta L (Hunter Lab-values) . When the surface fibrils and fibers protruding from the yarn are removed by the cellulase, the surface of the black fabric appears darker, and lower L values are obtained. 10 The samples are compared with a blind sample, i.e. washed without enzyme. Below is shown the delta L remission values compared to a blind sample. 15 ECU/1 Strain 2QQ 5_0_0 JOQQ 25Q0 13. Fusarium anguioides n.t. -0.71 n.t. -1.28 15. Fusarium solani n.t. -0.96 n.t. -1.37 24. Thielavia thermophila -0.30 n.t. -1.25 n.t. 25. Cladorrhinum foecun. n.t. -1.79 n.t. -2.18 37. Spongipellis (?) n.t. -1.01 n.t. -1.63 39. Rhizomucor pusillus n.t. -1.90 n.t. -2.66 41. Chaetostylum fresenii n.t. -0.17 n.t. -1.33 45. Ace No. : CBS 273.96 n.t. -1.31 n.t. -1.20 The data shows that all strains gives good color clarification under the conditions tested, (n.t. = not tested at this dosage). SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: (A) NAME: Novo Nordisk A/S (B) STREET: Novo Alle (C) CITY: DK-2880 Bagsvaerd (E) COUNTRY: Denmark (F) POSTAL CODE (ZIP) : DK-2880 (G) TELEPHONE: +45 44 44 88 88 (H) TELEFAX: +45 44 49 32 56 (ii) TITLE OF INVENTION: NOVEL ENDOGLUCANASES (iii) NUMBER OF SEQUENCES: 72 (iv) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: PatentIn Release #1.0, Version #1.30 (EPO) (2) INFORMATION FOR SEQ ID NO: 1A: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 891 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Saccharomyces cerevisiae (B) STRAIN: DSM 9770 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 1A: AAAGAAAGGC TCTCTGCTGT CGTCGCTCTC GTCGCTCTCG TCGGCATCCT CCATCCGTCC 60 GCCTTTGATA ACCCGCTCCC CGACTCAGTC AAGACGACGC ATACTTGGCA CCATGCATCT 120 CTCCGCCACC ACCGGGTTCC TCGCCCTCCC GGTCCTGGCC CTGGACCAGC TCTCGGGCAT 180 CGGCCAGACG ACCCGGTACT GGGACTGCTG CAAGCCGAGC TGCGCCTGGC CCGGCAAGGG 240 CCCCTCGTCT CCGGTGCAGG CCTGCGACAA GAACGACAAC CCGCTCAACG ACGGCGGCTC 300 CACCCGGTCC GGCTGCGACG CGGGCGGCAG CGCCTACATG TGCTCCTCCC AGAGCCCCTG 360 GGCCGTCAGC GACGAGCTGT CGTACGGCTG GGCGGCCGTC AAGCTCGCCG GCAGCTCCGA 420 GTCGCAGTGG TGCTGCGCCT GCTACGAGCT GACCTTCACC AGCGGGCCGG TCGCGGGCAA 480 GAAGATGATT GTGCAGGCGA CCAACACCGG TGGCGACCTG GGCGACAACC ACTTTGACCT 540 GGCCATCCCC GGTGGCGGTG TCGGTATTTT CAACGCCTGC ACCGACCAGT ACGGCGCTCC 600 CCCGAACGGC TGGGGCGACC GCTACGGCGG CATCCATTCC AAGGAAGAGT GCGAATCCTT 660 CCCGGAGGCC CTCAAGCCCG GCTGCAACTG GCGCTTCGAC TGGTTCCAAA ACGCCGACAA 720 CCCGTCGGTC ACCTTCCAGG AGGTGGCCTG CCCGTCGGAG CTCACGTCCA AGAGCGGCTG 780 CTCCCGTTAA GAGGGAAGAG AGGGGGCTGG AAGGACCGAA AGATTCAACC TCTGCTCCTG 840 CTGGGGAAGC TCGGGCGCGA GTGTGAAACT GGTGTAAATA TTGTGGCACA CACAAGCTAC 900 TACAGTCCGT CTCGCCGTCC GGCTAACTAG CCTTGCTGCG GATCTGTCCA AAAAAAAAAA 960 (2) INFORMATION FOR SEQ ID NO: IB: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 225 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: IB: Met His Leu Ser Ala Thr Thr Gly Phe Leu Ala Leu Pro Val Leu Ala 10 15 Leu Asp Gin Leu Ser Gly lie Gly Gin Thr Thr Arg Tyr Trp Asp Cys 20 25 30 Cyβ Lye Pro Ser Cys Ala Trp Pro Gly Lye Gly Pro Ser Ser Pro Val 35 40 45 Gin Ala Cyβ Asp Lye Aβn Asp Asn Pro Leu Asn Asp Gly Gly Ser Thr 50 55 60 Arg Ser Gly Cys Asp Ala Gly Gly Ser Ala Tyr Met Cyβ Ser Ser Gin 65 70 75 80 Ser Pro Trp Ala Val Ser Asp Glu Leu Ser Tyr Gly Trp Ala Ala Val 85 90 95 Lye Leu Ala Gly Ser Ser Glu Ser Gin Trp Cyβ Cys Ala Cys Tyr Glu 100 105 110 Leu Thr Phe Thr Ser Gly Pro Val Ala Gly Lys Lys Met lie Val Gin 115 120 125 Ala Thr Aβn Thr Gly Gly Asp Leu Gly Asp Asn His Phe Asp Leu Ala 130 135 140 lie Pro Gly Gly Gly Val Gly lie Phe Asn Ala Cys Thr Asp Gin Tyr 145 150 155 160 Gly Ala Pro Pro Asn Gly Trp Gly Asp Arg Tyr Gly Gly lie His Ser 165 170 175 Lys Glu Glu Cyβ Glu Ser Phe Pro Glu Ala Leu Lys Pro Gly Cys Asn 180 185 190 Trp Arg Phe Asp Trp Phe Gin Aβn Ala Asp Asn Pro Ser Val Thr Phe 195 200 205 Gin Glu Val Ala Cys Pro Ser Glu Leu Thr Ser Lys Ser Gly Cyβ Ser 210 215 220 Arg 225 (2) INFORMATION FOR SEQ ID NO: 2A: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 894 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: "Construction 1" (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 2A: ATGCATCTCT CCGCCACCAC CGGGTTCCTC GCCCTCCCGG TCCTGGCCCT GGACCAGCTC 60 TCGGGCATCG GCCAGACGAC CCGGTACTGG GACTGCTGCA AGCCGAGCTG CGCCTGGCCC 120 GGCAAGGGCC CCTCGTCTCC GGTGCAGGCC TGCGACAAGA ACGACAACCC GCTCAACGAC 180 GGCGGCTCCA CCCGGTCCGG CTGCGACGCG GGCGGCAGCG CCTACATGTG CTCCTCCCAG 240 AGCCCCTGGG CCGTCAGCGA CGAGCTGTCG TACGGCTGGG CGGCCGTCAA GCTCGCCGGC 300 AGCTCCGAGT CGCAGTGGTG CTGCGCCTGC TACGAGCTGA CCTTCACCAG CGGGCCGGTC 360 GCGGGCAAGA AGATGATTGT GCAGGCGACC AACACCGGTG GCGACCTGGG CGACAACCAC 420 TTTGACCTGG CCATCCCCGG TGGCGGTGTC GGTATTTTCA ACGCCTGCAC CGACCAGTAC 480 GGCGCTCCCC CGAACGGCTG GGGCGACCGC TACGGCGGCA TCCATTCCAA GGAAGAGTGC 540 GAATCCTTCC CGGAGGCCCT CAAGCCCGGC TGCAACTGGC GCTTCGACTG GTTCCAAAAC 600 GCCGACAACC CGTCGGTCAC CTTCCAGGAG GTGGCCTGCC CGTCGGAGCT CACGTCCAAG 660 AGCGGCTGCT CCCGTCCCTC CAGCAGCACC AGCTCTCCGG TCAACCAGCC TACCAGCACC 720 AGCACCACGT CCACCTCCAC CACCTCGAGC CCGCCAGTCC AGCCTACGAC TCCCAGCGGC 780 TGCACTGCTG AGAGGTGGGC TCAGTGCGGC GGCAATGGCT GGAGCGGCTG CACCACCTGC 840 GTCGCTGGCA GCACTTGCAC GAAGATTAAT GACTGGTACC ATCAGTGCCT GTAG 894 (2) INFORMATION FOR SEQ ID NO: 2B: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 297 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 2B : Met His Leu Ser Ala Thr Thr Gly Phe Leu Ala Leu Pro Val Leu Ala 10 15 Leu Asp Gin Leu Ser Gly lie Gly Gin Thr Thr Arg Tyr Trp Aβp Cyβ 20 25 30 Cyβ Lys Pro Ser Cyβ Ala Trp Pro Gly Lys Gly Pro Ser Ser Pro Val 35 40 45 Gin Ala Cys Aβp Lys Asn Aβp Aβn Pro Leu Asn Asp Gly Gly Ser Thr 50 55 60 Arg Ser Gly Cyβ Aβp Ala Gly Gly Ser Ala Tyr Met Cys Ser Ser Gin 65 70 75 80 Ser Pro Trp Ala Val Ser Asp Glu Leu Ser Tyr Gly Trp Ala Ala Val 85 90 95 Lys Leu Ala Gly Ser Ser Glu Ser Gin Trp Cys Cyβ Ala Cyβ Tyr Glu 100 105 110 Leu Thr Phe Thr Ser Gly Pro Val Ala Gly Lys Lye Met lie Val Gin 115 120 125 Ala Thr Asn Thr Gly Gly Asp Leu Gly Asp Aβn Hie Phe Aβp Leu Ala 130 135 140 lie Pro Gly Gly Gly Val Gly lie Phe Asn Ala Cyβ Thr λβp Gin Tyr 145 150 155 160 Gly Ala Pro Pro Aβn Gly Trp Gly Aβp Arg Tyr Gly Gly lie His Ser 165 170 175 Lys Glu Glu Cyβ Glu Ser Phe Pro Glu Ala Leu Lys Pro Gly Cys Asn 180 185 190 Trp Arg Phe Asp Trp Phe Gin Aβn Ala Aβp Asn Pro Ser Val Thr Phe 195 200 205 Gin Glu Val Ala Cyβ Pro Ser Glu Leu Thr Ser Lye Ser Gly Cys Ser 210 215 220 Arg Pro Ser Ser Ser Thr Ser Ser Pro Val Asn Gin Pro Thr Ser Thr 225 230 235 240 Ser Thr Thr Ser Thr Ser Thr Thr Ser Ser Pro Pro Val Gin Pro Thr 245 250 255 Thr Pro Ser Gly Cyβ Thr Ala Glu Arg Trp Ala Gin Cys Gly Gly Asn 260 265 270 Gly Trp Ser Gly Cyβ Thr Thr Cys Val Ala Gly Ser Thr Cys Thr Lys 275 280 285 lie Asn Asp Trp Tyr Hie Gin Cyβ Leu 290 295 (2) INFORMATION FOR SEQ ID NO: 3A: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 927 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: "Construction 2" (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 3A: ATGCATCTCT CCGCCACCAC CGGGTTCCTC GCCCTCCCGG TCCTGGCCCT GGACCAGCTC 60 TCGGGCATCG GCCAGACGAC CCGGTACTGG GACTGCTGCA AGCCGAGCTG CGCCTGGCCC 120 GGCAAGGGCC CCTCGTCTCC GGTGCAGGCC TGCGACAAGA ACGACAACCC GCTCAACGAC 180 GGCGGCTCCA CCCGGTCCGG CTGCGACGCG GGCGGCAGCG CCTACATGTG CTCCTCCCAG 240 AGCCCCTGGG CCGTCAGCGA CGAGCTGTCG TACGGCTGGG CGGCCGTCAA GCTCGCCGGC 300 AGCTCCGAGT CGCAGTGGTG CTGCGCCTGC TACGAGCTGA CCTTCACCAG CGGGCCGGTC 360 GCGGGCAAGA AGATGATTGT GCAGGCGACC AACACCGGTG GCGACCTGGG CGACAACCAC 420 TTTGACCTGG CCATCCCCGG TGGCGGTGTC GGTATTTTCA ACGCCTGCAC CGACCAGTAC 480 GGCGCTCCCC CGAACGGCTG GGGCGACCGC TACGGCGGCA TCCATTCCAA GGAAGAGTGC 540 GAATCCTTCC CGGAGGCCCT CAAGCCCGGC TGCAACTGGC GCTTCGACTG GTTCCAAAAC 600 GCCGACAACC CGTCGGTCAC CTTCCAGGAG GTGGCCTGCC CGTCGGAGCT CACGTCCAAG 660 AGCGGCTGCT CCCGTAACGA CGACGGCAAC TTCCCTGCCG TCCAGATCCC CTCCAGCAGC 720 ACCAGCTCTC CGGTCAACCA GCCTACCAGC ACCAGCACCA CGTCCACCTC CACCACCTCG 780 AGCCCGCCAG TCCAGCCTAC GACTCCCAGC GGCTGCACTG CTGAGAGGTG GGCTCAGTGC 840 GGCGGCAATG GCTGGAGCGG CTGCACCACC TGCGTCGCTG GCAGCACTTG CACGAAGATT 900 AATGACTGGT ACCATCAGTG CCTGTAG 927 (2) INFORMATION FOR SEQ ID NO: 3B: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 308 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii) MOLECULE TYPE : protein (Xi) SEQUENCE DESCRIPTION : SEQ ID NO : 3B : Met His Leu Ser Ala Thr Thr Gly Phe Leu Ala Leu Pro Val Leu Ala 1 5 10 15 Leu Asp Gin Leu Ser Gly lie Gly Gin Thr Thr Arg Tyr Trp Aβp Cyβ 20 25 30 Cyβ Lye Pro Ser Cys Ala Trp Pro Gly Lys Gly Pro Ser Ser Pro Val 35 40 45 Gin Ala Cys Aβp Lye Aβn Aβp Aβn Pro Leu Aβn Aβp Gly Gly Ser Thr 50 55 60 Arg Ser Gly Cys Asp Ala Gly Gly Ser Ala Tyr Met Cys Ser Ser Gin 65 70 75 80 Ser Pro Trp Ala Val Ser Asp Glu Leu Ser Tyr Gly Trp Ala Ala Val 85 90 95 Lys Leu Ala Gly Ser Ser Glu Ser Gin Trp Cyβ Cyβ Ala Cyβ Tyr Glu 100 105 110 Leu Thr Phe Thr Ser Gly Pro Val Ala Gly Lys Lys Met lie Val Gin 115 120 125 Ala Thr Asn Thr Gly Gly Aβp Leu Gly Asp Aβn Hie Phe Asp Leu Ala 130 135 140 lie Pro Gly Gly Gly Val Gly lie Phe Aβn Ala Cyβ Thr Aβp Gin Tyr 145 150 155 160 Gly Ala Pro Pro Aβn Gly Trp Gly Aβp Arg Tyr Gly Gly lie His Ser 165 170 175 Lys Glu Glu Cyβ Glu Ser Phe Pro Glu Ala Leu Lye Pro Gly Cyβ Asn 180 185 190 Trp Arg Phe Aβp Trp Phe Gin Aβn Ala λβp Aβn Pro Ser Val Thr Phe 195 200 205 Gin Glu Val Ala Cyβ Pro Ser Glu Leu Thr Ser Lye Ser Gly Cys Ser 210 215 220 Arg λβn λβp λβp Gly Aβn Phe Pro λla Val Gin lie Pro Ser Ser Ser 225 230 235 240 Thr Ser Ser Pro Val λβn Gin Pro Thr Ser Thr Ser Thr Thr Ser Thr 245 250 255 Ser Thr Thr Ser Ser Pro Pro Val Gin Pro Thr Thr Pro Ser Gly Cyβ 260 265 270 Thr λla Glu λrg Trp λla Gin Cyβ Gly Gly λβn Gly Trp Ser Gly Cys 275 280 285 Thr Thr Cyβ Val λla Gly Ser Thr Cys Thr Lys He λsn λsp Trp Tyr 290 295 300 His Gin Cys Leu 305 (2) INFORMATION FOR SEQ ID NO: 4 (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 888 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Saccharomyces cerevisiae, DSM 10082 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 4: CCAGTGTGCT GGλλλGCCTT CGTGCTGTCC CCGλCGTλTC CCTGλCCGCC λTGCGTTCCλ 60 CCλGCλTCTT GλTCGGCCTT GTTGCCGGCG TCGCTGCTCλ GλGCTCTGGC TCTGGCCλTλ 120 CλλCCλGGTλ CTGGGACTGC TGCλλGCCCT CATGCGCCTG GGATGAGAAG GCGGCTGTCA 180 GCCGGCCGGT CACAACATGC GACAGGAACA ACAGCCCCCT TTCGCCCGGC GCTGTGAGCG 240 GCTGCGλCCC CλλCGGCGTT GCλTTCλCCT GCλλCGλCλλ CCλGCCTTGG GCCGTλλλCλ 300 λCλλTGTCGC CTλCGGTTTT GCGGCTλCCG CCTTCCCTGG TGGCλλTGλG GCGTCGTGGT 360 GCTGTGCCTG CTλTGCTCTT CλλTTCλCAT CCGGCCCCGT TGCTGGCAλG λCGλTGGTTG 420 TGCλλTCCλC CλλCλCTGGC GGλGλTCTCλ GCGGCλCTCλ CTTCGλTλTC CλGλTGCCCG 480 GTGGλGGTCT CGGCλTCTTC GλCGGCTGCλ CCCCGCλGTT CGGCTTCλCG TTCCCCGGCA 540 ACCGCTλCGG CGGTλCCλCG λGCCGCλGCC λGTGCGCCGA GCTGCCCTCC GTCCTCCGTG 600 ACGGCTGCCA CTGGCGTTAC GACTGGTTCA λCGATGCCGA CAλCCCCλAC GTCλACTGGC 660 GCCGCGTCCG λTGCCCGGCG GCCCTCλCGA ACCGCTCCGG CTGCGTCCGC λλCGACGACA 720 λCλGCTλCCC CGTCTTCGλG CCCGGCλCGG GCλCCCCGCC GλCCCCCλCG λCCλCGACTA 780 CCAGCTCCCC TCCTCλGCCC λCCAACGGCG GλGGCGGCGG CλCTTCTCCT CACTGGGGCC 840 λGTGCGGCGG CCλGGGCTGG TCTGGCCCGλ CGGCCTGTGC CGGTGGGTCG ACCTGCAACC 900 TGλTCλλCCC GTGGTλCTCC CλGTGCλTTC CCλλCTλλGT GλTCCGGGCλ TTGCGGTCGλ 960 λλGGGGλCCG TTλGTCGλCλ λGGCCCλGCC λGλCCTCλGG CλGGTGGCTG CCλTGGCλGλ 1020 TTGTATATAG TCTTCCGAGT ACATACTATT GAATGAAAAT AAGAGCGGCT CGGACCATGA 1080 GCAGATGCCA TTTGATAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA 1140 AAAAAAAAAA AAAA 1154 (2) INFORMATION FOR SEQ ID NO: 5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 295 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 5: Met Arg Ser Thr Ser He Leu He Gly Leu Val Ala Gly Val Ala Ala 1 5 10 15 Gin Ser Ser Gly Ser Gly Hie Thr Thr Arg Tyr Trp Aβp Cyβ Cys Lye 20 25 30 Pro Ser Cyβ λla Trp λβp Glu Lye λla λla Val Ser λrg Pro Val Thr 35 40 45 Thr Cyβ λβp λrg λsn λβn Ser Pro Leu Ser Pro Gly λla Val Ser Gly 50 55 60 Cyβ λβp Pro λsn Gly Val λla Phe Thr Cyβ λβn λβp λβn Gin Pro Trp 65 70 75 80 λla Val λβn λβn λβn Val λla Tyr Gly Phe λla λla Thr λla Phe Pro 85 90 95 Gly Gly λβn Glu λla Ser Trp Cyβ Cyβ λla Cyβ Tyr λla Leu Gin Phe 100 105 110 Thr Ser Gly Pro Val λla Gly Lye Thr Met Val Val Gin Ser Thr Asn 115 120 125 Thr Gly Gly Asp Leu Ser Gly Thr His Phe λsp He Gin Met Pro Gly * 130 135 140 Gly Gly Leu Gly He Phe λβp Gly Cys Thr Pro Gin Phe Gly Phe Thr 145 150 155 160 Phe Pro Gly λβn λrg Tyr Gly Gly Thr Thr Ser Arg Ser Gin Cys Ala 165 170 175 Glu Leu Pro Ser Val Leu λrg λβp Gly Cyβ His Trp λrg Tyr λsp Trp 180 185 190 Phe λβn λβp λla λβp λβn Pro λβn Val λβn Trp λrg λrg Val λrg Cyβ 195 200 205 Pro λla λla Leu Thr λβn λrg Ser Gly Cyβ Val λrg λβn λβp λβp λβn 210 215 220 Ser Tyr Pro Val Phe Glu Pro Gly Thr Gly Thr Pro Pro Thr Pro Thr 225 230 235 240 Thr Thr Thr Thr Ser Ser Pro Pro Gin Pro Thr λβn Gly Gly Gly Gly 245 250 255 Gly Thr Ser Pro Hie Trp Gly Gin Cyβ Gly Gly Gin Gly Trp Ser Gly 260 265 270 Pro Thr λla Cyβ λla Gly Gly Ser Thr Cyβ λsn Leu He λβn Pro Trp 275 280 285 290 295 (2) INFORMATION FOR SEQ ID NO: 6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1423 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Saccharomyces cerevisiae, DSM 10080 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 6: λλλGTTCTGG CCGGλλCλGλ TCTCCGTTGT CGλTCTTCGA TTTTCCAGλC TCλGTCTGTG 60 λCλCTCCTTC λλTCCλCλTT CCTTTλCTTC TTCGTCλCTC λTTCλCλTCλ TGλTTTCλGC 120 TTGGλTTCTC CTGGGGCTGG TλGGCGCCGT GCCCTCCTCC GTCλTGGCCG CCTCGGGCAA 180 AGGCCλCλCC λCCCGCTλCT GGGλTTGCTG CλλGλCTTCT TGCGCATGGG AGGGCAAGGC 240 ATCCGTCTCC GλGCCTGTCC TGλCCTGTλλ CλλGCλGGλC λλCCCCλTCG TCGATGCCλλ 300 CGCCλGλλGC GGCTGCGλCG GCGGCGGGGC λTTTGCCTGT λCCλλCλλTT CCCCTTGGGC 360 CGTGλGCGλG GλCCTGGCCT λCGGλTTTGC TGCCACAGCC CTCAGCGGCG GCλCTGλGGG 420 CλGCTGGTGC TGCGCGTGTT λCGCCλTCλC λTTCλCGAGT GGCCCTGTGG CTGGCAAGAA 480 GATGGTCGTC CλGTCCλCGλ λCACGGGAGG CGACCTGTCC λλCAACCACT TTGACCTGAT 540 GATTCCCGGT GGλGGCCTCG GCλTCTTTGA CGGTTGCTCG GCTCAGTTCG GACAACTTCT 600 TCCCGGCGAG CGTTλCGGλG GTGTTTCGTC CCGCTCTCAA TGCGATGGCλ TGCCCGAGCT 660 CTTGλλλGλC GGTTGCCλGT GGCGCTTCGλ CTGGTTCλλG AACTCAGACA ACCCTGACAT 720 CGλGTTCGλG CλGGTCCλGT GTCCCλλλGλ GCTCλTTGCG GTCTCTGGGT GCGTCCGTGλ 780 CGλCGλTλGC λGCTTTCCCG TCTTCCλλGG TTCGGGCTCλ GGλGλTGTCλ λCCCλCCTCC 840 CAAGCCGACT λCGλCTλCGλ CCTCGTCλλλ GCCGAλλλCλ ACCTCTGCλC CλTCCλCTCT 900 CTCGλλCCCλ TCCGCCCCTC AACAGCCAGG GAACACTGAT AGACCTGCCG AGACAACCAC 960 TACCλλGCTG CCTGCCCTGC CGGCCλCGλC GAGCAGCCCT GCTGTCTCλG TTCCTTCGTC 1020 CλGCGCTCGC GTGCCTTTGT GGGGGCλλTG CGλCTCGGλλ GCTTCλTGGG λCGCλCCTλλ 1080 GλλGTGTGCλ λλGGGCλCCλ λGTGTGTCTλ CGTCλλCGλC TGGTλCTCTC λλTGCCλGCC 1140 GλλGλλCTCT TGTGCTTGλG λλGCλλTGCT CλCλGCλTGT CCTCTTGTCλ CCCCTTCTTT 1200 TCλTTCCCλλ λCλTλCTTλC TGTλTTλTTA TTTCCGATGC TTCλTTTCTT GCTTGTTTCT 1260 GTCTTTCCTG CλCGCλGCTT TCλλCGλTλC CCTTCλTGCG λTTGCCCTλC GλTCAGATGA 1320 TGGGCACGλC λTGGλGGλTG GTTTGGGCAC TCACGCGTTC λGGACGGGAA AATTTATTAG 1380 GGCTGAGATC CGTGAλTTGA CTTCATTTCG GCGGAATGTC TGC 1423 (2) INFORMATION FOR SEQ ID NO: 7: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 349 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION : SEQ ID NO : 7 : Met He Ser λla Trp He Leu Leu Gly Leu Val Gly λla Val Pro Ser 10 15 Ser Val Met λla λla Ser Gly Lye Gly Hie Thr Thr λrg Tyr Trp Asp 20 25 30 Cyβ Cys Lys Thr Ser Cys Ala Trp Glu Gly Lys Ala Ser Val Ser Glu 35 40 45 Pro Val Leu Thr Cyβ λβn Lye Gin λep Asn Pro He Val λsp λla λsn 50 55 60 λla λrg Ser Gly Cyβ Asp Gly Gly Gly λla Phe λla Cys Thr Asn Asn 65 70 75 80 Ser Pro Trp Ala Val Ser Glu Asp Leu Ala Tyr Gly Phe Ala Ala Thr 85 90 95 λla Leu Ser Gly Gly Thr Glu Gly Ser Trp Cys Cys λla Cys Tyr λla 100 105 110 He Thr Phe Thr Ser Gly Pro Val λla Gly Lys Lys Met Val Val Gin 115 120 125 Ser Thr λsn Thr Gly Gly λsp Leu Ser λsn λβn Hie Phe λβp Leu Met 130 135 140 He Pro Gly Gly Gly Leu Gly He Phe λep Gly Cyβ Ser λla Gin Phe 145 150 155 160 Gly Gin Leu Leu Pro Gly Glu λrg Tyr Gly Gly Val Ser Ser λrg Ser 165 170 175 Gin Cyβ Asp Gly Met Pro Glu Leu Leu Lys Asp Gly Cys Gin Trp Arg 180 185 190 Phe Asp Trp Phe Lys λβn Ser λsp λsn Pro Asp He Glu Phe Glu Gin 195 200 205 Val Gin Cys Pro Lys Glu Leu He Ala Val Ser Gly Cys Val Arg Asp 210 215 220 Asp Aβp Ser Ser Phe Pro Val Phe Gin Gly Ser Gly Ser Gly Asp Val 225 230 235 240 λsn Pro Pro Pro Lys Pro Thr Thr Thr Thr Thr Ser Ser Lys Pro Lye 245 250 255 Thr Thr Ser λla Pro Ser Thr Leu Ser λsn Pro Ser λla Pro Gin Gin 260 265 270 Pro Gly λβn Thr λβp λrg Pro λla Glu Thr Thr Thr Thr Lye Leu Pro 275 280 285 λla Leu Pro λla Thr Thr Ser Ser Pro λla Val Ser Val Pro Ser Ser 290 295 300 Ser λla λrg Val Pro Leu Trp Gly Gin Cyβ λsp Ser Glu λla Ser Trp 305 310 315 320 λsp λla Pro Lye Lye Cyβ λla Lys Gly Thr Lys Cys Val Tyr Val Asn 325 330 335 λβp Trp Tyr Ser Gin Cys Gin Pro Lys λβn Ser Cys λla 340 345 (2) INFORMATION FOR SEQ ID NO: 8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1174 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Saccharomyces cerevisiae, DSM 10081 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 8 GAGCAGCACC CCTCλλGCTG TλCλGTTTCC λCCCCGCTCT CTTTTCTTCG GCCCCCλGGλ 60 TGCGCTCTλC TCCCGTTCTT CGCλCλλCCC TGGCCGCTGC λCTTCCTCTG GTCGCCTCCG 120 CGGCCλGTGG CλGTGGCCλG TCCACGAGλT λCTGGGλCTG CTGCAAGCCG TCGTGCGCTT 180 GGCCCGGGλλ GGCCGCCGTC λGCCλλCCGG TCTλCGCGTG CGATGCCAAC TTCCAGCGCC 240 TGTCCGλCTT CλλTGTCCλG TCGGGCTGCλ λCGGCGGCTC GGCCTACTCC TGCGCCGACC 300 AGλCTCCCTG GGCGGTGλλC GλCλλTCTCG CCTλCGGCTT CGCCGCGACG AGCATCGCCG 360 GCGGGTCCGA ATCCTCGTGG TGCTGCGCCT GCTλCGCGCT CλCCTTCλCT TCCGGTCCCG 420 TCGCCGGCλλ GλCλλTGGTG GTGCAGTCAA CGAGCλCTGG CGGCGλCCTG GGλλGTAACC 480 AGTTCGλTλT CGCCλTGCCC GGCGGCGGCG TGGGCλTCTT CλACGGCTGC AGCTCGCAGT 540 TCGGCGGCCT CCCCGGCGCT CAλTACGGCG GCATTTCGTC GCGCGACCAG TGCGATTCCT 600 TCCCCGCGCC GCTCAAGCCC GGCTGCCAGT GGCGGTTTGA CTGGTTCCAG AACGCCGλCA 660 λCCCGλCGTT CACGTTCCλG CλGGTGCλGT GCCCCGCCGλ GλTCGTTGCC CGCTCCGGCT 720 GCAAGCGCλλ CGλCGλCTCC λGCTTCCCCG TCTTCλCCCC CCCλλGCGGT GGCλλCGGTG 780 GCλCCGGGλC GCCCλCGTCG λCTGCGCCTG GGTCGGGCCλ GλCGTCTCCC GGCGGCGGCλ 840 GTGGCTGCλC GTCTCλGλλG TGGGCTCλGT GCGGTGGCλT CGGCTTCλGC GGλTGCλCCλ 900 CCTGTGTCTC TGGCλCCλCC TGCCλGλλGT TGλλCGλCTλ CTλCTCGCλG TGCCTCTλλλ 960 CλGCTTTTCG CλCGλGGTGG CGGGλCGGλG CλλGGλGλCC GTCλλCTTCG TCλTGCλTλT 1020 TTTTTGλGCG CTCλλTλCλT λCλTλλCCTT CGλTTCTTGT λCλTλGCλCG CCGGTλCλCλ 1080 TCTCλCλCCG λCTTTGGGGG CGGλATCAGG CCCGTTTTAA AAAAλλλλλλ λλλAAλλλλλ 1140 λλλλλλλλλλ λλλλλλλλλλ λλλλλλλλλλ λλλλ 1174 (2) INFORMATION FOR SEQ ID NO: 9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 299 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear ( ii ) MOLECULE TYPE : peptide (Xi ) SEQUENCE DESCRIPTION : SEQ ID NO : 9 : Met λrg Ser Thr Pro Val Leu λrg Thr Thr Leu λla λla λla Leu Pro 1 5 10 15 Leu Val λla Ser λla λla Ser Gly Ser Gly Gin Ser Thr λrg Tyr Trp 20 25 30 λβp Cyβ Cys Lys Pro Ser Cys λla Trp Pro Gly Lys λla λla Val Ser 35 40 45 Gin Pro Val Tyr λla Cys Asp λla λβn Phe Gin λrg Leu Ser λsp Phe 50 55 60 λsn Val Gin Ser Gly Cys λsn Gly Gly Ser λla Tyr Ser Cys λla λsp 65 70 75 80 Gin Thr Pro Trp λla Val λsn Asp Asn Leu Ala Tyr Gly Phe λla λla 85 90 95 Thr Ser He λla Gly Gly Ser Glu Ser Ser Trp Cys Cyβ λla Cys Tyr 100 105 110 λla Leu Thr Phe Thr Ser Gly Pro Val Ala Gly Lys Thr Met Val Val 115 120 125 Gin Ser Thr Ser Thr Gly Gly Aβp Leu Gly Ser λsn Gin Phe Asp He 130 135 140 Ala Met Pro Gly Gly Gly Val Gly He Phe λsn Gly Cys Ser Ser Gin 145 150 155 160 Phe Gly Gly Leu Pro Gly λla Gin Tyr Gly Gly He Ser Ser λrg λsp 165 170 175 Gin Cys λsp Ser Phe Pro λla Pro Leu Lys Pro Gly Cyβ Gin Trp λrg 180 185 190 Phe λβp Trp Phe Gin λβn λla λβp λβn Pro Thr Phe Thr Phe Gin Gin 195 200 205 Val Gin Cyβ Pro λla Glu He Val λla λrg Ser Gly Cys Lys λrg λsn 210 215 220 Aβp Aβp Ser Ser Phe Pro Val Phe Thr Pro Pro Ser Gly Gly Asn Gly 225 230 235 240 Gly Thr Gly Thr Pro Thr Ser Thr Ala Pro Gly Ser Gly Gin Thr Ser 245 250 255 Pro Gly Gly Gly Ser Gly Cyβ Thr Ser Gin Lye Trp Ala Gin Cyβ Gly 260 265 270 Gly He Gly Phe Ser Gly Cyβ Thr Thr Cye Val Ser Gly Thr Thr Cys 275 280 285 Gin Lys Leu λβn λβp Tyr Tyr Ser Gin Cyβ Leu 290 295 VXOVOOWOO OOXOXWOXV OOOOWOOXV OO OOXOO XOOOOWOXX OXVOOOOXOO O fr 08* oooooooooo ooxvooooxv vooxxovoo wowoooox oovooooooo oovowoovo 03* gε xvwooxoox oxvwoow oooooxxxoo oooovooxoo voxxvovoxo owovxooxo 09ε ooxoxooxoo xxvoxovovo ovoovwooo oxoxoowoo ooooxoooxx oooovxooxx oε ooε xooovovoov oxoooooox voooooovoo woovooxov xovxooooov ooooooxvox oxooxooxov voxooxoxvo oovooooovo vooooowov oowoxvovo ooxoowooo gz 08T xooooowoo xoxoooxvoo vwooooovo oxxooxoxxo oooowoox ooxovoooxo ozτ 02 vxoovoowo voxoooooov xovooowox ovoooxooxx xvxooxooxo xooooxoxoo 09 ooooxoxooo oxoxoxxoxv oovoxxwxo woxxoooxo xxvooxoovo xoxxvxovoo gτ :oτ :ON αi oas :NoιidiHθsaα aoNanOas (TX) ∑τgoτ wsα Xτoo eτnoτ_ιa-ιosa :WSINYOHO (Y) :aoanos TYNIOIHO ( Λ) oτ YNαo :a Ai, ainoaiow (TT) αeeuTT '- KOc OdO' (α) aiβuτs :ssaNαaαNYais (o) pτoe oτeχonu :adAl (a) sατed aseq ετ6 :HJ,ONan (Y) :soιι,sιaaιoγaYHo aoNanOas (T) :0T :ON αi Oas HOa NOIXYWHOaNI (2) S0I00/96XQ7XDd _.6£6Z/96 OΛV TGGCGGCTTC λCTGλCCGCT CGCλλTGTGC GλCGCTCCCG TCCλλGTGGC λGGCCλGCTG 600 CAACTGGCGC TTCGACTGGT TCGAGAATGC CGACAACCCC ACCGTCGATT GGGAGCCTGT 660 CλCTTGCCCλ CλGGλλTTGG TCGCCCGGλC TGGCTGTTCC CGTλCCTλλG TGGGGGTGGλ 720 λCCTCCλTGT GλλTTGGTGT λTλTλGCTCC TGCCTGλGCλ TCCλCCλGTT CGCλTGTGTT 780 GλTCλGGλGT TGTGTTGCCT TGCTλGGλλλ GACTTTGTTG GAAλCTTGCG TGTTTλTTCC 840 AATTGAATAA CCCTGTATAG λCCGGTCλCλ TTTTTCTCTG λλλλλλλλλλ λλλλλλλλλλ 900 λλλλλλλλλλ AAA 913 (2) INFORMATION FOR SEQ ID NO: 11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 222 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 11: Met Phe Ser Pro Leu Trp λla Leu Ser λla Leu Leu Leu Phe Pro Ala 10 15 Thr Glu Ala Thr Ser Gly Val Thr Thr Arg Tyr Trp Asp Cys Cys Lye 20 25 30 Pro Ser Cys λla Trp Thr Gly Lys λla Ser Val Ser Lys Pro Val Gly 35 40 45 Thr Cyβ λβp He λβn λβp λβn λla Gin Thr Pro Ser λβp Leu Leu Lye 50 55 60 Ser Ser Cyβ λβp Gly Gly Ser λla Tyr Tyr Cys Ser λsn Gin Gly Pro 65 70 75 80 Trp λla Val λsn λsp Ser Leu Ser Tyr Gly Phe λla λla λla Lys Leu 85 90 95 Ser Gly Lys Gin Glu Thr λsp Trp Cyβ Cyβ Gly Cys Tyr Lys Leu Thr 100 105 110 Phe Thr Ser Thr λla Val Ser Gly Lys Gin Met He Val Gin He Thr 115 120 125 λβn Thr Gly Gly λβp Leu Gly λβn λβn His Phe λsp He λla Met Pro 130 135 140 Gly Gly Gly Val Gly He Phe λsn Gly Cys Ser Lys Gin Trp Asn Gly 145 150 155 160 He Asn Leu Gly Aβn Gin Tyr Gly Gly Phe Thr Aβp Arg Ser Gin Cys 165 170 175 λla Thr Leu Pro Ser Lys Trp Gin λla Ser Cys λsn Trp λrg Phe λβp 180 185 190 Trp Phe Glu λβn λla λβp λβn Pro Thr Val λβp Trp Glu Pro Val Thr 195 200 205 Cyβ Pro Gin Glu Leu Val λla λrg Thr Gly Cyβ Ser λrg Thr 210 215 220 2) INFORMATION FOR SEQ ID NO: 12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 808 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Escherichia coli, DSM 10511 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 12: CCGCTGCTGG GTλTλTλλTG CTCλGλCTTG GλλCCλλTGG TCCλTCCλAA CATGCTTAλA 60 λCGCTCGCTC CλTTGλTCAT CTTGGCCGCC TCGGTCACAG CGCAλλCλGC λGGAGTTACG 120 λCCCGCTλCT GGGλCTGCTG CλλGCCλλGC TGTGGλTGGA GTGGAAAGGC TTCTGTTTCT 180 GCTCCAGTCA GλACTTGCGA TCCTλλTGGλ λλTλCλCTTG GCCCλGACGT GAAAλGCGGA 240 U a^oαd :adλi ainosiow ( T) eeuττ ^DOTO OJ. (α) aibuτs :sS3NαaαNY LS (o) pτoe ouτuu. :adAI. (a) g spτoe ouτun. 922 :HJ.0N3n (Y) :S0I£SIH3I,DYHYH0 3DN3Ω03S (T) :ετ :ON αi Oss aoa NoiiYwπoaNi (2) oε 808 WWVWV VW WWW WWXXXOXO 08.. XOOOVOOXVO WVOXXOOVX vxovxoxvxo xoxvovxoxv xwooxoxov xoxvxwoov g∑ OZL xxvoxvwx ooxxoxoxoo oooxoxvxw xovoxoovoo oovooooxoo voxoxoovoo 099 02 oxxoovoxoo woooowxv oooooooxoo oxvooxovoo xxxoooxxw oxoxvooxoo 009 wooxoxoov oovooxxow oooxooxwo ovoxoooovo xoxoxoooo oovxwoxoo gτ xoooooowo oxoovoooxx xovoxooxoo xoxvoowov ovoxxoxooo oxxoxoovoo 08» xooooooxvo xvoxoovoxx xovoxwxw voooxoovox oovoooovov wovoxowo oτ 03* xxooovoxov wowoooxx ovxoooovoo xovoovxxxo ovoxxwoov xooxovooox xoxooxooov oowooovxo xoooooovxx ovoooovoox ooxxxxooxv xvooxovow ooε xwovoxxvo ooxxxvooxo oxwowooo ooxxovoxxv oxoowooxo ooovxvoxox 89τ S0I00/96XO71Dd _,6C6Z/96 OΛ (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 13: Met Val Hie Pro λsn Met Leu Lye Thr Leu λla Pro Leu He He Leu 1 5 10 15 λla λla Ser Val Thr λla Gin Thr λla Gly Val Thr Thr λrg Tyr Trp 20 25 30 λβp Cyβ Cyβ Lye Pro Ser Cys Gly Trp Ser Gly Lys λla Ser Val Ser 35 40 45 λla Pro Val λrg Thr Cys λsp λrg λsn Gly λsn Thr Leu Gly Pro λβp 50 55 60 Val Lys Ser Gly Cyβ λβp Ser Gly Gly Thr Ser Phe Thr Cyβ λla λsn 65 70 75 80 λβn Gly Pro Phe λla He λβp λβn λβn Thr λla Tyr Gly Phe λla λla 85 90 95 λla Hie Leu λla Gly Ser Ser Glu λla λla Trp Cys Cys Gin Cys Tyr 100 105 110 Glu Leu Thr Phe Thr Ser Gly Pro Val Val Gly Lys Lye Leu Thr Val 115 120 125 Gin Val Thr λβn Thr Gly Gly λβp Leu Gly λβn λsn His Phe Asp Leu 130 135 140 Met He Pro Gly Gly Gly Val Gly Leu Phe Thr Gin Gly Cyβ Pro Λla 145 150 155 160 Gin Phe Gly Ser Trp λβn Gly Gly λla Gin Tyr Gly Gly Val Ser Ser 165 170 175 λrg λβp Gin Cyβ Ser Gin Leu Pro λla λla Val Gin λla Gly Cys Gin 180 185 190 Phe λrg Phe λsp Trp Met Gly Gly λla λβp λβn Pro Asn Val Thr Phe 195 200 205 λrg Pro Val Thr Cyβ Pro λla Gin Leu Thr λβn He Ser Gly Cys Val 210 215 220 λrg Lys 225 (2) INFORMATION FOR SEQ ID NO: 14-A: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1048 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 14-A: GλCTTGGλλC CλλTGGTCCλ TCCλλλCλTG CTTλλλλCGC TCGCTCCλTT GλTCλTCTTG 60 GCCGCCTCGG TCλCλGCGCλ λλCλGCλGGλ GTTλCGλCCC GCTλCTGGGλ CTGCTGCλλG 120 CCλλGCTGTG GλTGGλGTGG λλλGGCTTCT GTTTCTGCTC CλGTCλGλλC TTGCGλTCGT 180 λλTGGλλλTλ CλCTTGGCCC λGλCGTGλλλ λGCGGλTGTG λTλGCGGTGG λλCGTCλTTC 240 λCTTGCGCGλ λCλλTGGTCC λTTTGCGλTT GλCλλTλλCλ CTGCλTλTGG TTTTGCTGCλ 300 GCCCλCTTλG CGGGCTCTλG CGλλGCλGCC TGGTGTTGCC λGTGCTλCGλ λTTGλCGTTT 360 ACGAGTGGAC CCGTλGTTGG GλλGλλλCTG λCCGTTCλλG TCλCλλλCAC GGGAGGTGλC 420 CTCGGλλλTλ λTCλCTTTGλ CCTGλTGATC CCCGGTGGAG GTGTTGGCCT CTTCACλCAA 480 GGλTGTCCTG CTCλGTTTGG GAGCTGGAλC GGGGGTGCTC λATACGGGGG TGTGTCCλGC 540 CGTGλCCλλT GCTCCCλλCT TCCλGCλGCT GTGCλλGCTG GATGTCAλTT CCGTTTCGAC 600 TGGATGGGTG GCGCGGATAλ CCCCλλCGTC λCCTTCCGAC CTGTGλCCTG CCCAGCGCAG 660 CTCACTλλTλ TCTCGGGCTG TGTTCGTλλA CCCTCCAGCA GCACCλGCTC TCCGGTCAAC 720 CAGCCTλCCλ GCλCCλGCλC CλCGTCCλCC TCCACCACCT CGAGCCCGCC AGTCCAGCCT 780 ACGλCTCCCλ GCGGCTGCλC TGCTGλGλGG TGGGCTCλGT GCGGCGGCAA TGGCTGGAGC 840 GGCTGCACCλ CCTGCGTCGC TGGCλGCλCT TGCλCGλλGλ TTλλTGλCTG GTλCCλTCλG 900 TGCCTGTλGλ CGCλGGGCλG CTTGλGGGCC TTλCTGGTGG CGCλλCGλλλ TGλCλCTCCC 960 λλTCλCTGTλ TTλGTTCTTG TλCλTλλTTT CGTCλTCCCT CCλGGGλTTG TCλCλTλλλT 1020 GCAATGAGGA λCλλTGλGTA CλGAATTC 1048 (2) INFORMATION FOR SEQ ID NO: 14 -B: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 298 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 14-B: Met Val Hie Pro λβn Met Leu Lye Thr Leu λla Pro Leu He He Leu 1 5 10 15 λla λla Ser Val Thr λla Gin Thr λla Gly Val Thr Thr λrg Tyr Trp 20 25 30 λβp Cyβ Cyβ Lye Pro Ser Cyβ Gly Trp Ser Gly Lye λla Ser Val Ser 35 40 45 λla Pro Val λrg Thr Cyβ λsp λrg λsn Gly λsn Thr Leu Gly Pro λsp 50 55 60 Val Lys Ser Gly Cyβ λβp Ser Gly Gly Thr Ser Phe Thr Cyβ λla λβn 65 70 75 80 λβn Gly Pro Phe λla He λβp λβn λβn Thr λla Tyr Gly Phe λla λla 85 90 95 λla Hie Leu λla Gly Ser Ser Glu λla λla Trp Cyβ Cyβ Gin Cye Tyr 100 105 110 Glu Leu Thr Phe Thr Ser Gly Pro Val Val Gly Lye Lye Leu Thr Val 115 120 125 Gin Val Thr Asn Thr Gly Gly λβp Leu Gly λβn Aβn His Phe λβp Leu 130 135 140 Met He Pro Gly Gly Gly Val Gly Leu Phe Thr Gin Gly Cys Pro λla 145 150 155 160 Gin Phe Gly Ser Trp λβn Gly Gly λla Gin Tyr Gly Gly Val Ser Ser 165 170 175 λrg λβp Gin Cyβ Ser Gin Leu Pro λla λla Val Gin λla Gly Cys Gin 180 185 190 Phe λrg Phe λβp Trp Met Gly Gly λla λsp λβn Pro λsn Val Thr Phe 195 200 205 Λrg Pro Val Thr Cyβ Pro λla Gin Leu Thr λβn He Ser Gly Cyβ Val 210 215 220 λrg Lye Pro Ser Ser Ser Thr Ser Ser Pro Val λβn Gin Pro Thr Ser 225 230 235 240 Thr Ser Thr Thr Ser Thr Ser Thr Thr Ser Ser Pro Pro Val Gin Pro 245 250 255 Thr Thr Pro Ser Gly Cye Thr λla Glu λrg Trp λla Gin Cyβ Gly Gly 260 265 270 λβn Gly Trp Ser Gly Cys Thr Thr Cys Val λla Gly Ser Thr Cys Thr 275 280 285 Lys He λβn λβp Trp Tyr Hie Gin Cyβ Leu 290 295 INFORMATION FOR SEQ ID NO : 15-A : ( i ) SEQUENCE CHARACTERISTICS : (A) LENGTH : 1031 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS : single (D) TOPOLOGY : linear ( ii ) MOLECULE TYPE : cDNA (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 15-A: CCλTCCλλλC λTGCTTλAAλ CGCTCGCTCC λTTGλTCλTC TTGGCCGCCT CGGTCλCλGC 60 GCλλλCλGCλ GGλGTTACGA CCCGCTλCTG GGλCTGCTGC λλGCCλλGCT GTGGλTGGλG 120 TGGλλλGGCT TCTGTTTCTG CTCCλGTCλG λλCTTGCGλT CGTλλTGGλλ λTλCλCTTGG 180 CCCλGλCGTG λλλλGCGGλT GTGλTλGCGG TGGλλCGTCλ TTCλCTTGCG CGλλCλλTGG 240 TCCλTTTGCG λTTGλCλλTλ λCλCTGCλTλ TGGTTTTGCT GCλGCCCλCT TλGCGGGCTC 300 TλGCGλλGCλ GCCTGGTGTT GCCλGTGCTλ CGλλTTGλCG TTTλCGλGTG GλCCCGTλGT 360 TGGGλλGλλλ CTGλCCGTTC AλGTCλCλλA CACGGGλGGT GλCCTCGGλλ λTλλTCλCTT 420 TGλCCTGλTG λTCCCCGGTG GλGGTGTTGG CCTCTTCλCλ CλλGGλTGTC CTGCTCλGTT 480 TGGGλGCTGG λλCGGGGGTG CTCλλTλCGG GGGTGTGTCC λGCCGTGλCC AλTGCTCCCλ 540 ACTTCCλGCλ GCTGTGCAλG CTGGATGTCλ λTTCCGTTTC GλCTGGATGG GTGGCGCGGA 600 TλλCCCCλλC GTCλCCTTCC GλCCTGTGAC CTGCCCAGCG CAGCTCACTA ATATCTCGGG 660 CTGTGTTCGT AλλCCCTCCA GCλGCλCCλG CTCTCCGGTC λλCCλGCCTA CCAGCACCAG 720 CACCλCGTCC λCCTCCλCCλ CCTCGλGCCC GCCλGTCCAG CCTλCGλCTC CCAGCGGCTG 780 CACTGCTGAG AGGTGGGCTC AGTGCGGCGG CλλTGGCTGG λGCGGCTGCA CCACCTGCGT 840 CGCTGGCλGC ACTTGCλCGA AGATTAATGA CTGGTACCλT CAGTGCCTGT λGλCGCλGGG 900 CAGCTTGAGG GCCTTλCTGG TGGCGCλλCG AAATGACACT CCCAATCACT GTATTAGTTC 960 TTGTACλTλλ TTTCGTCλTC CCTCCλGGGλ TTGTCACλTλ λλTGCλλTGA GGλλCλλTGλ 1020 GTλCλGλλTT C 1031 ( 2 ) INFORMATION FOR SEQ ID NO: 15-B: ( i) SEQUENCE CHARACTERISTICS : (A) LENGTH : 293 amino acids (B) TYPE : amino acid (C) STRANDEDNESS : single (D) TOPOLOGY : linear ( ii ) MOLECULE TYPE : peptide (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 15-B : Met Leu Lye Thr Leu λla Pro Leu He He Leu λla λla Ser Val Thr 1 5 10 15 λla Gin Thr λla Gly Val Thr Thr λrg Tyr Trp λsp Cyβ Cyβ Lys Pro 20 25 30 Ser Cyβ Gly Trp Ser Gly Lys λla Ser Val Ser Ala Pro Val Arg Thr 35 40 45 Cyβ Asp Arg Asn Gly Aβn Thr Leu Gly Pro Asp Val Lys Ser Gly Cys 50 55 60 λβp Ser Gly Gly Thr Ser Phe Thr Cyβ λla λβn Asn Gly Pro Phe Ala 65 70 75 80 He λβp λβn Asn Thr λla Tyr Gly Phe λla λla λla His Leu λla Gly 85 90 95 Ser Ser Glu λla λla Trp Cys Cys Gin Cyβ Tyr Glu Leu Thr Phe Thr 100 105 110 Ser Gly Pro Val Val Gly Lye Lye Leu Thr Val Gin Val Thr λβn Thr 115 120 125 Gly Gly λβp Leu Gly λβn λβn His Phe λβp Leu Met He Pro Gly Gly 130 135 140 Gly Val Gly Leu Phe Thr Gin Gly Cys Pro λla Gin Phe Gly Ser Trp 145 150 155 160 λβn Gly Gly λla Gin Tyr Gly Gly Val Ser Ser λrg λβp Gin Cyβ Ser 165 170 175 Gin Leu Pro λla λla Val Gin λla Gly Cyβ Gin Phe λrg Phe λsp Trp 180 185 190 Met Gly Gly λla λβp λsn Pro λβn Val Thr Phe λrg Pro Val Thr Cye 195 200 205 Pro λla Gin Leu Thr λβn He Ser Gly Cyβ Val λrg Lys Pro Ser Ser 210 215 220 Ser Thr Ser Ser Pro Val λsn Gin Pro Thr Ser Thr Ser Thr Thr Ser 225 230 235 240 Thr Ser Thr Thr Ser Ser Pro Pro Val Gin Pro Thr Thr Pro Ser Gly 245 250 255 Cys Thr λla Glu λrg Trp λla Gin Cys Gly Gly λsn Gly Trp Ser Gly 260 265 270 Cyβ Thr Thr Cyβ Val λla Gly Ser Thr Cys Thr Lys He λsn Asp Trp 275 280 285 Tyr His Gin Cys Leu 290 (2) INFORMATION FOR SEQ ID NO: 16: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1132 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA 08-. vovoxvoov xovooxvovo OVOXVOOVOO VOOOOOOOOO 000X000000 vooxxoxooo oxvxowooo ovoxvoooxo oooooooxoo ooovoooovo oovoxovooo oooooooxov 099 00X000000000X00X0X00 ooooowov ooooovoow oxxooxovoo vxoooooxov gε 009 ooxoooooo ovooxooooo oxooooxvw oooxooxovo oovooooovo ovoovooooo oovxoooow vooooooxxo ovoxoooooo xwoooooov ooxoooovoo xxoxvoooox o ε 08* 0000000000 oooxvoxoo xvovoxxxov owooooov oxoovooooo oooovovwo 03* g∑ vooxovooxo oxooxvoovo vwoooooxx oxooooooox oovoxxovox xooooxvxoo 09ε xoooxoxoox ooxoovoooo voooxvooxo oxovoxxxoo oovoooxoox xxxooxvxoo 02 ooε OOXOOWXVO OWOXOXOOO OXOOOOVOOV VXVOOWOOX OOVOVIOOOO xooooowoo 0*3 xxvoooxooo oovoovoooo ovooxoooox oxooowow owoovxvoo oxoovowox gτ ooooovooov oxoooxoooo wwoovooo xoooooxoox oooowooxo oxovoooxov 03τ oτ xvovoovoov ooooooovo ooxoxooxov oooooooxo ooooooxoo xoooooxvox 09 ooxovooxox ooxxoooxvo ovovxoxooo oxooooxoov ovxoovow voxxovowo g : 9τ : ON αi Oas t Noiidiπosaα aoNanOas (τ χ ) τ soτ wsα ' ττoo eτu.oτ_u-u;osa :WSINYOHO (Y) : aθHflOS TYNIOIHO ( TΛ) 6LZ S0I00/96Xd/I_3d _,6€6 96 OΛA CCTCλTCGTC GTCTTCGTCT TCGTCGTCGT CGλCTλCGGC TGGTλGCCCG CCTGTGCCGA 840 CTGGTGGTGG TλGTGGGCCλ λCGTCGCCTG TCTGGGGλCλ GTGCGGCGGT CλGGGλTGGλ 900 GTGGTCCTλC GCGTTGTGTT GCTGGGTCGλ CλTGCλGTGT GGTCλλCCCG TGGTλCTCGC 960 λGTGTTTTCC TTλλGGλGCC TCTGGCTGλG CλGλTCCTTT CGλλGλGGλG GGTCTCTCTG 1020 CTCTTTCλGT CTGTTCλGGG λλCGGCCGTC TCGGCTλCλT TGTλCλTλTC CCλCCTCGTλ 1080 TλTAGCTAGC TCATCTACAC TTGTGATCTC Cλλλλλλλλλ λλλλλλλλλλ AA 1132 (2) INFORMATION FOR SEQ ID NO: 17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 310 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 17: Met λrg Ser Ser λla Val Leu He Gly Leu Val λla Gly Val λla λla 10 15 Gin Ser Ser Gly Thr Gly λrg Thr Thr λrg Tyr Trp λsp Cyβ Cys Lys 20 25 30 Pro Ser Cyβ Gly Trp λsp Glu Lys Ala Ser Val Ser Gin Pro Val Lys 35 40 45 Thr Cyβ λsp λrg λβn λβn λβn Pro Leu λla Ser Thr λla λrg Ser Gly 50 55 60 Cys λβp Ser λsn Gly Val λla Tyr Thr Cys λβn λβp λβn Gin Pro Trp 65 70 75 80 λla Val λβn λβp Asn Leu λla Tyr Gly Phe λla λla Thr λla Phe Ser 85 90 95 Gly Gly Ser Glu λla Ser Trp Cyβ Cyβ λla Cyβ Tyr λla Leu Gin Phe 100 105 110 Thr Ser Gly Pro Val λla Gly Lye Thr Met Val Val Gin Ser Thr λβn 115 120 125 Thr Gly Gly Asp Leu Ser Gly Aβn His Phe λsp He Leu Met Pro Gly 130 135 140 Gly Gly Leu Gly He Phe λsp Gly Cys Thr Pro Gin Trp Gly Val Ser 145 150 155 160 Phe Pro Gly λβn λrg Tyr Gly Gly Thr Thr Ser λrg Ser Gin Cyβ Ser 165 170 175 Gin He Pro Ser λla Leu Gin Pro Gly Cys λsn Trp λrg Tyr Asp Trp 180 185 190 Phe λβn λβp λla λsp λβn Pro λβp Val Ser Trp λrg λrg Val Gin Cyβ 195 200 205 Pro λla λla Leu Thr λβp λrg Thr Gly Cyβ λrg λrg Ser λβp λβp Gly 210 215 220 λβn Tyr Pro Val Phe Gin Pro Gly Pro Pro Pro λla Thr Thr He λrg 225 230 235 240 Thr Ser Thr Thr He Thr λla Ser Ser Ser Ser Ser Ser Ser Ser Ser 245 250 255 Ser Thr Thr λla Gly Ser Pro Pro Val Pro Thr Gly Gly Gly Ser Gly 260 265 270 Pro Thr Ser Pro Val Trp Gly Gin Cyβ Gly Gly Gin Gly Trp Ser Gly 275 280 285 Pro Thr λrg Cyβ Val λla Gly Ser Thr Cys Ser Val Val Asn Pro Trp 290 295 300 305 310 (2) INFORMATION FOR SEQ ID NO: 18-A: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 885 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: "Construction from Macrophomina" (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..885 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 18-A: ATG TTC TCT CCG CTC TGG GCC CTG TCG GCT CTG CTC CTA TTT CCT GCC 48 Met Phe Ser Pro Leu Trp Ala Leu Ser Ala Leu Leu Leu Phe Pro λla 145 150 155 λCT Gλλ GCC λCT λGC GGC GTG λCλ λCC λGG TλC TGG GλC TGC TGC λAG 96 Thr Glu Ala Thr Ser Gly Val Thr Thr Arg Tyr Trp Asp Cys Cys Lys 160 165 170 CCG TCT TGT GCT TGG ACG GGC AλA GCλ TCC GTC TCC λλG CCC GTC GGA 144 Pro Ser Cyβ Ala Trp Thr Gly Lye Ala Ser Val Ser Lye Pro Val Gly 175 180 185 ACC TGC GAC λTC λλC GAC AλC GCC CλG λCG CCG AGC GAT CTG CTC AAG 192 Thr Cyβ λβp He λβn λβp λβn λla Gin Thr Pro Ser λsp Leu Leu Lys 190 195 200 205 TCG TCC TGT GλT GGC GGC λGC GCC TAC TAC TGC AGC AAC CAG GGC CCA 240 Ser Ser Cyβ λβp Gly Gly Ser λla Tyr Tyr Cyβ Ser λβn Gin Gly Pro 210 215 220 TGG GCC GTG λλC GλC λGC CTT TCC TλC GGC TTC GCT GCC GCC λλG CTG 288 Trp λla Val λβn λsp Ser Leu Ser Tyr Gly Phe λla λla λla Lys Leu 225 230 235 TCC GGλ λλG CλG GλG λCT GλT TGG TGC TGT GGC TGC TλC λλG CTC λCλ 336 Ser Gly Lye Gin Glu Thr λβp Trp Cyβ Cyβ Gly Cyβ Tyr Lye Leu Thr 240 245 250 TTC λCC TCC λCC GCC GTT TCC GGC λλG Cλλ λTG λTC GTG Cλλ ATC λCG 384 Phe Thr Ser Thr λla Val Ser Gly Lye Gin Met He Val Gin He Thr 255 260 265 AAC λCG GGC GGC GλC CTC GGC AAC AAC CAC TTC GλC λTC GCC λTG CCG 432 λβn Thr Gly Gly λβp Leu Gly Asn λβn Hie Phe λβp He λla Met Pro 270 275 280 285 GGC GGC GGC GTC GGC λTC TTC λλC GGG TGC TCC λλG CλA TGG AλC GGC 480 Gly Gly Gly Val Gly He Phe λβn Gly Cys Ser Lye Gin Trp λsn Gly 290 295 300 λTC λλT CTG GGC λλC CAG TAT GGC GGC TTC ACT GAC CGC TCG CAA TGT 528 He Aβn Leu Gly Aβn Gin Tyr Gly Gly Phe Thr Asp Arg Ser Gin Cys 305 310 315 GCG ACG CTC CCG TCC AλG TGG CλG GCC λGC TGC AAC TGG CGC TTC GAC 576 Ala Thr Leu Pro Ser Lys Trp Gin λla Ser Cys λsn Trp λrg Phe λsp 320 325 330 TGG TTC GλG λλT GCC GλC AAC CCC ACC GTC GAT TGG GAG CCT GTC ACT 624 Trp Phe Glu Asn Ala Aβp λsn Pro Thr Val λβp Trp Glu Pro Val Thr 335 340 345 TGC CCλ CλG Gλλ TTG GTC GCC CGG λCT GGC TGT TCC CGT λCC CCC TCC 672 Cyβ Pro G n Glu Leu Val λla λrg Thr Gly Cyβ Ser λrg Thr Pro Ser 350 355 360 365 λGC λGC λCC λGC TCT CCG GTC AAC CλG CCT λCC λGC λCC λGC λCC λCG 720 Ser Ser Thr Ser Ser Pro Val λβn Gin Pro Thr Ser Thr Ser Thr Thr 370 375 380 TCC λCC TCC λCC λCC TCG λGC CCG CCλ GTC CλG CCT λCG λCT CCC λGC 768 Ser Thr Ser Thr Thr Ser Ser Pro Pro Val Gin Pro Thr Thr Pro Ser 385 390 395 GGC TGC λCT GCT GλG λGG TGG GCT CλG TGC GGC GGC λλT GGC TGG λGC 816 Gly Cys Thr λla Glu λrg Trp λla Gin Cys Gly Gly λβn Gly Trp Ser 400 405 410 GGC TGC λCC λCC TGC GTC GCT GGC λGC λCT TGC λCG λλG λTT λλT GλC 864 Gly Cys Thr Thr Cys Val λla Gly Ser Thr Cys Thr Lys He λsn λβp 415 420 425 TGG TλC CλT CλG TGC CTG TλG 885 Trp Tyr Hie Gin Cys Leu * 430 435 (2) INFORMATION FOR SEQ ID NO: 18-B: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 295 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 18-B: Met Phe Ser Pro Leu Trp λla Leu Ser λla Leu Leu Leu Phe Pro Ala 10 15 Thr Glu λla Thr Ser Gly Val Thr Thr λrg Tyr Trp λsp Cys Cys Lys 20 25 30 Pro Ser Cys λla Trp Thr Gly Lys λla Ser Val Ser Lys Pro Val Gly 35 40 45 Thr Cyβ λβp He λβn λβp λβn λla Gin Thr Pro Ser λsp Leu Leu Lys 50 55 60 Ser Ser Cys λβp Gly Gly Ser λla Tyr Tyr Cyβ Ser λβn Gin Gly Pro 65 70 75 80 Trp λla Val λβn λβp Ser Leu Ser Tyr Gly Phe λla λla λla Lye Leu 85 90 95 Ser Gly Lye Gin Glu Thr λβp Trp Cye Cyβ Gly Cys Tyr Lys Leu Thr 100 105 110 Phe Thr Ser Thr λla Val Ser Gly Lys Gin Met He Val Gin He Thr 115 120 125 λβn Thr Gly Gly λβp Leu Gly λβn λβn His Phe λβp He λla Met Pro 130 135 140 Gly Gly Gly Val Gly He Phe λβn Gly Cyβ Ser Lys Gin Trp λsn Gly 145 150 155 160 He λsn Leu Gly λβn Gin Tyr Gly Gly Phe Thr λsp λrg Ser Gin Cyβ 165 170 175 λla Thr Leu Pro Ser Lys Trp Gin λla Ser Cys λβn Trp λrg Phe Asp 180 185 190 Trp Phe Glu Aβn Ala Aβp Aβn Pro Thr Val Aβp Trp Glu Pro Val Thr 195 200 205 Cyβ Pro Gin Glu Leu Val Ala Arg Thr Gly Cyβ Ser Arg Thr Pro Ser 210 215 220 Ser Ser Thr Ser Ser Pro Val λβn Gin Pro Thr Ser Thr Ser Thr Thr 225 230 235 240 Ser Thr Ser Thr Thr Ser Ser Pro Pro Val Gin Pro Thr Thr Pro Ser 245 250 255 Gly Cys Thr λla Glu λrg Trp λla Gin Cys Gly Gly λsn Gly Trp Ser 260 265 270 Gly Cyβ Thr Thr Cyβ Val λla Gly Ser Thr Cyβ Thr Lye He λβn λβp 275 280 285 Trp Tyr Hie Gin Cys Leu * 290 295 (2) INFORMATION FOR SEQ ID NO: 19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 425 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Escherichia coli, DSM 10576 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..425 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 19 CλλGλTACAA TATGCGTTCC TCCACTATTT TGCAAACCGG CCTGGTGGCC GTTCTCCCCT 60 TCGCCGTCCA GGCCGCCTCA GGATCCGGCA AGTCCλCCλG λTATTGGGAC TGCTGCAAAC 120 CλTCTTGTGC CTGGTCCGGC λλGGCTTCTG TCλλCCGCCC TGTTCTCGCC TGCAACGCAA 180 λCλλCλλCCC GCTGλλCGλC GCCλλCGTCλ λGTCλGGλTG TGλTGGCGGT TCTGCλTλCλ 240 CCTGTGCCλλ CλλCTCTCCC TGGGCλGTGλ λTGλCλλTCT GGCCTλCGGC TTCGCGGCCλ 300 CλλλλCTCλG CGGGGGGλCC GλGTCλTCTT GGTGCTGCGC CTGTTλTGCC CTCλCλTTCλ 360 CλTCGGGTCC TGTTTCTGGC λλλλCCTTGG TTGTCCλGTC TλCCλGTλCC GGTGGTGλTC 420 TTGGC 425 (2) INFORMATION FOR SEQ ID NO: 20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 141 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 20: Met λrg Ser Ser Thr He Leu Gin Thr Gly Leu Val λla Val Leu Pro 10 15 Phe λla Val Gin λla λla Ser Gly Ser Gly Lys Ser Thr λrg Tyr Trp 20 25 30 λβp Cyβ Cyβ Lys Pro Ser Cyβ λla Trp Ser Gly Lye Ala Ser Val Aβn 35 40 45 Arg Pro Val Leu Ala Cyβ Aβn Ala Asn Aβn λβn Pro Leu Aβn Asp Ala 50 55 60 λβn Val Lye Ser Gly Cyβ λβp Gly Gly Ser λla Tyr Thr Cyβ λla λβn 65 70 75 80 λβn Ser Pro Trp λla Val λβn Aβp λβn Leu λla Tyr Gly Phe λla λla 85 90 95 Thr Lye Leu Ser Gly Gly Thr Glu Ser Ser Trp Cys Cye λla Cyβ Tyr 100 105 110 λla Leu Thr Phe Thr Ser Gly Pro Val Ser Gly Lye Thr Leu Val Val 115 120 125 Gin Ser Thr Ser Thr Gly Gly λβp Leu Gly 130 135 (2) INFORMATION FOR SEQ ID NO: 21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 108 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Saccobolus dilutellus (B) STRAIN: CBS 275.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:1..108 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 21: TCG GCT TGC GλT AAC GGT GGT GGC ACT GCA TλC λTG TGT GCC λGC CλG Ser λla Cys λβp λβn Gly Gly Gly Thr λla Tyr Met Cyβ λla Ser Gin 1 5 10 15 GλG CCG TGG GCλ GTG λGC TCC λλC GTC GCG TλC GGC TTT GCT GCλ GTT Glu Pro Trp λla Val Ser Ser λβn Val λla Tyr Gly Phe λla λla Val 20 25 30 AGA ATC AGC GGA Arg He Ser Gly 35 (2) INFORMATION FOR SEQ ID NO: 22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 36 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 22: Ser λla Cyβ λβp λen Gly Gly Gly Thr λla Tyr Met Cyβ Ala Ser Gin 1 5 10 15 Glu Pro Trp Ala Val Ser Ser Aβn Val Ala Tyr Gly Phe Ala Ala Val 20 25 30 λrg He Ser Gly 35 (2) INFORMATION FOR SEQ ID NO: 23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 99 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Thermomyces verrucosus (B) STRAIN: CBS 285.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..99 (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 23 : GCC TGC λλC GCλ λλC TTC CλG CGC λTC λGT GλC CCC λλC GCC λλG TCG λla Cys Asn λla λβn Phe Gin λrg He Ser λsp Pro λβn λla Lys Ser GGC TGC GλT GGT GGC TCG GCC TTC TCT TGC GCC AλA Cλλ λCC CCT TGG Gly Cyβ λβp Gly Gly Ser λla Phe Ser Cyβ λla Lye Gin Thr Pro Trp GCC λla (2) INFORMATION FOR SEQ ID NO: 24: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 33 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 24: λla Cyβ λβn λla λβn Phe Gin λrg He Ser λβp Pro λβn λla Lye Ser 1 5 10 15 Gly Cye λβp Gly Gly Ser λla Phe Ser Cye λla Lye Gin Thr Pro Trp 20 25 30 λla (2) INFORMATION FOR SEQ ID NO: 25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 225 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Xylaria hypoxylon (B) STRAIN: CBS 284.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..225 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 25: GλC CλG CCG CTC GGC GGλ CAA CGG ACG CGA CCA AGG AGC GCG TGC GAC 48 λβp Gin Pro Leu Gly Gly Gin λrg Thr λrg Pro λrg Ser Ala Cyβ Aβp 35 40 45 λλT GGC GGC TCT GCλ TλC λTG TGC λGC AAC CλG λGC CCG TGG GCC GTC 96 λβn Gly Gly Ser λla Tyr Met Cyβ Ser λβn Gin Ser Pro Trp λla Val 50 55 60 65 GλC GλT TCT CTC λGT TλC GGλ TGG GCT GCC GTT λGG λTC TλT GGλ CλT 144 λβp Aβp Ser Leu Ser Tyr Gly Trp λla λla Val λrg He Tyr Gly Hie 70 75 80 λCC Gλλ λCT λCT TGG TGC TGC GCT TGC TλC GλG TTG λCT TTT λCC λGC 192 Thr Glu Thr Thr Trp Cyβ Cyβ λla Cye Tyr Glu Leu Thr Phe Thr Ser 85 90 95 GGT CCG GTT λGC GGC λλG λλG λTG λTT GTT CλG 225 Gly Pro Val Ser Gly Lye Lye Met He Val Gin 100 105 ( 2 ) INFORMATION FOR SEQ ID NO : 26 : ( i ) SEQUENCE CHARACTERISTICS : (A) LENGTH : 75 amino acids (B) TYPE : amino acid (D) TOPOLOGY : linear ( ii) MOLECULE TYPE : protein (xi ) SEQUENCE DESCRIPTION : SEQ ID NO : 26 : λβp Gin Pro Leu Gly Gly Gin λrg Thr λrg Pro λrg Ser Ala Cyβ Asp 1 5 10 15 λβn Gly Gly Ser λla Tyr Met Cyβ Ser λβn Gin Ser Pro Trp λla Val 20 25 30 λβp λβp Ser Leu Ser Tyr Gly Trp λla λla Val λrg He Tyr Gly Hie 35 40 45 Thr Glu Thr Thr Trp Cyβ Cyβ λla Cye Tyr Glu Leu Thr Phe Thr Ser 50 55 60 Gly Pro Val Ser Gly Lye Lye Met He Val Gin 65 70 75 (2) INFORMATION FOR SEQ ID NO: 27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Fusarium oxysporum ssp lycopersici (B) STRAIN: CBS 645.78 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..177 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 27: λGλ λλC GλC λλC CCC λTC TCC AAC ACC λλC GCT GTC AAC GGT TGT GAG 48 Arg Aβn Asp λβn Pro He Ser λβn Thr λβn λla Val λβn Gly Cye Glu 30 35 40 45 GGT GGT GGT TCT GCT TλT GCT TGC λCC AAC TAC TCT CCC TGG GCT GTC 96 Gly Gly Gly Ser Ala Tyr Ala Cye Thr Aβn Tyr Ser Pro Trp Ala Val 50 55 60 AλC GAT GAG CTT GCC TAC GGT TTC GCT GCT ACC AAG ATC TCC GGT GGC 144 λβn λβp Glu Leu λla Tyr Gly Phe λla λla Thr Lys He Ser Gly Gly 65 70 75 TCC GλG GCC λGC TGG TGC TGT GCC TGC TλT CTλ 177 Ser Glu λla Ser Trp Cys Cyβ λla Cyβ Tyr Leu 80 85 (2 ) INFORMATION FOR SEQ ID NO : 28 : ( i) SEQUENCE CHARACTERISTICS : (A) LENGTH : 59 amino acids (B) TYPE : amino acid (D) TOPOLOGY : linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 28: Arg Asn Asp Asn Pro lie Ser Asn Thr Asn Ala Val Asn Gly Cys Glu 1 5 10 15 Gly Gly Gly Ser Ala Tyr Ala Cys Thr Asn Tyr Ser Pro Trp Ala Val 20 25 30 Asn Asp Glu Leu Ala Tyr Gly Phe Ala Ala Thr Lys lie Ser Gly Gly 35 40 45 Ser Glu Ala Ser Trp Cys Cys Ala Cys Tyr Leu 50 55 (2) INFORMATION FOR SEQ ID NO: 29: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 63 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Nectria pinea (B) STRAIN: CBS 279.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..63 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 29: AGC GGC TGT GAC GGT GGT TCT GCC TAC GCC TGT GCA AAC AAC TCC CCT 48 Ser Gly Cys Asp Gly Gly Ser Ala Tyr Ala Cys Ala Asn Asn Ser Pro 60 65 70 75 TGG GCT GTC AAC GAT 63 Trp Ala Val Asn Asp 80 (2) INFORMATION FOR SEQ ID NO: 30: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 30: Ser Gly Cys Asp Gly Gly Ser Ala Tyr Ala Cys Ala Asn Asn Ser Pro 1 5 10 15 Trp Ala Val Asn Asp 20 (2) INFORMATION FOR SEQ ID NO: 31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Humicola grisea Traeen (B) STRAIN: ATCC 22726 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..177 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 31: AAC CAG CCT GTC TTC ACT TGC GAC GCC AAA TTC CAG CGC ATC ACC GAC 48 Asn Gin Pro Val Phe Thr Cys Asp Ala Lys Phe Gin Arg lie Thr Asp 25 30 35 CCC AAT ACC AAG TCG GGC TGC GAT GGC GGC TCG GCC TTT TCG TGT GCT 96 Pro Asn Thr Lys Ser Gly Cys Asp Gly Gly Ser Ala Phe Ser Cys Ala 40 45 50 GAC CAA ACC CCC TGG GCT CTG AAC GAC GAT TTC GCC TAT GGC TTC GCT 144 Asp Gin Thr Pro Trp Ala Leu Asn Asp Asp Phe Ala Tyr Gly Phe Ala 55 60 65 GCC ACG GCT ATT TCG GGT GGA TCG GAA GCC TCG 177 Ala Thr Ala lie Ser Gly Gly Ser Glu Ala Ser 70 75 80 (2) INFORMATION FOR SEQ ID NO: 32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 59 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 32: Asn Gin Pro Val Phe Thr Cys Asp Ala Lys Phe Gin Arg lie Thr Asp 1 5 10 15 Pro Asn Thr Lys Ser Gly Cys Asp Gly Gly Ser Ala Phe Ser Cys Ala 20 25 30 Asp Gin Thr Pro Trp Ala Leu Asn Asp Asp Phe Ala Tyr Gly Phe Ala 35 40 45 Ala Thr Ala lie Ser Gly Gly Ser Glu Ala Ser 50 55 (2) INFORMATION FOR SEQ ID NO: 33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 153 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Humicola nigrescens Omvik (B) STRAIN: CBS 819.73 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..153 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 33: GTC TAC GCC TGC AAC GCA AAC TTC CAG CGC ATC ACC GAC GCC AAC GCC 48 Val Tyr Ala Cys Asn Ala Asn Phe Gin Arg lie Thr Asp Ala Asn Ala 60 65 70 75 AAG TCC GGC TGC GAT GGC GGC TCC GCC TTC TCG TGC GCC AAC CAG ACC 96 Lys Ser Gly Cys Asp Gly Gly Ser Ala Phe Ser Cys Ala Asn Gin Thr 80 85 90 CCG TGG GCC GTG AGC GAC GAC TTT GCC TAC GGT TTC GCG GCT ACG GCG 144 Pro Trp Ala Val Ser Asp Asp Phe Ala Tyr Gly Phe Ala Ala Thr Ala 95 100 105 CTC GCC GGC 153 Leu Ala Gly 110 (2) INFORMATION FOR SEQ ID NO: 34: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 34: Val Tyr Ala Cys Asn Ala Asn Phe Gin Arg lie Thr Asp Ala Asn Ala 1 10 15 Lys Ser Gly Cys Asp Gly Gly Ser Ala Phe Ser Cys Ala Asn Gin Thr 20 25 30 Pro Trp Ala Val Ser Asp Asp Phe Ala Tyr Gly Phe Ala Ala Thr Ala 35 40 45 Leu Ala Gly 50 (2) INFORMATION FOR SEQ ID NO: 35: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 181 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Cladorrhinum foeeundissimum (B) STRAIN: ATCC 62373 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..181 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 35: GTC AAC CGC CCT GTC CTC GCC TGC GAC GCA AAC AAC AAC CCT CTG ACC 48 Val Asn Arg Pro Val Leu Ala Cys Asp Ala Asn Asn Asn Pro Leu Thr 1 5 10 15 GAC GCC GGC GTC AAG TCC GGA TGT GAT GGC GGT TCT GCA TAC ACC TGT 96 Asp Ala Gly Val Lys Ser Gly Cys Asp Gly Gly Ser Ala Tyr Thr Cys 20 25 30 GCC AAC AAC TCC CCA TGG GCA GTG AAC GAC CAG CTC GCC TAC GGC TTT 144 Ala Asn Asn Ser Pro Trp Ala Val Asn Asp Gin Leu Ala Tyr Gly Phe 35 40 45 GCC GCC ACC AAA CTG AGC GGC GGA ACT GAG TCG TCA 180 Ala Ala Thr Lys Leu Ser Gly Gly Thr Glu Ser Ser 50 55 60 (2) INFORMATION FOR SEQ ID NO: 36: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 60 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 36: Val Asn Arg Pro Val Leu Ala Cys Asp Ala Asn Asn Asn Pro Leu Thr 1 5 10 15 Asp Ala Gly Val Lys Ser Gly Cys Asp Gly Gly Ser Ala Tyr Thr Cys 20 25 30 Ala Asn Asn Ser Pro Trp Ala Val Asn Asp Gin Leu Ala Tyr Gly Phe 35 40 45 Ala Ala Thr Lys Leu Ser Gly Gly Thr Glu Ser Ser 50 55 60 (2) INFORMATION FOR SEQ ID NO: 37: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 64 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Syspastospora boninensis (B) STRAIN: NKBC 1515 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..64 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 37: GGC TGC GAC GGC GGC AGC GCC TTC ACC TGC TCC AAC AAC TCT CCA TGG 48 Gly Cys Asp Gly Gly Ser Ala Phe Thr Cys Ser Asn Asn Ser Pro Trp GCT GTG AAC GAA GAT 63 Ala Val Asn Glu Asp (2) INFORMATION FOR SEQ ID NO: 38: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 21 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 38 Gly Cys Asp Gly Gly Ser Ala Phe Thr Cys Ser Asn Asn Ser Pro Trp Ala Val Asn Glu Asp (2) INFORMATION FOR SEQ ID NO: 39: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 153 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Nigrospora sp (B) STRAIN: CBS 272.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:1..153 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 39: ACA AGA AAC GAC GGG CCC CTG TCC AGC CCC GAT GCC GCC TCC GGC TGT 48 Thr Arg Asn Asp Gly Pro Leu Ser Ser Pro Asp Ala Ala Ser Gly Cys 25 30 35 GAT GGC GGC GAA GCC TTT GCC TGT TCT AAT ACC TCG CCT TGG GCC GTC 96 Asp Gly Gly Glu Ala Phe Ala Cys Ser Asn Thr Ser Pro Trp Ala Val 40 45 50 AGC GAC CAG CTC GCG TAC GGA TAC GTC GCC ACG TCC ATC TCC GGC GGC 144 Ser Asp Gin Leu Ala Tyr Gly Tyr Val Ala Thr Ser lie Ser Gly Gly 55 60 65 ACC GAG TCA 153 Thr Glu Ser 70 (2) INFORMATION FOR SEQ ID NO: 40: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 40: Thr Arg Asn Asp Gly Pro Leu Ser Ser Pro Asp Ala Ala Ser Gly Cys 1 5 10 15 Asp Gly Gly Glu Ala Phe Ala Cys Ser Asn Thr Ser Pro Trp Ala Val 20 25 30 Ser Asp Gin Leu Ala Tyr Gly Tyr Val Ala Thr Ser lie Ser Gly Gly 35 40 45 Thr Glu Ser 50 (2) INFORMATION FOR SEQ ID NO: 41: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 159 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Chaetostylum fresenii (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:!..159 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 41: GTC CGA ACG TGT AGT GCC AAC GAC TCG CCC TTG TCC GAC CCA AAT GCC 48 Val Arg Thr Cys Ser Ala Asn Asp Ser Pro Leu Ser Asp Pro Asn Ala 55 60 65 CCA AGT GGG TGT GAC GGT GGT AGC GCC TTC ACT TGT TCC AAC AAC TCC 96 Pro Ser Gly Cys Asp Gly Gly Ser Ala Phe Thr Cys Ser Asn Asn Ser 70 75 80 CCG TGG GCA GTC GAT GAC CAG ACA GCT TAT GGC TTT GCG GCA ACA GCC 144 Pro Trp Ala Val Asp Asp Gin Thr Ala Tyr Gly Phe Ala Ala Thr Ala 85 90 95 ATC AGT GGC CAG TCC 159 lie Ser Gly Gin Ser 100 (2) INFORMATION FOR SEQ ID NO: 42: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 53 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 42: Val Arg Thr Cys Ser Ala Asn Asp Ser Pro Leu Ser Asp Pro Asn Ala 1 5 10 15 Pro Ser Gly Cys Asp Gly Gly Ser Ala Phe Thr Cys Ser Asn Asn Ser 20 25 30 Pro Trp Ala Val Asp Asp Gin Thr Ala Tyr Gly Phe Ala Ala Thr Ala 35 40 45 lie Ser Gly Gin Ser 50 (2) INFORMATION FOR SEQ ID NO: 43: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 153 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Exidia glandulosa (B) STRAIN: CBS 277.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:1..153 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 43: TGT GAG AAG AAC GAC AAC CCC TTA GCT GAC TTC AGC ACG AAA TCC GGG 48 Cys Glu Lys Asn Asp Asn Pro Leu Ala Asp Phe Ser Thr Lys Ser Gly 55 60 65 TGT GAA AGC GGA GGT TCG GCT TAT ACG TGT AAC AAC CAA TCA CCA TGG 96 Cys Glu Ser Gly Gly Ser Ala Tyr Thr Cys Asn Asn Gin Ser Pro Trp 70 75 80 85 GCC GTC AAT GAC TTG GTG TCG TAT GGC TTC GCC GCC ACA GCG ATC AAT 144 Ala Val Asn Asp Leu Val Ser Tyr Gly Phe Ala Ala Thr Ala lie Asn 90 95 100 GGT GGC AAT 153 Gly Gly Asn (2) INFORMATION FOR SEQ ID NO: 44: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 51 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 44: Cys Glu Lys Asn Asp Asn Pro Leu Ala Asp Phe Ser Thr Lys Ser Gly 1 5 10 15 Cys Glu Ser Gly Gly Ser Ala Tyr Thr Cys Asn Asn Gin Ser Pro Trp 20 25 30 Ala Val Asn Asp Leu Val Ser Tyr Gly Phe Ala Ala Thr Ala lie Asn 35 40 45 Gly Gly Asn 50 (2) INFORMATION FOR SEQ ID NO: 45: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 171 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (Vi) ORIGINAL SOURCE: (A) ORGANISM: Coniothecium sp (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:1..171 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 45: AGC CGC CCC GTC GGA ACC TGC AAG AGG AAC GAC AAC CCC CTC TCC GAC 48 Ser Arg Pro Val Gly Thr Cys Lys Arg Asn Asp Asn Pro Leu Ser Asp 55 60 65 CCC GAT GCC AAG TCC GGC TGC GAC GGC GGC GGC GCC TTC ATG TGC TCC 96 Pro Asp Ala Lys Ser Gly Cys Asp Gly Gly Gly Ala Phe Met Cys Ser 70 75 80 ACC CAG CAG CCG TGG GCC GTC AAC GAC AAT CTG GCA TAT GGC TTC GCC 144 Thr Gin Gin Pro Trp Ala Val Asn Asp Asn Leu Ala Tyr Gly Phe Ala 85 90 95 GCC ACG GCC ATC AGC GGC GGC AAC GAG 171 Ala Thr Ala lie Ser Gly Gly Asn Glu 100 105 (2) INFORMATION FOR SEQ ID NO: 46: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 57 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 46: Ser Arg Pro Val Gly Thr Cys Lys Arg Asn Asp Asn Pro Leu Ser Asp 1 5 10 15 Pro Asp Ala Lys Ser Gly Cys Asp Gly Gly Gly Ala Phe Met Cys Ser 20 25 30 Thr Gin Gin Pro Trp Ala Val Asn Asp Asn Leu Ala Tyr Gly Phe Ala 35 40 45 Ala Thr Ala lie Ser Gly Gly Asn Glu 50 55 (2) INFORMATION FOR SEQ ID NO: 47: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 159 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (B) STRAIN: CBS 271.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..159 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 47: ACT TGC AAC AAG AAC GAC GGG CCC CTG TCC AGC CCC GAT GCC GCC TCC 48 Thr Cys Asn Lys Asn Asp Gly Pro Leu Ser Ser Pro Asp Ala Ala Ser 60 65 70 GGC TGT GAT GGC GGC GAA GCC TTT GCC TGT TCT AAT ACC TCG CCT TGG 96 Gly Cys Asp Gly Gly Glu Ala Phe Ala Cys Ser Asn Thr Ser Pro Trp 75 80 85 GCC GTC AGC GAC CAG CTC GCG TAC GGA TAC CTC GCC ACG TCC ATC TCC 144 Ala Val Ser Asp Gin Leu Ala Tyr Gly Tyr Leu Ala Thr Ser He Ser 90 95 100 105 GGC GGC ACC GAG TCG 159 Gly Gly Thr Glu Ser 110 (2) INFORMATION FOR SEQ ID NO: 48: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 53 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 48: Thr Cys Asn Lys Asn Asp Gly Pro Leu Ser Ser Pro Asp Ala Ala Ser 1 5 10 15 Gly Cys Asp Gly Gly Glu Ala Phe Ala Cys Ser Asn Thr Ser Pro Trp 20 25 30 Ala Val Ser Asp Gin Leu Ala Tyr Gly Tyr Leu Ala Thr Ser He Ser 35 40 45 Gly Gly Thr Glu Ser 50 (2) INFORMATION FOR SEQ ID NO: 49: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 84 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (B) STRAIN: CBS 270.96 (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION:1..84 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 49: CCA GTT TTC TCC TGT GAC AAG TAC GAC AAC CCT CTA CCT GAC GCC AAT 48 Pro Val Phe Ser Cys Asp Lys Tyr Asp Asn Pro Leu Pro Asp Ala Asn 55 60 65 GCT GTG TCC GGG TGT GAC CCC GGA GGT ACT GCC TTC 84 Ala Val Ser Gly Cys Asp Pro Gly Gly Thr Ala Phe 70 75 80 (2) INFORMATION FOR SEQ ID NO: 50: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 28 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 50: Pro Val Phe Ser Cys Asp Lys Tyr Asp Asn Pro Leu Pro Asp Ala Asn 1 5 10 15 Ala Val Ser Gly Cys Asp Pro Gly Gly Thr Ala Phe 20 25 (2) INFORMATION FOR SEQ ID NO: 51: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 147 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Diplodia gossypina, CBS 274.96 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 51: ACCTGCGACG CCTGCGACAG CCCCCTCAGC GACTACGACG CCAAGTCCGG CTGCGACGGC 60 GGTAGCGCAT ACACCTGCAC CTACTCTACC CCCTGGGCCG TCGACGACAA CCTCTCCTAC 120 GGTTTCGCCG CCGCCAAGCT GAGCGGA 147 (2) INFORMATION FOR SEQ ID NO: 52: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 49 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 52: Thr Cys Asp Ala Cys Asp Ser Pro Leu Ser Asp Tyr Asp Ala Lys Ser 1 5 10 15 Gly Cys Asp Gly Gly Ser Ala Tyr Thr Cys Thr Tyr Ser Thr Pro Trp 20 25 30 Ala Val Asp Asp Asn Leu Ser Tyr Gly Phe Ala Ala Ala Lys Leu Ser 35 40 45 Gly (2) INFORMATION FOR SEQ ID NO: 53: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 135 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Ulospora bilgramii, NKBC 1444 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 53: CCACTAGCAG ATTTCACCGG TGGAACCGGC TGTAATGGCG GTTCGACATT CTCATGCTCA 60 AACCAACAAC CATGGGCGGT CAACGACACA TTCTCGTACG GCTTTGCGGG CATCTTTATC 120 ACAGGCCATG TCGAG 135 (2) INFORMATION FOR SEQ ID NO: 54: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 45 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 54: Pro Leu Ala Asp Phe Thr Gly Gly Thr Gly Cys Asn Gly Gly Ser Thr 1 5 10 15 Phe Ser Cys Ser Asn Gin Gin Pro Trp Ala Val Asn Asp Thr Phe Ser 20 25 30 Tyr Gly Phe Ala Gly He Phe He Thr Gly His Val Glu 35 40 45 (2) INFORMATION FOR SEQ ID NO: 55: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 114 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Penicillium verruculosum, ATCC 62396 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 55: GCCAAATCTG GATGTGATGC TGGTGGAGGT CAAGCCTACA TGTGCTCCAA CCAACAACCT 60 TGGGTAGTCA ACGACAACCT CGCCTACGGT TTCGCCGCAG TCAACATTGC CGGC 114 (2) INFORMATION FOR SEQ ID NO: 56: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 38 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 56: Ala Lys Ser Gly Cys Asp Ala Gly Gly Gly Gin Ala Tyr Met Cys Ser 1 5 10 15 Asn Gin Gin Pro Trp Val Val Asn Asp Asn Leu Ala Tyr Gly Phe Ala 20 25 30 Ala Val Asn He Ala Gly 35 (2) INFORMATION FOR SEQ ID NO: 57: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 113 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (Vi) ORIGINAL SOURCE: (B) STRAIN: Poronia punctata (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 57: TTCGACGTCC GGGTGCGACA ATGGCGGCAG CGCCTTCATG TGCTCTAACC AAAGCCCCTG 60 GGCCGTCAAC GACGATCTGG CCTACGGCTG GGCCGCCGTC TCAATCGCGG GCC 113 (2) INFORMATION FOR SEQ ID NO: 58: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 37 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 58: Ser Thr Ser Gly Cys Asp Asn Gly Gly Ser Ala Phe Met Cys Ser Asn 1 5 10 15 Gin Ser Pro Trp Ala Val Asn Asp Asp Leu Ala Tyr Gly Trp Ala Ala 20 25 30 Val Ser He Ala Gly 35 (2) INFORMATION FOR SEQ ID NO: 59: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 177 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Fusarium anguioides, IFO 4467 (Xi) SEQUENCE DESCRIPTION: SEQ ID NO: 59: TCAACACCGG TGCAGACGTG CGACCGCAAC GACAACCCGC TCTACGACGG CGGGTCGACG 60 CGGTCCGGCT GCGACGCCGG CGGCGGCGCC TACATGTGCT CGTCGCACAG CCCGTGGGCC 120 GTCAGCGACA GCCTCTCGTA CGGCTGGGCG GCCGTCCGCA TCGCCGGCCA GTCCGAG 177 (2) INFORMATION FOR SEQ ID NO: 60: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 59 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 60: Ser Thr Pro Val Gin Thr Cys Asp Arg Asn Asp Asn Pro Leu Tyr Asp 1 5 10 15 Gly Gly Ser Thr Arg Ser Gly Cys Asp Ala Gly Gly Gly Ala Tyr Met 20 25 30 Cys Ser Ser His Ser Pro Trp Ala Val Ser Asp Ser Leu Ser Tyr Gly 35 40 45 Trp Ala Ala Val Arg He Ala Gly Gin Ser Glu 50 55 (2) INFORMATION FOR SEQ ID NO: 61: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 150 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Thielavia thermophila, CBS 174.70 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 61: AACGACAACC CCATCTCCAA CACCAACGCT GTCAACGGTT GTGAGGGTGG TGGTTCTGCT 60 TACGCTTGCT CCAACTACTC TCCCTGGGCT GTCAACGATG ACCTTGCCTA CGGTTTCGCT 120 GTTACCAAGA TCTCCGGTGG CTCCGAGGCC 150 (2) INFORMATION FOR SEQ ID NO: 62: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 50 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 62: Asn Asp Asn Pro He Ser Asn Thr Asn Ala Val Asn Gly Cys Glu Gly 1 5 10 15 Gly Gly Ser Ala Tyr Ala Cys Ser Asn Tyr Ser Pro Trp Ala Val Asn 20 25 30 Asp Asp Leu Ala Tyr Gly Phe Ala Val Thr Lys He Ser Gly Gly Ser 35 40 45 Glu Ala 50 (2) INFORMATION FOR SEQ ID NO: 63: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 180 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (A) ORGANISM: Chaetomium cuniculorum, CBS 799.83 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 63: GTCAATCAGC CCATCCGAAC GTGTAGTGCC AACGACTCGC CCTTGTCCGA CCCAAATACC 60 CCAAGTGGCT GTGACGGTGG TAGCGCCTTC ACTTGTTCCA ACAACTCCCC GTGGGCAGTC 120 GATGACCAGA CAGCTTATGG CTTTGCGGCA ACAGCCATCA GTGGCCAGTC CGAGAGCAGC 180 (2) INFORMATION FOR SEQ ID NO: 64: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 60 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE : peptide (xi) SEQUENCE DESCRIPTION : SEQ ID NO : 64 : Val Asn Gin Pro He Arg Thr Cys Ser Ala Asn Asp Ser Pro Leu Ser 1 5 10 15 Asp Pro Asn Thr Pro Ser Gly Cys Asp Gly Gly Ser Ala Phe Thr Cys 20 25 30 Ser Asn Asn Ser Pro Trp Ala Val Asp Asp Gin Thr Ala Tyr Gly Phe 35 40 45 Ala Ala Thr Ala He Ser Gly Gin Ser Glu Ser Ser 50 55 60 (2) INFORMATION FOR SEQ ID NO: 65: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 159 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (iv) ORIGINAL SOURCE: Chaetomium virescens, CBS 547.75 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 65: ACCTGCGACA AGAAGGACAA CCCCATCTCT GATGCCAACG CCAAGAGCGG CTGTGATGGC 60 GGTTCTGCTT TCGCCTGCAC CAACTACTCT CCCTTCGCCG TCAACGACAA CCTCGCCTAC 120 GGTTTCGCTG CCACCAAGCT TGCTGGAGGC TCCGAGGCT 159 (2) INFORMATION FOR SEQ ID NO: 66: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 53 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 66: Thr Cys Asp Lys Lys Asp Asn Pro He Ser Asp Ala Asn Ala Lys Ser 1 5 10 15 Gly Cys Asp Gly Gly Ser Ala Phe Ala Cys Thr Asn Tyr Ser Pro Phe 20 25 30 Ala Val Asn Asp Asn Leu Ala Tyr Gly Phe Ala Ala Thr Lys Leu Ala 35 40 45 Gly Gly Ser Glu Ala 50 (2) INFORMATION FOR SEQ ID NO: 67: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 81 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: CDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Colletotrichum lagenarium (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 67: ACCTGCTACG CCAATGACCA GCGCATCGCC GACCGCAGCA CCAAGTCCGG CTGCGACGGC 60 GGCTCGGCCT ACTCCTGTTC T 81 (2) INFORMATION FOR SEQ ID NO: 68: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 27 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (Xi) SEQUENCE DESCRIPTION: SEQ ID NO : 68 : Thr Cys Tyr Ala Asn Asp Gin Arg He Ala Asp Arg Ser Thr Lys Ser 1 5 10 15 Gly Cys Asp Gly Gly Ser Ala Tyr Ser Cys Ser 20 25 (2) INFORMATION FOR SEQ ID NO: 69: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 160 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (vi) ORIGINAL SOURCE: (B) STRAIN: Phycomyces nitens (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 69: ACCTGTGACA AGAAGGACAA CCCCATCTCA AACTTGAACG CTGTCAACGG TTGTGAGGGT 60 GGTGGTTCTG CCTTCGCCTG CACCAACTAC TCTCCTTGGG CGGTCAATGA CAACCTTGCC 120 TACGGCTTCG CTGCAACCAA GCTTGCCGGT GGCTCCGAGG 160 (2) INFORMATION FOR SEQ ID NO: 70: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 53 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi ) SEQUENCE DESCRIPTION : SEQ ID NO : 70 : Thr Cys Asp Lys Lys Asp Asn Pro He Ser Asn Leu Asn Ala Val Asn 1 5 10 15 Gly Cys Glu Gly Gly Gly Ser Ala Phe Ala Cys Thr Asn Tyr Ser Pro 20 25 30 Trp Ala Val Asn Asp Asn Leu Ala Tyr Gly Phe Ala Ala Thr Lys Leu 35 40 45 Ala Gly Gly Ser Glu 50 (2) INFORMATION FOR SEQ ID NO: 71: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 165 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (iv) ORIGINAL SOURCE: Trichothecium roseum, IFO 5372 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 71: CCAGTAGGCA CCTGCGACGC CGGCAACAGC CCCCTCGGCG ACCCCCTGGC CAAGTCTGGC 60 TGCGAGGGCG GCCCGTCGTA CACGTGCGCC AACTACCAGC CGTGGGCGGT CAACGACCAG 120 CTGGCCTACG GCTTCGCGGC CACGGCCATC AACGGCGGCA CCGAG 165 (2) INFORMATION FOR SEQ ID NO: 72: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 55 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: peptide (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 72: Pro Val Gly Thr Cys Asp Ala Gly Asn Ser Pro Leu Gly Asp Pro Leu 1 5 10 15 Ala Lys Ser Gly Cys Glu Gly Gly Pro Ser Tyr Thr Cys Ala Asn Tyr 20 25 30 Gin Pro Trp Ala Val Asn Asp Gin Leu Ala Tyr Gly Phe Ala Ala Thr 35 40 45 Ala He Asn Gly Gly Thr Glu 50 55 REFERENCES Background of the invention: GB-A-1368599 EP-A-0 307 564 EP-A-0 435 876 WO 91/17243 WO 91/10732 WO 91/17244 WO 95/24471 WO 95/26398 Methods in Enzymology, 1988, Vol. 160, p. 200-391 (edited by Wood, W.A. and Kellogg, S.T.). 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Xue, G. et al., "A novel polysaccharide hydrolase cDNA (celD) from Neocallimastix patriciarum encoding three multi-functional catalytical domains with high endoglucanase, cellobiohydrolase and xylanase activities", J. Gen. Microbiol. (1992), Vol. 138, pp. 2397-2403. Zhou, L. et al., "Intronless celB from the anaerobic fungus Neocallimastix patriciarum encodes a modular family A endoglucanase", Biochem. J. (1994), Vol. 297, pp. 359-364. Dalbøge, H. and Heldt-Hansen, H.P., "A novel method for efficient expression cloning of fungal enzyme genes", Mol. Gen. Genet. (1994), Vol. 243, pp. 253-260. Ali, B.R.S. et al., "Cellulases and hemicellulases of the anaerobic fungus Piromyceε constitute a multiprotein cellulose-binding complex and are encoded by multigene families", FEMS Microbiol. Lett. (1995), Vol. 125, No. 1, pp. 15-21. DNA Data Bank of Japan (DDBJ) . 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Jiilich, W. : Higher Taxa of Basidiomycetes, Bibliotheca Mycologia 85, 485pp (1981). O'Donnell, K. : Zygomycetes in culture, University of Georgia, US, 257pp (1979). Hawksworth, D.L. , Kirk, P.M., Sutton, B.C. and Pegler, D.N.: Dictionary of the fungi, International Mycological Institute, 616pp (1995); Von Arx, J.A. : The genera of fungi sporulating in culture, 424pp (1981) . Detailed Description: Ford et al.. Protein Expression and Purification 2.: 95- 107, 1991. Cunningham and Wells, Science 244. 1081-1085, 1989. de Vos et al.. Science 255: 306-312, 1992. Smith et al., J. Mol. Biol. 22A' 899-904, 1992. Wlodaver et al., FEBS Lett. 3jϋ_9_: 59-64, 1992. Tomme, P. et al. "Cellulose-Binding Domains: Classi¬ fication and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Michael H. Penner (Eds.), ACS Symposium Series, No. 618, 1996. WO 90/00609 WO 95/16782 Needleman, S.B. and Wunsch, CD., Journal of Molecular Biology, 48_: 443-453, 1970. WO 94/14953 Sambrook, J., Fritsch, E. F. & Maniatis, T. 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Lab., Cold Spring Harbor, NY. Beaucage and Caruthers, Tetrahedron Letters 22 (1981) , 1859 - 1869. Matthes et al., EMBO Journal 3 (1984), 801 - 805. US 4,683,202 Saiki et al.. Science 239 (1988), 487 - 491. Hitzeman et al., J. Biol. Chem. 255 (1980), 12073 - 12080. Alber and Kawasaki, J. Mol. APPI. Gen. 1 (1982) , 419 - 434) . Young et al., in Genetic Engineering of Microorganisms for Chemicals (Hollaender et al, eds.), Plenum Press, New York, 1982). US 4,599,311 Russell et al., Nature 304 (1983), 652 - 654. McKnight et al., The EMBO J. 1 (1985), 2093 - 2099 P.R. Russell, Gene 40, 1985, pp. 125-130. US 4,870,008 O. Hagenbuchle et al., Nature 289. 1981, pp. 643-646. L.A. Vails et al., Cell 48., 1987, pp. 887-897. WO 87/02670 M. Egel-Mitani et al., Yeast 6. 1990, pp. 127-137. US 4,546,082 EP 16 201 EP 123 294 EP 123 544 EP 163 529 WO 89/02463 WO 92/11378 US 4,599,311 US 4,931,373 US 4,870,008 US 5,037,743 US 4,845,075 US 4,931,373 Gleeson et al., J. Gen. Microbiol. 132. 1986, pp. 3459- 3465. US 4,882,279 EP 272 277 EP 230 023 Malardier et al., 1989, Gene 78: 147-156. WO 93/11249. WO 94/14953. . Horton, R. M. , Hunt, H. D. , Ho, S. N. , Pullen, J. K. , and Pease, L. R. (1989) Gene 77, 61-68 Dalboge, H. , and Heldt-Hansen, H. (1994) Mol . Gen . Genet . 243, 253-260 Christensen, T. , Wøldike, H. , Boel, E. , Mortensen, S. B. , Hjortshøj, K., Thim, L. , and Hansen, M. T. (1988) Bio /Technology 6, 1419-1422 Sanger, F. , Nicklen, S., and Coulson, A. R. (1977) Proc. Natl . Acad . Sci . U. S . A. 74, 5463-5467 Devereux, J., Haeberli, P., and Smithies, O. (1984) Nucleic Acids Reε . 12, 387-395 Becker, D. M. & Guarante, L. 1991. Methods Enzymol. 194: 182-187. Gubler, U. & Hoffman, B. J. 1983. Gene 25: 263-269. R. Higuchi, B. Krummel, and R.K. Saiki (1988) . A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucl. Acids Res. 16: 7351-7367. Sanger, F., Nicklen, S. & Coulson, A. R. 1977. Proc. Natl. Acad. Sci. U. S. A. 74: 5463-5467. N. Axelsen et al., A Manual of Quantitative Immunoelectrophoresis. Blackwell Scientific Publications, 1973, Chapters 2,3,4 and 23. INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page A. O , line © B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | X | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 270. 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet | | During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau later (specify the general nature of the mάcaiions eg., 'Accession Number of Deposit') For International Bureau use only I I This sheet was received by ihe International Bureau on Authorized officer Form PCT. ' RO/ 134 ( J _lv \ WZ ) INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page -7. Q , line _g_ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |x | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat l, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 271. 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaάons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listedbelow will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit') For receiving Office use only For International Bureau use only & This sheet was received with the international application I ) This sheet was received by the International Bureau on Auibonzed officer Authorized office: INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule Ωbis) A. The indications made below relate to the microorganism refeπed to in the description on page f , line 2 8 _ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | χ | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 272. 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [^ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau later (specify the general nature oj the indications eg., 'Accession Number of Deposit") For receiving Office use only For International Bureau use only This sheet was received with the international application I I This sheet was received by the International Bureau on Authorized officer , . Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 2 O . line ___ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet ~ Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 273 . 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For International Bureau use onlv I I This sheet was received by the International Bureau on Authorized office: INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13bis) A. The indications made below relate to the microorganism referred to in the description on page f8 ■ line 3 6 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | X | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 274.96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution". D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For receiving Office use only For International Bureau use only This sheet was received with the international application I I This sheet was received by the International Bureau on. Authorized officer Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13bis) A. The indications made below relate to the microorganism referred to in the description on page _£ . line ό ?~ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |χ | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 275. 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [ | During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for alt designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below ill be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For receiving Office use only For International Bureau use only 2 To |S ϊheet w « received with the international application I 1 This sheet was received by the International Bureau on: Authorized officer Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13bis) A. The indications made below relate to the microorganism referred to in the description on page 7 - , line / 2 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | χ | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 276.96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet ] During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of theindications eg., "Accession Number of Deposit") For receiving Office use only For international Bureau use only I ^} This sheet was received with the international application j [ This sheet was received by the International Bureau on Authorized officer Authorized officer _r_- θ <_rv~. INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PC Rule l3W_-) For International Bureau use only I 1 This sheet was received by the International Bureau on Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page ^ , line ■< ? B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet I x I Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 278.96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet j] During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For receiving Office use only For International Bureau use only This sheet was received with the international application I j This sheet was received by the international Bureau on: Authorized offi Authorized officer At.; -ι_-(j_'__. M c* n 'r!«'.SSG'' INDICATIONS RELATING TO A DEPOSITED MICROORGANISM A. The indications made below relate to the microorganism referred to in the description on page *W o , line 37" B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet [7~] Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (includin postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 279.96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of theindications eg., 'Accession Number of Deposit") For International Bureau use only I j This sheet was received by the International Bureau on: Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 7* 7 , line f " O B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | χ| Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 280.96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet | | During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indicaύons are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For receiving Office use only For International Bureau use only | * ^J This sheet was received with the international application I I This sheet was received by the International Bureau ι Authorized officer Authorized office: INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13bis) A. The indications made below relate to the microorganism referred to in the description on page 7* 8 , line & B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |χ | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 281.96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [ | During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau later (specify the general nature of theindications eg.. 'Accession Number of Deposit") For International Bureau use only α This sheet was received bv the International Bureau on Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page τ~ . line 37 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | X | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 282 . 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for alt designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For International Bureau use only I I This sheet was received by the International Bureau on: Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) The indications made below relate to the microorganism referred to in the description on page r , line - V B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | " x " | Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 283. 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [~~| During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution". D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of theindications eg., 'Accession Number of Deposit") INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 7* φ , line <. < jp B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet I x I Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (includin postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 284 . 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71 ) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed beiowwill be submitted to the International Bureau later (specify the general nature of theindications eg., 'Accession Number of Deposit") For International Bureau use only I ] This sheet was received by the International Bureau on: Authoπztd oft.ce: INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 7 . line 2. B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet V~\ Name of depositary institution CENTRAALBUREAU VOOR SCHIMMELCULTURES Address of depositary institution (including postal code and country) Oosterstraat 1, Postbus 273, NL-3740 AG Baarn, the Netherlands Date of deposit Accession Number 12 March 1996 CBS 285 . 96 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet Q During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau later (specify the general nature of theindications eg., 'Accession Number of Deposit") For receiving Office use only For International Bureau use only This sheet was received wub the international application f j This sheet was received by the International Bureau on: Authorized office: Authorized office: a. - _s.- fe INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13_u_) INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on Pa e 2 Z, . line 3 ? B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet [xj Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re¬ public of Germany Date of deposit Accession Number 24 February 1995 DSM 9770 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet f~] During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature o) ' Vindications eg., 'Accession Number of Deposit") INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule l3_u_-) For International Bureau use only [ I This sheet was received by the International Bureau on: Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) The indications made below relate to the microorganism referred to in the description on page *( _2 ; , line .3 j* B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet κ~j Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 30 June 1995 DSM 10081 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [__ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg.. 'Accession Number of Deposit') For International Bureau use only I I This sheet was received by the International Bureau on. Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13-ύ.) The indications made below relate to the microorganism referred to in the description on page 2 & , line J ' *„ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |χ | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 30 June 1995 DSM 10082 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [__ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau later (specify the general nature of theindications eg., 'Accession Number of Deposit') INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule l3ύ_y) The indications made below relate to the microorganism referred to in the description on page 2 3 , line s B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet [X^ Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 2 February 1996 DSM 10511 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet ___ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (ifthe indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit") For International Bureau use only I j This sheet was received by the International Bureau on: Auihoπzed officer Form PCT/R 0/ 134 d ly 1 921 INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 13_>tϊ) A. The indications made below relate to the microorganism referred to in the description on page ^ 3 ; , line __. B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |χ | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 6 March 1996 DSM 10571 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet _~_ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill besubmitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit') For International Bureau use only [ j This sheet was received by the International Bureau on. Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM The indications made below relate to the microorganism referred to in the description on page ; , line B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | x | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 2 February 1996 DSM 10512 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet __] During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated Slates) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau \ner (specify the general nature of thein£catιons eg., 'Accession Number of Deposit") INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 2 . line _^ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | x | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re¬ public of Germany Date of deposit Accession Number 12 March 1996 DSM 10576 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet f__ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (ifthe indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau \ncr (specify the general nature of the indications eg., "Accession Number of Deposit") For International Bureau use only D This sheet was received by the International Bureau on: Autnor zed officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM A. The indications made below relate to the microorganism referred to in the description on page s , line 2 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | x [ Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re¬ public of Germany Date of deposit Accession Number 13 March 1996 DSM 10583 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet _ " _ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (ifthe indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be subraitted to the International Bureau later (specify the general nature of the indications eg., 'Accession Number of Deposit') For receiving Office use only For International Bureau use only [_V_ This sheet was received with the international application j ] This sheet was received by the International Bureau on. Authorized officer Authorized officer " ι . C ' INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 2 r , line 2 7 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | x | Name of depositary institution DEUT S CHE SAMMLUNG VON MIKROORGANISMEN UND ZELL¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 13 March 1996 DSM 10584 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet __J During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (ifthe indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg.. 'Accession Number of Deposit") For receiving Office use only For International Bureau use only jO" This sheet was received with the international application I I This sheet was received by the International Bureau on. Authorized officer X£ - * ±4- Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 7 , line 37 B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |x | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 13 March 1996 DSM 10585 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet ___ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indicat i ons listed belowwill be submitted to the International Bureau later (specify the general nature o) 'th indications eg., 'Accession Number of Deposit') For International Bureau use only I I This sheet was received by the International Bureau on: Authorized office: INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 2 -? , line B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | X | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (includin postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re¬ public of Germany Date of deposit Accession Number 13 March 1996 DSM 10586 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet [__ During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) he indications listed below will be submitted to the International Bureau later (specify the general nature of the indications _.«_ 'Accession Number of Deposit') For International Bureau use only I I This sheet was received by the International Bureau on. A-thorned officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule I3bis) A. The indications made below relate to the microorganism referred to in the description on page 2S~ . line 6_ B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet |χ | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re¬ public of Germany Date of deposit Accession Number 13 March 1996 DSM 10587 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet __] During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution". D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (if the indications are not for all designated States) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed below will be submitted to the International Bureau later (specify the general nature of the indications eg.. 'Accession Number of Deposit") For International Bureau use only [ ~ I This sheet was received by the International Bureau on: Authorized officer INDICATIONS RELATING TO A DEPOSITED MICROORGANISM (PCT Rule 136-J) The indications made below relate to the microorganism referred to in the description on page ZJC > line 7f B. IDENTIFICATION OF DEPOSIT Further deposits are identified on an additional sheet | x | Name of depositary institution DEUTSCHE SAMMLUNG VON MIKROORGANISMEN UND ZELL ¬ KULTUREN GmbH Address of depositary institution (including postal code and country) Mascheroder Weg lb, D-38124 Braunschweig, Federal Re ¬ public of Germany Date of deposit Accession Number 13 March 1996 DSM 10588 C. ADDITIONAL INDICATIONS (leave blank if not applicable) This information is continued on an additional sheet __] During the pendency of the patent application a sample of the deposited microorganism is only to be provided to an independent expert nominated by the person requesting the sample (cf. e.g. Rule 28(4) EPC / Regulation 3.25 of Australia Statutory Rules 1991 No 71) in those designated states providing for such "expert solution" . D. DESIGNATED STATES FOR WHICH INDICATIONS ARE MADE (ifthe indications are not for all designated Stales) E. SEPARATE FURNISHING OF INDICATIONS (leave blank if not applicable) The indications listed belowwill be submitted to the International Bureau later (specify the general nature of the indications eg, 'Accession Number of Deposit')

Claims: CLAIMS 1. An enzyme preparation consisting essentially of an enzyme which has cellulytic activity and comprises a first amino acid sequence consisting of 14 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp Xaa 1 2 3 4 5 6 7 8 9 10 11 12 13 14 and a second amino acid sequence consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, 12 and 14, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues with the provisos that, in the first amino acid sequence, (i) when the amino residue in position 12 is Ser, then the amino acid residue in position 14 is not Ser, and (ii) when the amino residue in position 12 is Gly, then the amino acid residue in position 14 is not Ala. 2. The enzyme preparation according to claim 1, wherein the amino acid residue in position 9 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group consisting of proline and threonine. 3. The enzyme preparation according to claim 1 or 2, wherein the amino acid residue in position 10 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably serine. 4. The enzyme preparation according to any of the claims 1-3 , wherein the amino acid residue in position 12 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group consisting of alanine and glycine. 5. The enzyme preparation according to any of the claims 1-4, wherein the amino acid residue in position 14 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine, tryptophan, glutamic acid and aspartic acid, preferably from the group consisting of proline, threonine, serine, alanine, glutamic acid and aspartic acid. 6. The enzyme preparation according to any of the claims 1-5, wherein the amino acid residue in position 4 of the second sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine, tryptophan, glutamic acid and aspartic acid, preferably from the group consisting of alanine, glycine, and glutamine. 7. The enzyme preparation according to any of the claims 1-6, wherein, in the first sequence, the amino acid residue in position 3 is tyrosine; or the amino acid residue in position 4 is tryptophan; or the amino acid residue in position 8 is lysine. 8. The enzyme preparation according to any of the claims 1-7, wherein the first sequence comprises an amino acid sequence selected from the group consisting of the sequences Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Ala Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 ; Thr Arg Tyr Trp Asp Cys Cys Lys Thr Ser Cys Ala Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 ; and Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Gly Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 . 9. The enzyme preparation according to any of the claims 1-8 which is of microbial origin, preferably fungal origin. 10. A DNA construct encoding for the enzyme according to any of the claims 1-9. 11. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to Hymen omyceteε (Baεidiomycota) which enzyme comprises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 12. The enzyme preparation according to claim 11, wherein the amino acid residue in position 7 is cysteine (Cys) . 13. The enzyme preparation according to claim 11, wherein the amino acid residue in position 1 is selected from the group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 14. The enzyme preparation according to any of the claims 11-13, wherein the enzyme comprises a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein. in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9 , 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 15. The enzyme preparation according to any of the claims 11-14 wherein the enzyme is obtainable from a strain belonging to the group consisting of the orders Agarica- les, Aphyllophorales, and Auriculariales . 16. The enzyme preparation according to claim 15 wherein the enzyme is obtainable from a strain belonging to the group consisting of the families Exidiaceae, Tricholomataceae, Coprinaceae, Schizophyllaceae, Bjerkanderaceae and Polyporaceae , preferably belonging to the group consisting of the genera Exidia, Crinipellis, Fomes, Panaeolus, Trameteε, Schizophyllum, and Spongipel¬ lis . 17. The enzyme preparation according to claim 16 wherein the enzyme is obtainable from a strain belonging to the group consisting of the species Exidia glandulosa, Crinipellis scabella, Fomes fomentarius, and Spongipelliε sp. , preferably from Exidia glandulosa, CBS 277.96, Crinipellis scabella, CBS 280.96, Fomeε fomentariuε, CBS 276.96, and Spongipellis sp. , CBS 283.96. 18. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to Chytridiomycota which enzyme comprises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 19. The enzyme preparation according to claim 18, wherein the amino acid residue in position 7 is cysteine (Cys) . 20. The enzyme preparation according to claim 18, wherein the amino acid residue in position 1 is selected from the group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 21. The enzyme preparation according to any of the claims 18-20, wherein the enzyme comprises a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, - in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 22. The enzyme preparation according to any of the claims 18-21 wherein the enzyme is obtainable from a strain belonging to the class of Chytridiomycetes , preferably belonging to the group consisting of the orders Chytridi- ales, Spizellomycetales, Harpochytrialeε , and Blaεtocladialeε . 23. The enzyme preparation according to claim 22 wherein the enzyme is obtainable from a strain belonging the family Spizellomycetaceae , preferably belonging to the genus Rhizophlyctiε , preferably belonging to the species Rhizophlyctiε roεea, eεpecially R. . roεea . , CBS 282.96. 24. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to Zygomycota which enzyme com- prises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 25. The enzyme preparation according to claim 24, wherein the amino acid residue in position 7 is cysteine (Cys) . 26. The enzyme preparation according to claim 24, wherein the amino acid residue in position 1 is selected from the group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 27. The enzyme preparation according to any of the claims 24-26, wherein the enzyme comprises a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg , Lys or His ; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 28. The enzyme according to any of the claims 24-27 which enzyme is obtainable from a strain belonging to the class Zygomycetes, preferably to the order Mucorales . 29. The enzyme according to claim 28 which enzyme is obtainable from a strain belonging to the group consisting of the families Mucoracea and Thamnidiaceae , preferably belonging to the group consisting of the ge- nera Jϊhizojπucor, Phycomyces and Chaetostylum . 30. The enzyme according to claim 29 which enzyme is obtainable from a strain belonging the group consisting of the species Rhizomucor pusillus, Phycomyceε nitenε, Chaetoεtylum fresenii, preferably Rhizomucor pusilluε, IFO 4578, Phycomyceε nitenε, IFO 4814, and Chaetoεtylum freεenii , NRRL 2305. 31. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to the group consisting of Ar- chaeaεcomyceteε, Discomycetes, Hermiascomycete , Loculoa¬ scomycetes, and Plectomycetes which enzyme comprises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 32. The enzyme preparation according to claim 31, wherein the amino acid residue in position 7 is cysteine (Cys) . 33. The enzyme preparation according to claim 31, wherein the amino acid residue in position 1 is selected from the group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 34. The enzyme preparation according to any of the claims 31-33, wherein the enzyme comprises a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 35. The enzyme preparation according to any of the claims 31-34 wherein the enzyme is obtainable from a strain belonging to the group consisting of the orders Pezizales, Phytismatales , Dothideales, and Eurotiales . 36. The enzyme preparation according to claim 35 wherein the enzyme is obtainable from a strain belonging the the group consisting of the families Cucurbitariaceae, Rhytismataceae , Ascobolaceae, and Trichocomaceae, pre¬ ferably belonging the the group consisting of the genera Diplodia, Micros phaeropsiε, Ulospora, Macrophomina, Ascobolus, Saccoboluε, Penicillium, and Thermomyceε . 37. The enzyme preparation according to claim 36 wherein the enzyme is obtainable from a strain belonging the the group consisting of the species Diplodia goεεypina, Micros phaeropsiε εp. , Uloεpora bilgramii, Macrophomina phaseolina, Ascobolus stictoideε, Saccoboluε dilutelluε, Penicillium verruculosum, Penicillium chrysogenum, and Thermomyceε verrucoεuε; preferably Diplodia gossypina, CBS 274 .96, Ulospora bilgramii, NKBC 1444, Macrophomina phaseolina, CBS 281.96, Saccoboluε dilutelluε, CBS 275.96, Penicillium verruculoεu , ATCC 62396, Penicillium chrysogenum, ATCC 9480, and Thermomyces verrucoεuε , CBS 285.96. 38. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to the group consisting of the orders Diaportaleε, Xylarialeε, Trichoaphaerialeε and Phyllachoraleε which enzyme comprises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 5 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and 0 Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and 5 in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 39. The enzyme preparation according to claim 38, wherein the amino acid residue in position 7 is cysteine (Cys) . 0 40. The enzyme preparation according to claim 38, wherein the amino acid residue in position 1 is selected from the group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 5 41. The enzyme preparation according to any of the claims 38-40, wherein the enzyme comprises a first peptide consisting of 13 amino acid residues having the following sequence 0 Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues 5 having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 42. The enzyme preparation according to any of the claims 38-41 wherein the enzyme is obtainable from a strain belonging to the group consisting of the families Xylariaceae, Valsaceae, and Phyllachoraceae , preferably belonging to the genera Diaporthe, Colletotrichum, Nigrospora, Xylaria, Nodulisporum and Poronia . 43. The enzyme according to claim 42 which enzyme is ob¬ tainable from a strain belonging to the group consisting of the species Diaporthe syngeneεia, Colletotrichum lagenarium, Nigroεpora εp. , Xylaria hypoxylon, Noduliεporum εp . , and Poronia punctata, preferably Dia- porthe εyngeneεia, CBS 278 .96, Colletotrichum lagenarium, ATCC 52609, Nigroεpora sp. , CBS 272 .96, Xylaria hypoxylon, CBS 284 .96 44. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to the group consisting of the families Nectriaceae, Sordariaceae, Chaetomiaceae, Ceratostomaceae , Lasiosphaeriaceae and the genera Acremonium, Gliocladium, Scytalidium, Cylindrocarpon and Volutella which enzyme comprises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 5 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 0 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 5 45. The enzyme preparation according to claim 44, wherein the amino acid residue in position 7 is cysteine (Cys) . 46. The enzyme preparation according to claim 44, wherein the amino acid residue in position 1 is selected from the 0 group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 47. The enzyme preparation according to any of the claims 44-46, wherein the enzyme comprises a first peptide 5 consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 0 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 5 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 48. The enzyme preparation according to any of the claims 44-47 wherein the enzyme is obtainable from a strain belonging to the group consisting of the genera Cylindro- carpon, Nectria, Volutella, Sordaria, Thielavia, Sypasto- spora, Chaetomium, Myceliophthora, Scytalidium, Cladorrhinum, Gliocladium, Acremonium . 49. The enzyme according to claim 48 which enzyme is ob- tainable from a strain belonging to the group consisting of the species Cylindrocarpon sp. , Nectria pinea, Volu¬ tella colletotrichoides , Sordaria fimicola, Sordaria macrospora, Thielavia terrestriε, Thielavia thermophila, Syspastospora boninensiε, Cladorrhinum foecundiεεimum, Chaetomium murorum, Chaetomium vireεcenε, Chaetomium brasiliensis, Chaetomium cunicolorum, Myceliophthora thermophila, Gliocladium catenulatum, Scytalidium thermophila, and Acremonium sp. , preferably from Gliocladium catenulatum, ATCC 10523 & CBS 227.48, Nectria pinea, CBS 279.96, Volutella colletotrichoides, CBS 400.58, Sordaria fimicola, ATCC 52644, Sordaria macrospora, ATCC 60255, Thielavia terrestriε, NRRL 8126, Thielavia thermophila, CCBS 174 .70, Chaetomium murorum, CBS 163 .52, Chaetomium vireεcenε, CBS 547.75, Chaetomium brasiliensiε, CBS 122.65, Chaetomium cunicolorum, CBS 799.83, Syεpastospora boninensiε, NKBC 1515, Cladorrhinum foecundiεεimum, ATCC 62373, Myceliophthora thermophila, CBS 117.65, Scytalidium thermophila, ATCC 28085, and Acremonium sp. , CBS 478.94 50. An enzyme preparation consisting essentially of an enzyme having cellulytic activity and being obtainable from a strain belonging to the group consisting of the species Fusarium lycopersici, Fusarium passiflora, Fusarium solani, Fusarium anguioides, Fusarium poae, Humicola nigrescens and Humicola grisea which enzyme com- prises an amino acid sequence selected from the group consisting of the sequences Xaa Thr Arg Xaa Phe Asp Xaa 1 2 3 4 5 6 7 ; Xaa Thr Arg Xaa Tyr Asp Xaa 1 2 3 4 5 6 7 ; and Xaa Thr Arg Xaa Trp Asp Xaa 1 2 3 4 5 6 7 wherein, in position 4, Xaa is Trp, Tyr or Phe; and in position 1 and 7, Xaa is any of the 20 naturally occurring amino acid residues. 51. The enzyme preparation according to claim 50, wherein the amino acid residue in position 7 is cysteine (Cys) . 52. The enzyme preparation according to claim 50, wherein the amino acid residue in position 1 is selected from the group consisting of aspartic acid (Asp) , threonine (Thr) and alanine (Ala) . 53. The enzyme preparation according to any of the claims 50-52, wherein the enzyme comprises a first peptide consisting of 13 amino acid residues having the following sequence Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 and a second peptide consisting of 5 amino acid residues having the following sequence Trp Cys Cys Xaa Cys 1 2 3 4 5 wherein, in position 3 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 4 of the first sequence, the amino acid is Trp, Tyr or Phe; in position 8 of the first sequence, the amino acid is Arg, Lys or His; in position 9, 10, and 12, respectively, of the first sequence, and in position 4 of the second sequence, the amino acid is any of the 20 naturally occurring amino acid residues. 54. The enzyme preparation according to claim 53 wherein the enzyme is obtainable from a strain belonging to the group consisting of the strains Fusarium oxysporum sεp lycopersici, CBS 645. 78, Fusarium oxysporum sεp paεεiflora, CBS 744. 79, Fuεarium εolani, IMI 107.511, Fuεarium anguioideε, IFO 4467, Fuεarium poae, ATCC 60883, Humicola nigreεcen , CBS 819.73 and Humicola griεea , ATCC 22726. 55. The enzyme according to any of the claims 14-17, 21- 23, 27-30, 34-37, 41-43, 47-49, 53 and 54, wherein the amino acid residue in position 9 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group consisting of proline and threonine. 56. The enzyme according to any of the claims 14-17, 21- 23, 27-30, 34-37, 41-43, 47-49, 53 and 54, wherein the amino acid residue in position 10 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably serine. 57. The enzyme according to any of the claims 14-17, 21- 23, 27-30, 34-37, 41-43, 47-49, 53 and 54, wherein the amino acid residue in position 12 of the first sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine and tryptophan, preferably from the group consisting of alanine and glycine. 58. The enzyme according to any of the claims 14-17, 21- 23, 27-30, 34-37, 41-43, 47-49, 53 and 54, wherein the amino acid residue in position 4 of the second sequence is selected from the group consisting of proline, threonine, valine, alanine, leucine, isoleucine, phenylalanine, glycine, cysteine, asparagine, glutamine, tyrosine, serine, methionine, tryptophan, glutamic acid and aspartic acid, preferably from the group consisting of alanine, glycine, and glutamine. 59. The enzyme according to any of the claims 14-17, 21- 23, 27-30, 34-37, 41-43, 47-49, 53 and 54, wherein, in the first sequence, the amino acid residue in position 3 is tyrosine; or the amino acid residue in position 4 is tryptophan; or the amino acid residue in position 8 is lysine. 60. A DNA construct encoding for the enzyme according to any of the claims 11-59. 61. The enzyme preparation according to any of the claims 14-17, 21-23, 27-30, 34-37, 41-43, 47-49, 53 and 54, wherein the first sequence comprises an amino acid sequence selected from the group consisting of the sequences Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Ala Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 ; Thr Arg Tyr Trp Asp Cys Cys Lys Thr Ser Cys Ala Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 ; and Thr Arg Tyr Trp Asp Cys Cys Lys Pro Ser Cys Gly Trp 1 2 3 4 5 6 7 8 9 10 11 12 13 . 62. A method for providing a microbial strain comprising a gene encoding for the enzyme present in the enzyme preparation according to any of the claims 1-9, 11-59, and 61 which method comprises hybridization, e.g. PCR amplification, under standard conditions with an oligonucleotide derived from any of the conserved regions illustrated in Fig.l. 63. The method according to claims 62, wherein the oligonucleotide comprises a nucleotide sequence encoding at least a pentapeptide comprised in a peptide selected from the group consisting of a. Thr Arg Xaa Xaa Asp Cys Cys Xaa Xaa Xaa Cys Xaa Trp Xaa 1 2 3 4 5 6 7 8 9 10 11 12 13 14 the amino acid in position 3 or 4 being Trp, Tyr or Phe; the amino acid in postion 8 being Arg, Lys or His; the amino acid in position 9, 10, 12 and 14, respectively, being any of the 20 naturally occurring amino acid residues ; and b. Trp Cys Cys Xaa Cys Tyr 1 2 3 4 5 6 the amino acid in position 4 being any of the 20 natural¬ ly occurring amino acid residues ; and c. Xaa Pro Gly Gly Gly Xaa Gly Xaa Phe 1 2 3 4 5 6 7 8 9 the amino acid in position 1 being Met or lie; the amino acid in position 6 and 8, respectively, being Leu, lie or Val; and d. Gly Cys Xaa Xaa Arg Xaa Asp Trp Xaa 1 2 3 4 5 6 7 8 9 the amino acid in position 3 being any of the 20 natural¬ ly occurring amino acid residues; the amino acid in position 4 and 6, respectively, being Trp, Tyr or Phe; and the amino acid in position 9 being Phe or Met; 64. The method according to claim 62, wherein the oligonucleotide comprises a nucleotide sequence complementary to the sequences of claim 63. 65. The method according to claim 63, wherein the oligonucleotide corresponds to a PCR primer selected from the group consisting of the PCR primers sense, 5 ' -CCCCAAGCTTACI A / c GITA c / τ TGGGA c / τ TG c / τ TG c / τ AA A / α A / c C-3 ' antisense 1, 5'- CTAGTCTAGATA A / 0 CAIGC A / 0 CA A / 0 CACC -3 ' ; antisense 2, 5'- CTAGTCTAGAAAIA A / α / τ ICCIA A / c /°ICCICCICCIGG -3'; and antisense 3, 5 ' - CTAGTCTAGAIAACCA A / α TCA A / 0 A / τ AIC°/ τ CC -3 . 66. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting cellulytic activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 1, and/or the DNA sequence obtainable from the plasmid in Saccharomyceε cerevisiae DSM 9770, or b) an analogue of the DNA secruence shown in SEQ ID No. 1 or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 9770, which i) is homologous, preferably at least 70% homologous, with the DNA sequence shown in SEQ ID No. 1 and/or the DNA sequence obtainable from the plasmid in Saccharomyceε cereviεiae DSM 9770, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 1 and/or the DNA sequence obtainable from the plasmid in Saccharomyceε cerevisiae DSM 9770, iii) encodes a polypeptide which is homologous preferably at least 65% homologous, with the poly- peptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 1 and/or the DNA sequence obtainable from the plasmid in Sac¬ charomyces cerevisiae DSM 9770, iv) encodes a polypeptide which is immunologically re- active with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 1 or obtainable from the plasmid in Saccharomyceε cereviεiae , DSM 9770. 67. The DNA construct according to claim 66, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family Chaetomiaceae, preferably to the genus Myceliophthora, in particular a strain of M. thermophila , especially M. thermophila , CBS 117.65. 68. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 4, and/or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10082, or b) an analogue of the DNA sequence shown in SEQ ID No. 4 or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10082, which i) is homologous, preferably at least 70% homologous, with the DNA sequence shown in SEQ ID No. 4 and/or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10082, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 4 and/or the DNA sequence obtainable from the plasmid in Saccharomyces cereviεiae DSM 10082, iii) encodes a polypeptide which is homologous preferably at least 60% homologous, with the poly- peptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. and/or the DNA sequence obtainable from the plasmid in Sac¬ charomyceε cereviεiae DSM 10085, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 4 or obtainable from the plasmid in Saccharomyceε cereviεiae , DSM 10082. 69. The DNA construct according to claim 68, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family Hypocreaceae , preferably to the genus Acremonium, in par¬ ticular Acremonium sp. , CBS 478.94. 70. A DNA construct comprising a DNA secruence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 6, or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10080, or b) an analogue of the DNA sequence shown in SEQ ID No. 6 or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10080, which i) is homologous, preferably 65% homologous, with the DNA sequence shown in SEQ ID No. 6 or the DNA sequence obtainable from the plasmid in Sac¬ charomyces cerevisiae DSM 10080, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 6 or the DNA sequence obtai- nable from the plasmid in Saccharomyces cerevisiae DSM 10080, iii) encodes a polypeptide which is homologous, preferably at least 70%, with the polypeptide encoded by a DNA sequence comprising the DNA se- quence shown in SEQ ID No. 6 or the DNA sequence obtainable from the plasmid in Saccharomyceε cereviεiae DSM 10080, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 6 /or obtainable from the plasmid in Saccharomyceε cereviεiae , DSM 10080. 71. The DNA construct according to claim 70, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family Chaetomiceae, preferably to the genus Acremonium, in par- ticular Acremonium sp. , CBS 478.94. 72. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 8, or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10081, or b) an analogue of the DNA secruence shown in SEQ ID No. 8 or the DNA sequence obtainable from the plasmid in Saccharomyces cerevisiae DSM 10081, which i) is homologous, preferably at least 75% homologous, with the DNA sequence shown in SEQ ID No. 8 or the DNA sequence obtainable from the plasmid in Sac- charomyces cerevisiae DSM 10081, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 8 or the DNA sequence obtai¬ nable from the plasmid in Saccharomyces cereviεiae DSM 10081, iii) encodes a polypeptide which is homologous, preferably at least 70% homologous, with the poly¬ peptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 8 or the DNA sequence obtainable from the plasmid in Saccharomyceε cerevisiae DSM 10081, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 8 or obtainable from the plasmid in Saccharomyces cerevisiae , DSM 10081. 73. The DNA construct according to claim 72, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family Chaetomiaceae , preferably to the genus Thielavia, in par¬ ticular a strain of Thielavia terrestriε , especially Thielavia terrestris , NRRL 8126. 74. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 10, or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10512, or b) an analogue of the DNA sequence shown in SEQ ID No. 10 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10512, which i) is homologous, preferably at least 65% homologous, with the DNA sequence shown in SEQ ID No. 10 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10512, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 10 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10512, iii) encodes a polypeptide which is homologous, preferably at least 55% homologous, with the polypeptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 10 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10512, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 10 or obtainable from the plasmid in Escherichia coli , DSM 10512. 75. The DNA construct according to claim 74, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family Rhytismataceae , preferably to the genus Macrophomina, in particular Macrophomina phaseolina, especially M.phaseolicola, CBS 281 .96. 76. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 12, or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10511, or b) an analogue of the DNA sequence shown in SEQ ID No. 12 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10511, which i) is homologous, preferably at least 60% homologous, with the DNA sequence shown in SEQ ID No. 12 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10511, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 12 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10511, iii) encodes a polypeptide which is homologous, preferably at least 60% homologous, with the polypeptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 12 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10511, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 12 or obtainable from the plasmid in Eεcherichia coli , DSM 10511. 77. The DNA construct according to claim 76, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family Tricholomataceae, preferably to the genus Crinipelliε, in particular Crinipellis scabella, especially C. scabella, CBS 280.96. 78. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 16, or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10571, or b) an analogue of the DNA sequence shown in SEQ ID No. 16 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10571, which i) is homologous, preferably at least 70 % homologous, with the DNA sequence shown in SEQ ID No. 16 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10571, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 16 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10571, iii) encodes a polypeptide which is homologous, preferably at least 60% hoologous, with the polypeptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 16 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10571, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 16 or obtainable from the plasmid in Eεcherichia coli , DSM 10571. 79. The DNA construct according to claim 78, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain of Volutella, in particular Volutella colletotrichoides, especially V. colletotrochoides, CBS 400.58. 80. A DNA construct comprising a DNA sequence encoding an enzyme exhibiting endoglucanase activity, which DNA sequence comprises a) the DNA sequence shown in SEQ ID No. 19, or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10576, or b) an analogue of the DNA sequence shown in SEQ ID No. 19 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10576, which i) is homologous with the DNA sequence shown in SEQ ID No. 19 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10576, ii) hybridizes under the conditions described herein with the same nucleotide probe as the DNA sequence shown in SEQ ID No. 19 or the DNA sequence obtainable from the plasmid in Escherichia coli , DSM 10576, iii) encodes a polypeptide which is homologous with the polypeptide encoded by a DNA sequence comprising the DNA sequence shown in SEQ ID No. 19 or the DNA sequence ob¬ tainable from the plasmid in Escherichia COli, DSM 10576, iv) encodes a polypeptide which is immunologically reactive with an antibody raised against the purified endoglucanase encoded by the DNA sequence shown in SEQ ID No 19 or obtainable from the plasmid in Escherichia coli , DSM 10576. 81. The DNA construct according to claim 80, in which the DNA sequence is isolated from or produced on the basis of a DNA library of a strain belonging to the family of Sordariaceae, preferably to the genus Sordaria, in par- ticular Sordaria fimicola , especially S. fimicola, ATCC 52644. 82. The DNA construct according to any of the claims 66- 81 which further comprises a DNA sequence encoding a cellulose-binding domain. 83. The DNA construct according to claim 82 which further comprises a DNA sequence encoding a cellulose-binding doain (CBD) , the cellulose-binding domain and enzyme core (catalytically active domain) of the enzyme encoded by the DNA sequence of the DNA construct being operably linked. 84. A recombinant expression vector comprising a DNA construct according to any of claims 62-83. 85. A cell comprising a DNA construct according to any of claims 66-83 or a recombinant expression vector according to claim 84. 86. A cell according to claim 85, which is a eukaryotic cell, in particular a fungal cell, such as a yeast cell or a filamentous fungal cell, or an endogenous cell from which the gene originates. 87. A cell according to claim 86, wherein the cell belongs to a strain of Aspergillus, Fusarium, or Trichoderma , in particular a strain of Fusarium graminearum, Aspergillus niger or Aspergillus oryzae . 88. A method of producing an enzyme exhibiting endoglucanase activity, the method comprising culturing a cell according to any of claims 85-87 under conditions permitting the production of the enzyme, and recovering the enzyme from the culture. 89. An enzyme exhibiting endoglucanase activity, which enzyme a) is encoded by a DNA construct according to any of claims 66-83, b) produced by the method according to claim 88, or c) is immunologically reactive with an antibody raised against a purified endoglucanase encoded by the DNA sequence shown in any of the sequence listings SEQ ID No 1, 4, 6, 8, 10, 12, 16, 19. 90. A method of providing colour clarification of laun¬ dry, which method comprising treating the laundry with a soaking, washing or rinsing liquor comprising an enzyme preparation according to any of the claims 1-9, 11-61 and 89. 91. The method according to claim 90, wherein the laundry is treated in a washing machine. 92. The method according to claim 90 or 91, wherein the endoglucanase is present in the soaking, washing, or rinsing liquor in an effective amount of between 1 and 1000 S-CEVU, preferably between 5 and 200 S-CEVU, per liter of liquor during machine cycle use conditions. 93. The method according to any of the claim 90-92, wherein the pH of the soaking, washing, or rinsing liquor is between 4 and 11, preferably between 6 and 10.5. 94. The method according to any of the claims 90-93, whrein the temperature is between 15 * C and 60 * C. 95. The method according to any of the claims 90-94, wherein the soaking, washing or rinsing liquor further comprises one or more enzymes selected from the group consisting of proteases, cellulases, xylanases, amylases, Upases, peroxidases and laccases. 96. A laundry composition comprising the enzyme preparation according to any of the claims 1-9, 11-61 and 89, and a compound selected from the group consisting of a surfactant, a builder compound, and a fabric softening agent. 97. The laundry composition according to claim 96, which further comprises one or more enzymes selected from the group consisting of proteases, amylases, lipases, cellulases, xylanases, peroxidases and laccases. 98. The composition according to claim 97, wherein the surfactant is a nonionic, anionic, cationic, zwitterionic, ampholytic or amphoteric surfactant. 99. The composition according to claim 98, wherein the fabric softening agent is a cationic or nonionic soften¬ ing agent, preferably a quaternary ammonium compound, and which optionally further comprises one or more compounds selected from a surfactant, an electrolyte, a buffer, an antioxidant and a liquid carrier. 100. Use of the enzyme according to any of the claims 1- 9, 11-61 and 89 for degradation or modification of plant material, e.g. cell walls. 101. Use of the enzyme according to any of the claims 1- 9, 11-61 and 89 for treatment of fabric or textile, preferably for preventing backstaining, for bio-polishing or for "stone-washing" cellulosic fabric. 102. Use of the enzyme according to any of the claims 1- 9, 11-61 and 89 in the treatment of paper pulp, pre¬ ferably for debarking, defibration, fibre modification, enzymatic de-inking or drainage improvement. 103. An enzyme preparation which is enriched in an enzyme exhibiting cellulytic activity according to any of the claims 1-9, 11-61 and 89. 104. The preparation according to claim 103, which additionally comprises one or more enzymes selected from the group consisting of galactanases, xylanases, arabinanases, pectin acetyl esterases, polygalacturonases, rhamnogalacturonases, pectin lyases, pectate lyases, endoglucanases, pectin methylesterases, proteases, lipases, amylases, cutinases, peroxidases, laccases, cellobiohydrolases and transglutaminases.

Inventors: ANDERSEN LENE NONBOE, IHARA MICHIKO, KAUPPINEN MARKUS SAKARI, LANGE LENE, LASSEN SOEREN FLENSTED, NIELSEN RUBY ILUM, SCHUELEIN MARTIN, TAKAGI SHINOBU, ANDERSEN, LENE, NONBOE, IHARA, MICHIKO, KAUPPINEN, MARKUS, SAKARI, LANGE, LENE, LASSEN, SOEREN, FLENSTED, NIELSEN, RUBY, ILUM, SCHUELEIN, MARTIN, TAKAGI, SHINOBU
Applicants: ANDERSEN LENE NONBOE, IHARA MICHIKO, KAUPPINEN MARKUS SAKARI, LANGE LENE, LASSEN SOEREN FLENSTED, NIELSEN RUBY ILUM, NOVONORDISK AS, SCHUELEIN MARTIN, TAKAGI SHINOBU, ANDERSEN, LENE, NONBOE, IHARA, MICHIKO, KAUPPINEN, MARKUS, SAKARI, LANGE, LENE, LASSEN, SOEREN, FLENSTED, NIELSEN, RUBY, ILUM, NOVO NORDISK A/S, SCHUELEIN, MARTIN, TAKAGI, SHINOBU
Application year: 1996
Main classification: C12N9
IPC codes: C05F11, C05F17, C11D3, C12N1, C12N9, C12N15, C12R1, C12S3, C12S11, D06M13, D06M16, D06P5, D21C5, D21H11, D21H17, D21H21