DETERGENT COMPOSITIONS HAVING IMPROVED WASH PERFORMANCE COMPRISING A SUBTILASE VARIANT AND A SURFACTANT

Abstract: The present invention relates to novel detergent compositions, in particular to novel laundry detergent compositions, comprising a subtilase variant and alkylpolysaccharides, polyhydroxy fatty acid amides or alpha -sulfonated fatty acid esters having an improved wash performance.

Description: DETERGENT COMPOSITIONS HAVING IMPROVED WASH PERFORMANCE COMPRISING A SUBTILASE VARIANT AND A SURFACTANT TECHNICAL FIELD The present invention relates to novel detergent compositions, in particular to novel laundry detergent compositions, comprising a subtilase variant and certain specific surfactants, where said compositions exhibit an improved wash performance. BACKGROUND OF THE INVENTION In the detergent industry enzymes have for more than 30 years been implemented in washing formulations. Enzymes used in such formulations comprise proteases, lipases, amylases, cellulases, as well as other enzymes, or mixtures thereof. Commercially most important enzymes are proteases . An increasing number of commercially used proteases are protein engineered variants of naturally occurring wild type proteases, e.g. DURAZYM * (Novo Nordisk A/S) , RELASE ® (Novo Nordisk A/S) , MAXAPEM ® (Gist-Brocades N.V.), PURAFECT ® (Genencor International, Inc . ) . Further a number of protease variants are described in the art, such as in EP 130756 (GENENTECH) (corresponding to US Reissue Patent No. 34,606 (GENENCOR)); EP 214435 (HENKEL); WO 87/04461 (AMGEN); WO 87/05050 (GENEX) ; EP 260105 (GENENCOR); Thomas, Russell, and Fersht (1985) Nature 318 375-376; Thomas, Russell, and Fersht (1987) J " . Mol . Biol . 193 803-813; Russel and Fersht Nature 328 496-500 (1987) ; WO 88/08028 (Genex) ; WO 88/08033 (Amgen); WO 95/27049 (SOLVAY S.A.); WO 95/30011 (PROCTER & GAMBLE COMPANY) ; WO 95/30010 (PROCTER & GAMBLE COMPANY) ; WO 95/29979 (PROCTER & GAMBLE COMPANY); US 5.543.302 (SOLVAY S.A.); EP 251 446 (GENENCOR) ; WO 89/06279 (NOVO NORDISK A/S) ; WO 91/00345 (NOVO NORDISK A/S) ; EP 525 610 Al (SOLVAY) ; and WO 94/02618 (GIST- BROCADES N.V.) . The currently used proteases have for the most part been found by isolating proteases from nature and testing them in detergent formulations . However, although proteases have been used in the detergent industry for more than 30 years, much remains unknown as to details of how these enzymes interact with substrates and/or other substances present in e . g. detergent compositions. Some factors re- lated to specific residues of the proteases and influencing certain properties, such as oxidative and thermal stability in general, of the proteases have been elucidated, but much remains to be found out. Also, it is still not exactly known which physical or chemical characteristics are responsible for a good washing performance or stability of a protease in a specific detergent composition. A large research effort has been devoted to the field of preparing improved, cheap and environmentally desirable detergents. A detailed description of various cleaning compositions comprising protease variants can, for example, be found in WO 99/20727 (PROCTER & GAMBLE COMPANY) . However, due to consumers demand there is still a need in this technical field for new detergent compositions having improved washing performance . Accordingly, it is an object of the present invention to provide novel detergent compositions having an improved washing perfor- mance . SUMMARY OF THE INVENTION It has now surprisingly been found that detergent compositions comprising one or more of the specific variants described herein in combination with the specific surfactants disclosed herein show an improved washing performance when compared to similar detergent composition not comprising such specific surfactants. In other words, detergent compositions comprising i ) the specific variants mentioned herein, and ii ) the specific surfactants men- tiond herein have been found to exhibit excellent washing performance . Thus, the present invention relates to a detergent composition comprising an effective amount of a subtilase variant, where the subtilase variant comprises a modification of the amino acid sequence at a calcium binding site such that the electrostatic at- tractive interaction between the amino acids at the calcium binding site and the calcium ion is increased relative to that of the corresponding parent subtilase, and an effective amount of a surfactant selected from the group consisting of an alkylpolysaccharide comprising a hydrophobic moiety having from about 6 to about 30 carbon atoms and a hydrophilic moiety derived from a polysachharide containing from about 1.3 to about 10 saccharide units; a polyhydroxy fatty acid amide of the general formula (I) : R 2 -C(=0) -N(R X ) (Z) (I) wherein R 1 is selected from the group consisting of hydrogen, C-- C 4 -hydrocarbyl, 2-hydroxyethyl, and 2-hydroxypropyl; R 2 is C 5 -C 31 hydrocarbyl, such as C 5 -C 31 -alkyl or C 5 -C 31 -alkenyl ; and Z is selected from the group consisting of glucose, fructose, maltose, lactose, galactose, mannose and xylose; and an α-sulfonated fatty acid esters. DEFINITONS Prior to discussing this invention in further detail, the following terms and conventions will first be defined. Nomenclature of amino acids A Ala = Alanine V Val = Valine L Leu = Leucine I He = Isoleucine P Pro = Proline F Phe = Phenylalanine W Trp = Tryptophan M Met = Methionine G = Gly = Glycine S = Ser = Serine T = Thr = Threonine c = Cys = Cysteine Y = Tyr = Tyrosine N = Asn = Asparagine Q = Gin = Glutamine D = Asp = Aspartic Acid E = Glu = Glutamic Acid K = Lys = Lysine R = Arg = Arginine H = His = Histidine X = Xaa = Any amino acid Nomenclature of nucleic acids A = Adenine G = Guanine C = Cytosine T = Thymine (only in DNA) U = Uraci 1 (only in RNA) Nomenclature and conventions for designation of variants In describing the various enzyme variants produced or contemplated according to the invention, the following nomenclatures and conventions have been adapted for ease of reference: A frame of reference is first defined by aligning the isolated or parent wild type enzyme with subtilisin BPN' (BASBPN) . The alignment can be obtained by the GAP routine of the GCG package version 9.1 to number the variants using the following parameters: gap creation penalty = 8 and gap extension penalty = 8 and all other parameters kept at their default values. Another method is to use known recognised alignments between sub- tilases, such as the alignment indicated in WO 91/00345. In most cases the differences will not be of any importance. Such alignments between subtilisin BPN' (BASBPN) and subtilisin 309 (BLSAVI or BLS309) and subtilisin Carlsberg (BLSCAR) , respectively are indicated in Figs. 1, la, 2, and 2a. By this a number of deletions and insertions will be defined in relation to BASBPN. In Fig. 1 subtilisin 309 has 6 deletions in positions 36, 58, 158, 162, 163, and 164 in comparison to BASBPN, whereas in Fig. la subtilisin 309 has the same deletions in positions 36, 56, 159, 164, 165, and 166 in comparison to BASBPN. In Fig. 2 subtilisin Carlsberg has one deletion in position 58 in compari- son to BASBPN, whereas in Fig. 2a subtilisin Carlsberg has the one deletion in position 56 in comparison to BASBPN. These deletions are in Figs. 1, la, 2, and 2a indicated by asterixes (*) . The various modifications performed in a wild type enzyme is in- dicated in general using three elements as follows: Original amino acid Position Substituted amino acid The notation G195E thus means a substitution of a glycine in po- sition 195 with a glutamic acid. Position Substituted amino acid In the case when the original amino acid residue may be any amino acid residue, a short hand notation may at times be used indicat- ing only the position and substituted amino acid, Such a notation is particular relevant in connection with modification (s) in homologous subtilases. Original amino acid Position This notation can be used when the amino acid residue (s) replacing a specific amino acid in a position is immaterial. Position When both the original amino acid(s) and substituted amino acid(s) may comprise any amino acid, then only the position is indicated, e.g.: 170. Original amino acid position (substituted amino acid^, . . . , substituted amino acid n ) When the original amino acid(s) and/or substituted amino acid(s) may comprise more than one, but not all amino acid(s), then the selected amino acids are indicated inside brackets { } , For specific variants the specific three or one letter codes are used, including the codes Xaa and X to indicate any amino acid residue . Substitutions The substitution of Glutamic acid for glycine in position 195 is designated as : Glyl95Glu or G195E or the substitution of any amino acid residue acid for glycine in position 195 is designated as: Glyl95Xaa or G195X or Glyl95 or G195 The substitution of serine for any amino acid residue in position 170 would thus be designated Xaal70Ser or X170S. or 170Ser or 170S Such a notation is particular relevant in connection with modification^) in homologous subtilases { vide infra) . 170Ser is thus meant to comprise e . g. both a Lysl70Ser modification in BASBPN and an Argl70Ser modification in BLSAVI (cf . Fig. 1) . For a modification where the original amino acid(s) and/or substituted amino acid(s) may comprise more than one, but not all amino acid(s), the substitution of glycine, alanine, serine or threonine for arginine in position 170 would be indicated by Argl70{Gly,Ala,Ser,Thr} or R17θ{G,A, S, T} to indicate the variants R170G, R170A, R170S, and R170T. Deletions : A deletion of glycine in position 195 will be indicated by: Glyl95* or G195* Correspondingly the deletion of more than one amino acid residue, such as the deletion of glycine and leucine in positions 195 and 196 will be designated Glyl95*+Leul96* or G195*+L196* Insertions : The insertion of an additional amino acid residue such as e . g. a lysine after G195 is : Glyl95GlyLys or G195GK; or when more than one amino acid residue is inserted, such as e . g. a Lys, Ala and Ser after G195 this is : Glyl95GlyLysAlaSer or G195GKAS In such cases the inserted amino acid residue (s) are numbered by the addition of lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue (s) . In the above example the sequences 194 to 196 would thus be: 194 195 196 BLSAVI A - G - L 194 195 195a 195b 195c 196 Variant A - G - K - A - S - L In cases where an amino acid residue identical to the existing amino acid residue is inserted it is clear that a degeneracy in the nomenclature arises. If for example a glycine is inserted after the glycine in the above example this would be indicated by G195GG. The same actual change could just as well be indicated as A194AG for the change from 194 195 196 BLSAVI A - G - L to 194 195 195a 196 Variant A - G - G - L 194 194a 195 196 Such instances will be apparent to the skilled person, and the indication G195GG and corresponding indications for this type of insertions are thus meant to comprise such equivalent degenerate indications . Some times it is desired to both perform a modification and an insertion at the same time. This situation is also covered by the present definitions. Thus S130TP indicatets that the serine in position 130 has been replaced by a tyrosine and a proline has been inserted between positions 130 and 131. A more cumbersome way of describing such a variant would be: S130SP+S130T. Filling a gap: Where a deletion in an enzyme exists in the reference comparison with the subtilisin BPN' sequence used for the numbering, an insertion in such a position is indicated as: *36Asp or *36D for the insertion of an aspartic acid in position 36. Multiple modifications: Variants comprising multiple modifications are separated by pluses, e . g. : Argl70Tyr+Glyl95Glu or R170Y+G195E representing modifications in positions 170 and 195 substituting tyrosine and glutamic acid for arginine and glycine, respectively, or e . g. Tyrl67{Gly,Ala, Ser, Thr}+Argl70 {Gly,Ala, Ser,Thr} designates the variants Tyrl67Gly+Argl70Gly, Tyrl67Gly+Argl70Ala, Tyrl67Gly+Argl70Ser, Tyrl67Gly+Argl70Thr, Tyrl67Ala+Argl70Gly, Tyrl67Ala+Argl70Ala, Tyrl67Ala+Argl70Ser, Tyrl67Ala+Argl70Thr, Tyrl67Ser+Argl70Gly, Tyrl67Ser+Argl70Ala, Tyrl67Ser+Argl70Ser, Tyrl67Ser+Argl70Thr, Tyrl67Thr+Argl70Gly, Tyrl67Thr+Argl70Ala, Tyrl67Thr+Argl70Ser, and Tyrl67Thr+Argl70Thr . This nomenclature is particular relevant relating to modifications aimed at substituting, replacing, inserting or deleting amino acid residues having specific common properties, such as residues of positive charge (K, R, H) , negative charge (D, E) , or conservative amino acid modification (s) of e . g. Tyrl67{Gly,Ala, Ser,Thr}+Argl7θ{Gly, Ala, Ser,Thr} , which signifies substituting a small amino acid for another small amino acid. See section "De- tailed description of the invention" for further details. Numbering of amino acid positions/residues: If nothing else is mentioned the amino acid numbering used herein corresponds to that of the subtilase BPN" (BASBPN) sequence. For further description of the BPN' sequence see Figs. 1 and 2, or Siezen et al . , Protein Engng. 4 (1991) 719-737. Proteases : Enzymes cleaving the amide linkages in protein substrates are classified as proteases, or (interchangeably) peptidases (see Walsh, 1979, Enzymatic Reaction Mechanisms . W.H. Freeman and Company, San Francisco, Chapter 3) . Serine proteases : A serine protease is an enzyme which catalyzes the hydrolysis of peptide bonds, and in which there is an essential serine residue at the active site (White, Handler and Smith, 1973 " Principles of Biochemistry, " Fifth Edition, McGraw-Hill Book Company, NY, pp. 271-272) . The bacterial serine proteases have molecular weights in the 20,000 to 45,000 Dalton range. They are inhibited by diisopropyl- fluorophosphate . They hydrolyze simple terminal esters and are similar in activity to eukaryotic chymotrypsin, also a serine protease. A more narrow term, alkaline protease, covering a sub-group, reflects the high pH optimum of some of the serine proteases, from pH 9.0 to 11.0 (for review, see Priest (1977) Bacteriological Rev. 41 711-753) . Subtilases . A sub-group of the serine proteases tentatively designated subtilases has been proposed by Siezen et al . , Protein Engng. 4 (1991) 719-737 and Siezen et al . Protein Science 6 (1997) 501-523. They are defined by homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin- like proteases. A subtilisin was previously often defined as a serine protease produced by Gram-positive bacteria or fungi, and according to Siezen et al . now is a subgroup of the subtilases. A wide variety of subtilases have been identified, and the amino acid sequence of a number of subtilases has been determined. For a more detailed description of such subtilases and their amino acid sequences reference is made to Siezen et al . (1997) . One subgroup of the subtilases, I-Sl or "true" subtilisins, comprises the "classical" subtilisins, such as subtilisin 168 (BSS168) , subtilisin BPN' (BASBPN) , subtilisin Carlsberg (BLSCAR) (ALCALASE ® , NOVO NORDISK A/S) , and subtilisin DY (BSSDY) . A further subgroup of the subtilases, I-S2 or high alkaline subtilisins, is recognised by Siezen et al . Sub-group I-S2 proteases are described as highly alkaline subtilisins and comprises enzymes such as subtilisin PB92 (BAALKP) (MAXACAL ® , Gist-Brocades NV) , subtilisin 309 (BLSAVI or BLS 309) (SAVINASE ® , NOVO NORDISK A/S) , subtilisin 147 (BLS147) (ESPERASE ® , NOVO NORDISK A/S) , and alkaline elastase YaB (BSEYAB) . "SAVINASE®" : SAVINASE® is marketed by NOVO NORDISK A/S. It is subtilisin 309 from B. Lentus and differs from BAALKP only in one position (N87S, see Fig. 1 herein) . SAVINASE® has the amino acid sequence designated b) in Fig. 1. Parent subtilase: The term "parent subtilase" describes a subtilase defined according to Siezen et al . (1991 and 1997) . For further details see description of "SUBTILASES" immediately above. A parent subtilase may also be a subtilase isolated from a natural source, wherein subsequent modification have been made while retaining the characteristic of a subtilase. Alternatively the term "parent subtilase" may be termed "wild type subtilase" . Modification (s) of a subtilase variant: The term "modification (s) " used herein is defined to include chemical modification of a subtilase as well as genetic manipulation of the DNA encoding a subtilase. The modification (s) can be replacement (s) of the amino acid side chain(s), substitution (s) , deletion (s) and/or insertions in or at the amino acid(s) of in- terest. Subtilase variant: In the context of this invention, the term subtilase variant or mutated subtilase means a subtilase that has been produced by an organism which is expressing a mutant gene derived from a parent microorganism which possessed an original or parent gene and which produced a corresponding parent enzyme, the parent gene having been mutated in order to produce the mutant gene from which said mutated subtilase protease is produced when expressed in a suitable host. Homologous subtilase sequences: Specific active site loop regions, and amino acid insertions in said loops of the subtilase SAVINASE® are identified for modification herein to obtain a subtilase variant of the invention. However, the invention is not limited to modifications of this particular subtilase, but extends to other parent (wild-type) subtilases, which have a homologous primary structure to that of SAVINASE®. The homology between two amino acid sequences is in this context described by the parameter "identity" . In order to determine the degree of identity between two subtilases the GAP routine of the GCG package version 9.1 can be applied using the same settings as indicated above. The output from the routine is besides the amino acid alignment the calculation of the "Percent Identity" between the two sequences. Based on this description it is routine for a person skilled in the art to identify suitable homologous subtilases and corresponding homologous active site loop regions, which can be modi- fied according to the invention. Isolated DNA sequence: The term "isolated", when applied to a DNA sequence molecule, denotes that the DNA sequence has been removed from its natural ge- netic milieu and is thus free of other extraneous or unwanted coding sequences, and is in a form suitable for use within genetically engineered protein production systems. Such isolated molecules are those that are separated from their natural environment and include cDNA and genomic clones. Isolated DNA mole- cules of the present invention are free of other genes with which they are ordinarily associated, but may include naturally occurring 5' and 3' untranslated regions such as promoters and terminators. The identification of associated regions will be evident to one of ordinary skill in the art (see for example, Dynan and Tijan, Nature 316:774-78, 1985). The term "an isolated DNA sequence" may alternatively be termed "a cloned DNA sequence" . Isolated protein: When applied to a protein, the term "isolated" indicates that the protein has been removed from its native environment . In a preferred form, the isolated protein is substantially free of other proteins, particularly other homologous proteins (i.e. "homologous impurities" (see below) ) . An isolated protein is greater than 10 % pure, preferably greater than 20 % pure, more preferably greater than 30 % pure, as deter- mined by SDS-PAGE. Further it is preferred to provide the protein in a highly purified form, i.e., greater than 40% pure, greater than 60% pure, greater than 80% pure, more preferably greater than 95% pure, and even more preferably greater than 99% pure, as determined by SDS-PAGE. The term "isolated protein" may alterna- tively be termed "purified protein" . Homologous impurities: The term "homologous impurities" means any impurity (e.g. another polypeptide than the desired polypeptide) which originate from the homologous cell where the polypeptide of the invention is originally obtained from. Obtained from: The term "obtained from" as used herein in connection with a spe- cific microbial source, means that the polynucleotide and/or polypeptide is produced by the specific source, or by a cell in which a gene from the source has been inserted. Substrate : The term "Substrate" used in connection with a substrate for a protease should be interpreted in its broadest form as comprising a compound containing at least one peptide bond susceptible to hydrolysis by a subtilisin protease. Product: The term "product" used in connection with a product derived from a protease enzymatic reaction should in the context of this invention be interpreted to include the products of a hydrolysis reaction involving a subtilase protease. A product may be the substrate in a subsequent hydrolysis reaction. Free energy : The term "free energy" is used in its conventional meaning, i.e. as a thermodynamic quantity which describes the behavior of systems in dynamic equilibrium. The symbol G represents the Gibbs free energy. Electrostatic attractive interaction: The "electrostatic attractive interaction" is defined with reference to Coulomb's law: ΔE = (Z-Z b -e 2 )/(D eff -r ab ) where ΔE is the energy change that results from bringing two charges, a and b initially separated by infinity, to some distance, r ab . Z a and Z^ are the respective number of unit charges; e is one unit of charge; and D eff is the effective dielectric constant of the medium separating the charges. When the charges a and b are of opposite signs, the coulombic interaction is attractive. When the positive charge is a divalent metal ion, and the negative charges come from an array of points in the structure of a protein, then the same energy involved in this attractive interaction must be overcome in order to unfold the protein. This means that the free energy of metal ion binding is added to the overall free energy change for unfolding, ΔG U , thus making this latter parameter more positive and shifting the equilibrium to the folded state. Metal ion binding site: A structural segment or segments of polypeptide chain folded in such a way so as to give the proper geometry and electrostatic configuration for binding a divalent metal ion. This is the physical arrangement of protein atoms around a bound metal ion. Protein stability: Protein is defined herein in terms of the ΔG of unfolding. The larger ΔG the more the equilibrium folded <-> unfolded is shifted in favor of the folded state. One can get an estimate of ΔG U from the midpoint of the unfolding transition, T m , measured by scanning calorimetry. Alternatively one may measure the kinetic stability of a protein from the rate of thermal inactivation. Detergent composition: When used herein, the term "detergent composition" is intended to cover cleaning compositions which may have been formulated as hand or machine laundry detergents compositions, including laundry additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics. The term "detergent composition" is also intended to cover rinse added fabric softener compositions as well as compositions for use in general household hard surface cleaning operations and dishwashing operations. Such detergent compositions may be in the form of powder, liquid, paste, gel, bars or granules. Wash performance : The ability of an enzyme (typically incorporated in a detergent) to catalyze the degradation of various naturally occurring substrates present on the objects to be cleaned during e. g. wash is often referred to as its washing ability, washability, detergency, or wash performance. Throughout this application the term wash performance will be used to encompass this property. BRIEF DESCRIPTION OF THE DRAWINGS Fig. 1 shows an alignment between subtilisin BPN' (a) and Savi- ® nase (b) using the GAP routine mentioned above. Fig. la shows the alignment between subtilisin BPN' and Savinase as taken from WO 91/00345. Fig. 2 shows an alignment between subtilisin BPN' and subtilisin Carlsberg using the GAP routine mentioned above. Fig. 2a shows the alignment between subtilisin BPN' and subtilisin Carlsberg as taken from WO 91/00345. Fig. 3 shows the three dimensional structure of Savinase (Protein data bank (PDB) entry 1SVN) . DETAILED DESCRIPTION OF THE INVENTION Subtilase variants suitable for incorporation in the composition of the invention: As indicated above, the present inventors have surprisingly found that the combination of certain specific subtilase variants certain surfactants shows an improved wash performance. The present section relates to the specific subtilase variants suitable for incorporation in the detergent compositions of the invention. Subtilase variants which are useful for the purposes described herein are such subtilase variants as described in EP 0 353 250 (NOVO NORDISK A/S) and EP 0 916 732 (NOVO NORDISK A/S) , which are hereby incorporated by reference . Thus, at its most general level, suitable subtilase variants to be incorporated in the detergent compositions of the invention comprise a modification of the amino acid sequence at a calcium binding site such that the electrostatic attractive interaction between the amino acids at the calcium binding site and the calcium ion is increased relative to that of the corresponding parent subtilase. The guide for designing the alteration of the metal ion binding site through the substitution, deletion, or insertion of amino acid residues is Coulomb's law: ΔE = (Z a -Z b -e 2 )/(D eff -r ab ) where ΔE, measured in Kcal/mole, is the change in energy for a system that consists of two point charges, a and b, as they are brought together as a function of their distance of separation, r a j-). Z a and Z^ are the respective number of unit charges; e is one unit of electronic charge (4.8032xl0 -10 esu) ; and D eff is the effective dielectric constant of the medium separating the charges. In the case of a divalent metal cation binding site, Z a = 2+. If = Zfc is a charge of the opposite sign then the interac- tion is attractive and the energy of the system is decreased. If, on the other hand, the sign of Zj-, is positive then the interaction becomes repulsive and the energy of the system is increased. It should be noted that for natural systems like proteins, where the charges are not point charges, there is a limit to how small r ab can become before steric problems result. The lower limit of r ab therefore has been found to be in the range of 2 to 3 A for low molecular weight ion complexes. The special case where the electrostatic interaction is between a metal ion and negatively charged or dipolar ligands has been thoroughly studied and understood through the use of the electrostatic crystal field theory (CFT) first expounded by H. Bethe in 1929. This theory treats the interaction between the metal ion and the ligands as a purely electrostatic problem in which the ligands are treated as point charges (or point dipoles) . This theory did not adequately explain the covalent nature of some metal-ligand interactions and has been modified into the adjusted crystal field theory (ACFT) or the ligand field theory (LFT) in order to allow for covalency (Cotton & Wilkinson, Advanced Inorganic Chemistry, Interscience, John Wiley pub. , N.Y. 3d ed. (1972) ) . However, in the cases where the divalent metal ion in question is from the Group II metals, i.e., Mg 2+ , Ca 2+ , Sr 2+ , and Ba 2+ , then the CFT does quite well in predicting geometry, affin- ity (K^) , and other physical chemical parameters of these metal ion complexes. The reason for the CFT success in these cases is due to the fact that the d electron orbitals responsible for the covalency of transition metal ion complexes are empty for the Group II divalent metal ions, thereby greatly simplifying the correlation of experimental results with theory. One major source of uncertainty that is encountered in electrostatic interactions in proteins is the dielectric constant. It varies non-uniformly depending on shielding and charge effects. Many attempts have been made to simulate the effective screening (dielectric value) of electrostatic charges inside the tertiary structures of folded proteins (Matthew, Ann. Rev. Biophys. Chem., 14:387-417 (1985)). Even the most sophisticated models, however, have a 5 kcal/mole error range (more than 3 pKa units) when at- tempting to calculate intrinsic pKa values of ionizable groups inside proteins (Russell & Warshel, J. Mol . Biol . , 185:389-404 (1985) ) . Nevertheless, electrostatic interactions are expected to be significant over relatively long distances even with moderate screening, and vary inversely with the linear distance. The electrostatic forces described above are also involved in interactions between uncharged but polar molecules, but the energy of the interaction is more complex than that between simple ions. The energy expression for such interactions also generally varies inversely with the distance between such molecules, raised to a power usually greater than 1, but less than 6 (Creighton, Proteins : Structure and Molecular Properties, Freeman & Co., N.Y. (1984) ) . This is due to the polarizability of dipoles when in the vicinity of electric fields, i.e., Group II metals, M 2+ . It is thus easier to predict results with charged ions. For these reasons, it is preferred to use Group II metals, M 2+ , in this invention and charged side groups of amino acids residues; COO " of Asp and Glu; NH 3+ of Lys and the amino-terminus, and the guanidinium cationic group of Arg. As indicated above, it has surprisingly been found that such subtilase variants having an increased affinity for divalent metal ions are particular suitable for incorporation in the specific detergent compositions described herein. Examples as well as procedures for selecting and producing such subtilases are described in EP 0 353 250 and EP 0 916 732 and comprise the following steps: A. ) Correlating the metal ion binding structural site with some parameter of protein stability - This parameter can be the rate of thermal inactivation derived from kinetic experiments at elevated temperatures and varying concentrations of metal ion. Al- ternatively, one may use thermodynamic measurements of the melting temperature, Tm, derived from calorimetry or some other physical assessment of the unfolding transition. These measurements not only allow an estimate of the degree to which one is successful in affecting stability in a desirable way but also al- low an estimate of the affinity of this site for divalent metal ions. In identifying the metal ion binding site for correlation with a parameter of protein stability one may analyze the three dimensional structure of the protein of interest or some evolutionally related variant. The three-dimensional structure may be obtained from published sources or determined by known methods of X-ray crystallography. Other methods of obtaining structural informa- tion may include circular dichroism, light scattering, measuring the absorption and emission of radiant energy, neutron diffraction, and magnetic resonance. B. ) Altering the metal ion binding site through the substitu- tion, insertion, or deletion of amino acid residue (s) in close proximity to that site so that the electrostatic attractive interaction between the amino acids and the metal ion is increased - These amino acid changes may be introduced into the cloned, se- quenced gene for the protein by the technique of oligonucleotide site-directed in vitro mutagenesis. This method is described in detail in Bryan et al., Proc . Nat'l Acad. Sci. USA 83 :3743-3745 (1986), incorporated herein by reference. The criteria for selection of amino acids in close proximity to the bound metal ion for substitution, insertion, or deletion via site-directed mutagenesis is as follows: Select amino acids for substitution, insertion, or deletion as close as possible to the bound metal ion, but without introducing steric hinderance. Amino acids are selected for substitution, insertion, or deletion that will optimize the distance and geometry of the electrostatic attractive forces at the binding site. (a) In substituting amino acids, preference should be given to changing those amino acids that are not conserved in evolution- ally related homologous proteins. Conserved amino acids in evolutionally related homologous proteins will generally indicate that these conserved amino acids are favorable to the enzyme and should be maintained. In contradistinction, amino acid substitu- tions should be evaluated that differ (variable positions) in the area of the metal ion binding site between the protein to be altered and in evolutionally related homologous proteins. Thus, for example, if the protein to be altered contains a neutral residue in the region of binding and a related protein contains an Asp or Glu (negatively charged) , then high priority should be given to substituting the neutral residue with Asp or Glu. (b) In insertion and/or deletion of amino acid residues, pref- erence should be given to those amino acids that will optimize the distance and geometry of ligand interactions. In general, this involves creating a radius between the amino acid(s) and the metal ion as close as possible to 2.5 A that can be obtained without creating steric hindrance. For example, if a position when changed to Asp or Glu is not at the optimum distance (2.5 A) from the metal ion, then the introduction of an insertion or deletion in this vicinity may allow the Asp or Glu to swing in closer in distance to that found to be optimal. (c) Positively charged residues that are close to the bound metal ion should be changed to neutral or negatively charged residues. Positively charged residues may also simply be deleted. Neutral or negatively charged residues may be inserted. Combinations of insertions, deletions, and substitutions are also con- templated. As the divalent metal ion has a positive charge, changing positively charged residues to neutral or negatively charged residues will increase the affinity of the metal ion binding site. Candidate amino acid substitutions selected by the criteria given above may then be simulated on a high resolution computer graphics system such as the Evans Sutherland Model PS330 interfaced with a computer of suitable configuration such as the VAX 11/780. Such a graphics system allows one to graphically make the pro- posed change and test whether there are any obvious steric problems that the new amino acid residue will introduce, assuming there is no movement of the main chain atoms of the polypeptide fold. The criteria employed in such an analysis are as follows: a) Measure the interatomic distances between most of the atoms of the proposed residue's side chain with those of most of the atoms of its nearest neighbors in the enzyme structure. b) If there are any serious violations of the van der Waals radii of any of the atoms or severe electrostatic repulsion between any of the negative charges, then rotate one or more of the bonds in an attempt to reduce these effects. If either a) or b) gives a structure with no serious van der Waals radii violations or electrostatic repulsions, then introduce the proposed change into the protein via site-directed mutagenesis. If serious van der Waals radii violations or electrostatic repulsions persist, then give the change a low priority for experimental evaluation. Examples of subtilases which may conveniently be modified as described herein include, but are not limited to, those from Bacillus amyloliquefaciens, subtilisin Carlsberg from Bacillus licheniformis , subtilisin DY from Bacillus DY, subtilisin amy- losachariticus from Bacillus amylosachariticus, and mesenterico- peptidase. Fungal proteases, such as protease K, thermomycolase, and thermitase from Thermoactinomyces vulgaris may also be modified, as well as mammalian proteases produced in a bacterial host . In general, the subtilases of interest are those belonging to the subgroups I-Sl and I-S2. Referring to subgroup I-Sl, preferred parent subtilases are selected from the group consisting of ABSS168, BASBPN, BSSDY, BLSCAR and functional variants thereof having retained the characteristic of sub-group I-Sl. Referring to subgroup I-S2, preferred parent subtilases are selected from the group consisting of BLS147, BLS309, BAPB92 (sub- tilisin PB92), TVTHER (thermitase) , BYSYAB (alkaline elastase YaB) and functional variants thereof having retained the characteristic of sub-group I-S2. A particular interesting parent subtilase is BLS309 (SAVINASE® NOVO NORDISK A/S) . The amino acid substitutions, deletions, and insertions may be accomplished by site-directed (i.e., oligonucleotide) mutagenesis. Site-directed mutagenesis is well-known in the art and is described in detail in Bryan et al . , Proc . Nat ' 1 Acad. Sci. USA 8 . 3:3743-3745 (1986), incorporated herein by reference. Further, regional directed in vitro random mutagenesis may also be used to alter the amino acid residue (s) in the loops responsible for metal ion binding in the enzyme of interest. The preferred procedure for in vitro random mutagenesis is described in detail in U.S. patent application Ser. No. 828,545 and PCT appli- cation PCT/US87/00348, both incorporated herein by reference. The variants generated by this procedure can be screened or selected for those variants that exhibit the desired parameter of enhanced protein stability. These screened or selected variants can then be further characterized first through genetic manipulations to identify the change (s) in amino acid residue (s) . In addition, these screened or selected variants can be further identified by kinetic and thermodynamic characterization of stability. Finally, these variant enzymes may be crystallized and X-ray crystal structures obtained at high resolution to fully correlate the in- creased stability with known protein structural information. It is well known in the art that substitution of one amino acid to a similar conservative amino acid is only expected to provide a minor change in the characteristic of the enzyme, and Table I below list the groups of such conservative amino acids. Table I Conservative amino acid substitutions Basic: R = arginine K = lysine H = histidine Acidic: E = glutamic acid D = aspartic acid Polar: Q = glutamine N = asparagine Hydrophobic: L = leucine I = isoleucine V = valine M = methionine Aromatic: F = phenylalanine W = tryptophan Y = tyrosine Small: G = glycine A = alanine S = serine T = threonine Based on the disclosed subtilase variants herein, it is routine work, for a person skilled in the art, to identify further suitable conservative modification (s) of the variants disclosed herein in order to obtain a subtilase variant which are suitable for incorporation in the detergent compositions of the present invention. Any of the above-mentioned modifications may also be combined with one or more modification (s) in any other position (s). In particular, combinations with other modifications known to confer improved properties to the enzyme are preferred. The prior art describes a number of subtilase variants with different improved properties and a number of those are mentioned in the "Background of the invention" section herein ( vide supra) . Thus, examples of such additional modifications include the following positions: 222 (improves oxidation stability) and 218 (improves thermal stability) . Other relevant positions will be apparent from the prior art references and will be known to the person skilled in protease engineering. Based thereon, it contemplated that the above-mentioned subtilase variants may advantageously be combined with one or more modification^) in any of the positions: 27, 36, 57, 76 87, 97, 98, 99, 101 , 103 , 104 , 120 , 123 , 159 , 206 , 218 , 222 , 224 , 232 , 235 , 236 , 245 , 248 , 252 and 274 . In particular, the following BLS309 and BAPB92 variants are con- 5 sidered suitable for combination: K27R, *36D, S57P, N76D, S87N, G97N, S101G, S103A, V104A, V104N, V104Y, V104I, H120D, N123S, G159D, Q206E, N218S, M222S, M222A, T224S, A232V, K235L, Q236H, Q245R, N248D, N252K and T274A. 10 Furthermore, variants comprising any of the variants S101G+V104N, S87N+S101G+V104N, K27R+V104Y+N123S+T274A, N76D+V104A, S101G+S103A+V104I+G159D+A232V+Q236H+Q245R+N248D+N252K or other combinations of these mutations (V104N, S101G, K27R, V104Y, N123S, T274A, V104A) , in combination with any one or more of the 15 modification (s) mentioned above are expected to be suitable for the purposes described herein. Further interesting subtilase variants are preferably combined with one or more modification (s) in any of the positions 129, 20 131, 133 and 194, preferably as 129K, 131H, 133P, 133D and 194P modifications, and most preferably as P129K, P131H, A133P, A133D and A194P modifications. Any of those modification (s) give a higher expression level of a subtilase variant. For further details reference is made to working examples herein ( vide infra) . 25 Producing mutations in subtilase genes: Many methods for cloning a subtilase of the invention and for introducing mutations into genes ( e . g. subtilase genes) are well known in the art . 30 In general standard procedures for cloning of genes and introducing mutations (random and/or site directed) into said genes may be used in order to obtain a subtilase variant suitable for incorporation in the detergent composition of the invention. 35 For further description of suitable techniques reference is made to working examples herein ( vide infra) and (Sambrook et al . (1989) Molecular cloning: A laboratory manual, Cold Spring Harbor lab., Cold Spring Harbor, NY; Ausubel, F. M. et al . (eds.) "Current protocols in Molecular Biology". John Wiley and Sons, 1995; Harwood, C. R. , and Cutting, S. M. (eds.) "Molecular Biological Methods for Bacillus". John Wiley and Sons, 1990); and WO 96/34946. Expression vectors: A recombinant expression vector comprising a DNA construct encoding the enzyme 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 in part or in its entirety 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 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 bacterial host cells include the promoter of the Bacillus stearothermophilus maltogenic amylase gene, the Bacillus licheniformis alpha-amylase gene, the Bacillus amyloliquefaciens alpha-amylase gene, the Bacillus subtilis alkaline protease gen, or the Bacillus pumilus xylosidase gene, or the phage Lambda P R or P L promoters or the E. coli lac, trp or tac promoters. The DNA sequence encoding the enzyme may also, if necessary, be operably connected to a suitable terminator. The recombinant vector 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, or a gene encoding resistance to e.g. antibiotics like kanamycin, chloramphenicol , erythromycin, tetracycline, spectinomycine, or the like, or resistance to heavy metals or herbicides. To direct an enzyme 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. 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, or to assemble these sequences by suitable PCR amplification schemes, and to insert them into suitable vectors containing the information necessary for replication or integration, are well known to persons skilled in the art (cf., for instance, Sambrook et al . , o . cit . ) . Host cell : 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 DNA 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 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 are gram-positive bacteria such as strains of Bacillus, such as strains of B . subtilis, B. licheniformis, B. lentus, B. brevis, B. stearothermophilus , B. alkalophilus, B. amyloliquefaciens, B . coagulans, B. circulans, B . lautus , B. megatherium or B . thuringiensis , ox strains of Strepto-nyces, such as S. lividans or S. murinus, or gram-negative bacteria such as Echerichia coli . The transformation of the bacteria may be effected by protoplast transformation, electroporation, conjugation, 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. When expressing the enzyme in gram-positive bacteria such as Bacillus or Streptomyces strains, the enzyme may be retained in the cytoplasm, or may be directed to the extracellular medium by a bacterial secretion sequence. In the latter case, the enzyme may be recovered from the medium as described below. Method of producing subtilase: When an expression vector comprising a DNA sequence encoding the enzyme is transformed into a heterologous host cell it is possible to enable heterologous recombinant production of the enzyme. Thereby it is possible to make a highly purified subtilase composition, characterized in being free from homologous impurities. The medium used to culture the transformed host cells may be any conventional medium suitable for growing the host cells in question. The expressed subtilase may conveniently be secreted into the culture medium and may be recovered therefrom by well- known procedures including separating the cells from the medium by centrifugation or filtration, precipitating proteinaceous components of the medium by means of a salt such as ammonium sulphate, followed by chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like. Detergent compositions according to the invention: The detergent compositions according to the invention (i.e. detergent compositions comprising the subtilases described herein as well as an alkylpolysaccharide) will be described in further details below. When used herein the term "detergent composition" is intended to cover cleaning compositions which may have been formulated as hand or machine laundry detergents compositions, including laundry additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics. The term "detergent composition" is also intended to cover rinse added fabric softener compositions as well as compositions for use in general household hard surface cleaning operations and dishwashing operations. Such detergent compositions may be in the form of powder, liquid, paste, gel, bars or granules. Surfactant system: The surfactant is typically present at a level from 0.1% to 60% by weight. The surfactant is preferably formulated to be compatible with subtilase components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated in such a way that it promotes, or at least does not degrade, the stability of any subtilase in these compositions. Preferred systems to be used according to the present invention comprise, in addition to the alkylpolysaccharide, the polyhydroxy fatty acid amide or the α-sulfonated fatty acid esters, one or more of the nonionic and/or anionic surfactants described herein. Nonionic surfactants (including alkylpolysaccharides and polyhy- droxyfatty acid amides) : As indicated above, the compositions of the present invention are characterised in that they contain one or more alkylpolysaccharides, polyhydroxy fatty acid amides or α-sulfonated fatty acid esters. In general, the laundry detergent compositions of the present invention typically comprise from about 0.5% to about 20%, preferably from about 1% to about 15%, e.g. from about 2% to about 10% by weight of nonionic surfactants. Thus, suitable alkylpolysaccharides to be incorporated in the detergent composition of the invention comprise the alkylpolysaccharides disclosed in US 4,565,647, comprising a hydrophobic moi- ety having from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms, and a hydrophilic moiety derived from a polysaccharide, e.g. a polyglycoside, containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units. Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties (optionally the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside) . The intersaccharide bonds can be, e.g., between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units. In a preferred embodiment of the invention the alkylpolysaccharide has the general formula I R 3 0(C n H 2n O) t (glycosyl) x wherein R 3 is selected from the group consisting of alkyl, alkyl- phenyl, hydroxyalkyl , hydroxyalkylphenyl and mixtures thereof in which the alkyl group contains from about 10 to about 18 carbon atoms, preferably from about 10 to about 16 carbon atoms, more preferably from about 12 to about 14 carbon atoms; n is 2 or 3, preferably 2; t is from 0 to 10, preferably 0; and x is from about 1.3 to 10, preferably from about 1.3 to about 3, more preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1-position) . The additional glycosyl units can then be attached between their 1-position and the preceding glycosyl units 2-, 3-, 4-, and/or 6-position, preferably predominantly the 2 -position. The alkylpolysaccharide may constitute from as little as 1% by weight of the total amount of nonionic surfactants present in the composition of the invention to as much as more than 99% by weight of the total amount of nonionic surfactants present in the composition of the invention. Examples of the amount of alkylpolysaccharide in the compositions of the invention (expressed as a percentage of the total amount of nonionic surfactants present in the composition) are, for example at least 1% by weight, at least 2% by weight, at least 3% by weight, at least 4% by weight, at least 5% by weight, at least 10% by weight, at least 15% by weight, at least 20% by weight, at least 25% by weight, at least 30% by weight, at least 35 %by weight, at least 40% by weight, at least 45% by weight, at least 50% by weight, at least 55% by weight, at least 60% by weight, at least 65% by weight, at least 70% by weight, at least 75% by weight, at least 80% by weight, at least 85% by weight, at least 90% by weight, at least 95% by weight, or even as high as at least 99% by weight, calculated on the total amount of nonionic surfactants present in the detergent composition. In an interesting embodiment of the invention the alkylpolysaccharide is the sole nonionic surfactant present in the composition of the invention. As will be understood by the skilled person, the composition of the invention should at least comprise an effective amount of at least one of the above-mentioned alkylpolysaccharides, i.e. an amount, which is sufficient for obtaining the improved washing efficiency defined herein. The polyhydroxy fatty acid amides which are useful for the pur- poses described herein are have the general formula (I) : R 2 -C(=0)-N(R 1 ) (Z) (I) wherein R 1 is selected from the group consisting of hydrogen, C x - C 4 -hydrocarbyl , 2-hydroxyethyl, and 2-hydroxypropyl; R 2 is C 5 -C 31 hydrocarbyl, such as alkyl or alkenyl (e.g. coconut alkyl or mixtures thereof) ; and Z is selected from the group consisting of glucose, fructose, maltose, lactose, galactose, mannose and xylose, preferably glucose. In an interesting embodiment of the invention R 1 and R 2 are saturated. Preferably, R 1 is selected from the group consisting of methyl, ethyl, n-propyl and n-butyl, in particular methyl. Furthermore, it preferred that R 1 is C 10 -C 31 -alkyl or a mixture thereof. More preferably, R 1 is C 12 -C 18 -alkyl or a mixture thereof, in particular C 12 -C 14 -alkyl or a mixture thereof, or C 16 -C 18 -alkyl or a mixture thereof . Thus, specific examples of preferred glucoamides include C 12 -C 14 - alkyl N-methyl glucamide and C 16 -C 18 -alkyl N-methyl glucamide. The polyhydroxy fatty acid amide may constitute from as little as 1% by weight of the total amount of nonionic surfactants present in the composition of the invention to as much as more than 99% by weight of the total amount of nonionic surfactants present in the composition of the invention. Examples of the amount of polyhydroxy fatty acid amide in the compositions of the invention (expressed as a percentage of the total amount of nonionic surfactants present in the composition) are, for example at least 1% by weight, at least 2% by weight, at least 3% by weight, at least 4% by weight, at least 5% by weight, at least 10% by weight, at least 15% by weight, at least 20% by weight, at least 25% by weight, at least 30% by weight, at least 35 %by weight, at least 40% by weight, at least 45% by weight, at least 50% by weight, at least 55% by weight, at least 60% by weight, at least 65% by weight, at least 70% by weight, at least 75% by weight, at least 80% by weight, at least 85% by weight, at least 90% by weight, at least 95% by weight, or even as high as at least 99% by weight, calculated on the total amount of nonionic surfactants present in the detergent composition. In an interesting embodiment of the invention the polyhydroxy fatty acid amide is the sole nonionic surfactant present in the composition of the invention. As will be understood by the skilled person, the composition of the invention should at least comprise an effective amount of at least one of the above-mentioned polyhydroxy fatty acid amides, i.e. an amount which is sufficient for obtaining the improved washing efficiency defined herein. As explained above, the compositions of the invention may, in ad- dition to the alkylpolysaccharide or the polyhydroxy fatty acid amide, contain other nonionic surfactants. Examples of such additional nonionic surfactants are given below. Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are suitable for use as additional nonionic surfactant, with the polyethylene oxide condensates being preferred. These compounds include the condensation products of alkyl phe- nols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, in either a straight chain or branched-chain configuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to from about 2 to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkyl phenol. Commercially available nonionic surfactants of this type include Igepal™ CO-630, marketed by the GAF Corporation; and Triton™ X-45, X-114, X-100 and X-102, all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkyl phenol eth- oxylates) . The condensation products of primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suit- able for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol are pre- sent in said condensation products. Examples of commercially available nonionic surfactants of this type include Tergitol™ 15- S-9 (The condensation product of C 1:L -C 15 linear alcohol with 9 moles ethylene oxide) , Tergitol™ 24-L-6 NMW (the condensation product of C 12 -C 14 primary alcohol with 6 moles ethylene oxide with a narrow molecular weight distribution) , both marketed by Union Carbide Corporation; Neodol™ 45-9 (the condensation product of C 14 -C 15 linear alcohol with 9 moles of ethylene oxide) , Neodol™ 23-3 (the condensation product of C 12 -C 13 linear alcohol with 3.0 moles of ethylene oxide) , Neodol™ 45-7 (the condensation product of C 14 -C 15 linear alcohol with 7 moles of ethylene oxide) , Neodol™ 45-5 (the condensation product of C 14 -C 15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company, Ky- ro™ EOB (the condensation product of C 13 -C 15 alcohol with 9 moles ethylene oxide) , marketed by The Procter & Gamble Company, and Genapol LA 050 (the condensation product of C 12 -C 14 alcohol with 5 moles of ethylene oxide) marketed by Hoechst . Preferred range of HLB in these products is from 8-11 and most preferred from 8-10. The condensation products of ethylene oxide with a hydrophobic base formed by the condensation of propylene oxide with propylene glycol are also suitable for use as the additional nonionic surfactant systems of the present invention. The hydrophobic portion of these compounds will preferably have a molecular weight from about 1500 to about 1800 and will exhibit water insolubility. The addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain of the commercially available Pluronic™ surfactants, marketed by BASF. Also suitable for use as additional nonionic surfactant are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine . The hydrophobic moiety of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and gener- ally has a molecular weight of from about 2500 to about 3000. This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000. Examples of this type of nonionic surfactant include certain of the commercially available Tetronic™ compounds, marketed by BASF. Preferred for use as the additional nonionic surfactant are polyethylene oxide condensates of alkyl phenols, condensation prod- ucts of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethyleneoxide, alkylpolysaccharides, and mixtures hereof. Most preferred are C 8 -C 14 alkyl phenol etho- xylates having from 3 to 15 ethoxy groups and C 8 -C 18 alcohol etho- xylates (preferably C 10 avg.) having from 2 to 10 ethoxy groups, and mixtures thereof . Anionic surfactants (including α-sulfonated fatty acid esters) : Typically, the compositions of the present invention contain from 0.1% to about 60%, such as from about 1% to about 50%, e.g. from about 10% to about 50%, preferably from about 15% to about 50%, more preferably from about 20% to 40%, and most preferably from 20% to about 30%, by weight of a natural or synthetic anionic surfactant. As will be understood from the below discussion at least some of the anionic surfactant must be constituted by an α- sulfonated fatty acid ester. As indicated above, the compositions of the present invention are characterised in that they contain one or more α-sulfonated fatty acid esters. In general, such α-sulfonated fatty acid esters distinguish themselves form other (and even similar) anionic surfactants in that they exhibit less sensitivity to water hardness, i.e. the performance of such α-sulfonated fatty acid esters in, e.g., detergent compositions will be less sensitive to the Ca 2+ concentration in the wash liquor than will other commonly employed anionic surfactants, such as, for example, LAS and AS. α-sulfonated fatty acid esters which are useful for the purposes described herein are α-sulfonated fatty acid ester having the general formula I R x -CH(S0 3 M) -C(=0) -OR y (I) wherein R x is a C 8 -C 20 hydrocarbyl group , R y is a C. -Cg hydrocarbyl group , and M is a cation which forms a water-soluble salt with the α-sulfonated fatty acid ester . Preferably, the R x is a saturated C 8 -C 20 hydrocarbyl group , i . e . a C 8 -C 20 alkyl group, in particular a C 10 -C 16 alkyl group . Moreover, it is preferred that the R x group is linear and typical examples of linear C 10 -C 16 alkyl group are, e.g., decanyl , unde- canyl, dodecanyl, tridecanyl, tetradecanyl , pentadecanyl, hexa- decanyl , and mixtures thereof . It should be understood that the employed α-sulfonated fatty acid ester described herein may also (which may very well be the case during to the manufacturing procedure of such α-sulfonated fatty acid esters) be a mixture of α-sulfonated fatty acid esters. In such cases it is preferred that the molecular weight distribution is such that the main R x chain length range is between 10 and 16 carbon atoms, in particular between 12 and 16 carbon atoms, such as 13, 14, or 15 carbon atoms. R y is preferably a C--C 6 alkyl group, such as methyl, ethyl, n- propyl , isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, cy- clobutyl, n-pentyl, isopentyl, neopentyl , cyclopentyl, n-hexyl, and cyclohexyl, preferably methyl, ethyl, n-propyl and isopropyl. In a particular preferred embodiment of the present invention, R y is methyl, i.e. an α-sulfonated fatty acid methyl ester. Thus, examples of specific α-sulfonated fatty acid esters which are considered particular useful for the purposes described herein include α-sulfonated lauric acid methyl ester, α- sulfonated tridecylic acid mehtyl ester, α-sulfonated myristic acid methyl ester, α-sulfonated pentadecylic acid methyl ester, α-sulfonated palmitic acid methyl ester, and mixtures thereof. The cationic counterion, M, described above in connection with formula I, may be any cation capable of forming a water-soluble salt with the α-sulfonated fatty acid ester in question. A vaste number of suitable cations are available and the person skilled in detergent formulation will be able to select suitable cations for the purpose. However, typical examples of suitable cations include cations selected from the group consisting of metal ions, such as sodium, potassium and lithium, and substituted and unsub- stituted ammonium cations, such as monoethanolamine, dietha- noleamine and triethanolamine. A particular preferred cation is the sodium ion. The α-sulfonated fatty acid esters may constitute from as little as 1% by weight of the total amount of anionic surfactants present in the composition of the invention to as much as more than 99% by weight of the total amount of anionic surfactants present in the composition of the invention. Examples of the amount of α-sulfonated fatty acid esters in the compositions of the invention (expressed as a percentage of the total amount of anionic surfactants present in the composition) are, for example at least 1% by weight, at least 2% by weight, at least 3% by weight, at least 4% by weight, at least 5% by weight, at least 10% by weight, at least 15% by weight, at least 20% by weight, at least 25% by weight, at least 30% by weight, at least 35 %by weight, at least 40% by weight, at least 45% by weight, at least 50% by weight, at least 55% by weight, at least 60% by weight, at least 65% by weight, at least 70% by weight, at least 75% by weight, at least 80% by weight, at least 85% by weight, at least 90% by weight, at least 95% by weight, or even as high as at least 99% by weight, calculated on the total amount of anionic surfactants present in the detergent composition. In an interesting embodiment of the invention the α-sulfonated fatty acid ester is the sole anionic surfactant present in the composition of the invention. As will be understood by the skilled person, the composition of the invention should at least comprise an effective amount of at least one of the above-mentioned α-sulfonated fatty acid esters, i.e. an amount which is sufficient for obtaining the improved washing efficiency defined herein. Such α-sulfonated fatty acid ester may be prepared by methods which will be well-known to the person skilled in the art. Thus, the α-sulfonated fatty acid ester of the above formula I may, for example, be prepared as described in "The Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329 (sulfonation by means of gaseous S0 3 ) . Examples of suitable starting materials include, for example, natural fatty substances as derived from tallow, palm oil, etc. As explained above, the compositions of the invention may, in ad- dition to the α-sulfonated fatty acid ester, contain other anionic surfactants. Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants. Examples hereof are water soluble salts or acids of the formula RO (A) m S0 3 M wherein R is an unsubstituted C 10 - C 24 alkyl or hydroxyalkyl group having a C 10 -C 24 alkyl component, preferably a C 12 -C 20 alkyl or hydroxyalkyl, more preferably C 12 -C 18 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, and M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or sub- stituted-ammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific ex- amples of substituted ammonium cations include methyl-, dimethyl- , trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and those derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary surfac- tants are C 12 -C 18 alkyl polyethoxylate (1.0) sulfate (C 12 - C 18 E(1.0)M), C 12 -C 18 alkyl polyethoxylate (2.25) sulfate (C 12 - C 18 (2.25)M, and C 12 -C 18 alkyl polyethoxylate (3.0) sulfate (C 12 - C 18 E(3.0)M), and C 12 -C 18 alkyl polyethoxylate (4.0) sulfate (C 12 - C 18 E (4.0) M) , wherein M is conveniently selected from sodium and potassium. Other suitable anionic surfactants include the alkyl sulfate surfactants which are water soluble salts or acids of the formula ROS0 3 M wherein R preferably is a C 10 -C 24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C 10 -C 20 alkyl component, more preferably a C 12 -C 18 alkyl or hydroxyalkyl, and M is H or a cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl ammonium cations and quaternary ammonium cations such as tetramethyl -ammonium and dimethyl piperdinium cations and quaternary ammonium cations derived from alkylamines such as ethyl - amine, diethylamine, triethylamine, and mixtures thereof, and the like) . Typically, alkyl chains of C 12 -C 16 are preferred for lower wash temperatures (e.g. below about 50°C) and C 16 -C 18 alkyl chains are preferred for higher wash temperatures (e.g. above about 50°C) . Other anionic surfactants useful for detersive purposes can also be included in the laundry detergent compositions of the present invention. Theses can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono- di- and triethanolamine salts) of soap, C 8 -C 22 primary or secondary alkanesulfonates, C 8 -C 24 olefinsulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No. 1,082,179, C 8 -C 24 alkylpo- lyglycolethersulfates (containing up to 10 moles of ethylene oxide) ; alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates, alkyl succina- mates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C 12 -C 18 monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated C 6 -C 12 diesters) , acyl sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsul- fated compounds being described below) , branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as those of the formula RO (CH 2 CH 2 0) k -CH 2 C00-M+ wherein R is a C 8 -C 22 alkyl, k is an integer from 1 to 10, and M is a soluble salt forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil. Alkylbenzene sulfonates are highly preferred. Especially preferred are linear (straight-chain) alkyl benzene sulfonates (LAS) wherein the alkyl group preferably contains from 10 to 18 carbon atoms . Further examples are described in "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perrry and Berch) . A variety of such surfactants are also generally disclosed in US 3,929,678, (Column 23, line 58 through Column 29, line 23, herein incorporated by reference) . Other surfactants: The laundry detergent compositions of the present invention may also contain cationic, ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein. Cationic detersive surfactants suitable for use in the laundry detergent compositions of the present invention are those having one long-chain hydrocarbyl group. Examples of such cationic surfactants include the ammonium surfactants such as alkyltrimethyl- ammonium halogenides, and those surfactants having the formula: [R 2 (OR 3 ) y ] [R 4 (OR 3 ) y ] 2 R 5 N+X- wherein R 2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R 3 is selected form the group consisting of -CH 2 CH 2 -, -CH 2 CH (CH 3 ) - , -CH 2 CH (CH 2 OH) - , -CH 2 CH 2 CH 2 -, and mixtures thereof; each R 4 is selected from the group consisting of C 1 -C 4 alkyl, C.-C 4 hydroxyalkyl, benzyl ring structures formed by joining the two R 4 groups, CH 2 CHOHCHOHCOR 6 CHOHCH 2 OH, wherein R 6 is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when y is not 0; R 5 is the same as R 4 or is an alkyl chain, wherein the total number of carbon atoms or R 2 plus R 5 is not more than about 18; each y is from 0 to about 10, and the sum of the y values is from 0 to about 15; and X is any compatible anion. Highly preferred cationic surfactants are the water soluble quaternary ammonium compounds useful in the present composition having the formula: R.R^R^X " (i) wherein R ± is C 8 -C 16 alkyl, each of R 2 , R 3 and R 4 is independently C.-C 4 alkyl, C x -C 4 hydroxy alkyl, benzyl, and -(C 2 H 40 ) X H where x has a value from 2 to 5, and X is an anion. Not more than one of R 2 , R 3 or R 4 should be benzyl. The preferred alkyl chain length for R. is C 12 -C 15 , particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or 0X0 alcohols synthesis. Preferred groups for R 2 , R 3 and R 4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosul- phate, acetate and phosphate ions. Examples of suitable quaternary ammonium compounds of formulae (i) for use herein are: coconut trimethyl ammonium chloride or bromide; coconut methyl dihydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; ci 2 -i 5 dimethyl hydroxyethyl ammonium chloride or bromide; coconut dimethyl hydroxyethyl ammonium chloride or bromide; myristyl trimethyl ammonium methyl sulphate; lauryl dimethyl benzyl ammonium chloride or bromide; lauryl dimethyl (ethenoxy) 4 ammonium chloride or bromide; choline esters (compounds of formula (i) wherein R. is CH 2 -CH 2 -0-C-C 12 _ 14 alkyl and R 2 , R 3 and R 4 are methyl) 0 di-alkyl imidazolines [compounds of formula (i) ] . Other cationic surfactants useful herein are also described in US 4,228,044 and in EP 000 224. When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 25%, preferably from about 1% to about 8% by weight of such cationic surfactants . Ampholytic surfactants are also suitable for use in the laundry detergent compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight- or branched-chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic wa- ter-solubilizing group, e.g. carboxy, sulfonate, sulfate. See US 3,929,678 (column 19, lines 18-35) for examples of ampholytic surfactants . When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such ampholytic surfactants. Zwitterionic surfactants are also suitable for use in laundry detergent compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See US 3,929,678 (column 19, line 38 through column 22, line 48) for examples of zwitterionic surfactants. When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such zwitterionic surfactants. Semi-polar nonionic surfactants are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; watersoluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms . Semi -polar nonionic detergent surfactants include the amine oxide surfactants having the formula: O t R 3 (OR 4 ) x N(R 5 ) 2 wherein R 3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereof containing from about 8 to about 22 carbon at- oms; R 4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is from 0 to about 3 : and each R 5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R 5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure. These amine oxide surfactants in particular include C 10 -C 18 alkyl dimethyl amine oxides and C 8 -C 12 alkoxy ethyl dihydroxy ethyl amine oxides. When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such semi- polar nonionic surfactants. Builder system: The compositions according to the present invention may further comprise a builder system. Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates and fatty acids, materials such as ethylenediamine tetraacetate, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethyle- ne phosphonic acid and diethylene triamine pentamethylene phos- phonic acid. Although less preferred for obvious environmental reasons, phosphate builders can also be used herein. Suitable builders can be an inorganic ion exchange material, com- monly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP. Another suitable inorganic builder material is layered silicate, e.g. SKS-6 (Hoechst) . SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na 2 Si 2 0 5 ) . Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as dis- closed in Belgian Patent Nos. 831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups include the water- soluble salts of succinic acid, malonic acid, (ethylenedioxy) di- acetic acid, maleic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxy- lates described in German Offenlegungsschrift 2,446,686, and 2,446,487, US 3,935,257 and the sulfinyl carboxylates described in Belgian Patent No. 840,623. Polycarboxylates containing three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconates as well as succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1,379,241, lactoxysuccinates described in Netherlands Application 7205873, and the oxypolycarboxylate materials such as 2-oxa-l, 1, 3 -propane tricarboxylates described in British Patent No. 1,387,447. Polycarboxylates containing four carboxy groups include oxydisuc- cinates disclosed in British Patent No. 1,261,829, 1,1,2,2,- ethane tetracarboxylates, 1, 1, 3 , 3 -propane tetracarboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in British Patent Nos. 1,398,421 and 1,398,422 and in US 3,936,448, and the sulfonated pyrolysed citrates described in British Patent No. 1,082,179, while polycarboxylates containing phosphone substituents are disclosed in British Patent No. 1,439,000. Alicyclic and heterocyclic polycarboxylates include cyclopentane- cis, cis-cis-tetracarboxylates, cyclopentadienide pentacarboxy- lates, 2 , 3 , 4 , 5-tetrahydro-furan - cis, cis, cis-tetracarboxy- lates, 2 , 5-tetrahydro-furan-cis, discarboxylates, 2,2,5,5,- tetrahydrofuran - tetracarboxylates, 1, 2 , 3 , 4 , 5, 6-hexane - hex- acarboxylates and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No. 1,425,343. Of the above, the preferred polycarboxylates are hydroxy- carboxylates containing up to three carboxy groups per molecule, more particularly citrates. Preferred builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6) , and a water- soluble carboxylate chelating agent such as citric acid. A suitable chelant for inclusion in the detergent composi-ions in accordance with the invention is ethylenediamine-N,N' -disuccinic acid (EDDS) or the alkali metal, alkaline earth metal, ammonium, or substituted ammonium salts thereof, or mixtures thereof. Preferred EDDS compounds are the free acid form and the sodium or magnesium salt thereof. Examples of such preferred sodium salts of EDDS include Na 2 EDDS and Na 4 EDDS . Examples of such preferred magnesium salts of EDDS include MgEDDS and Mg 2 EDDS . The magnesium salts are the most preferred for inclusion in compositions in accordance with the invention. Preferred builder systems include a mixture of a water-insoluble aluminosilicate builder such as zeolite A, and a water soluble carboxylate chelating agent such as citric acid. Other builder materials that can form part of the builder system for use in granular compositions include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as the organic phosphonates, amino polyalkylene phosphonates and amino polycarboxylates . Other suitable water-soluble organic salts are the homo- or co- polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated form each other by not more than two carbon atoms . Polymers of this type are disclosed in GB-A-1, 596, 756. Examples of such salts are polyacrylates of MW 2000-5000 and their copoly- mers with maleic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000. Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition. Preferred levels of builder for liquid detergents are from 5% to 30%. Enzymes : Preferred detergent compositions, in addition to the variants discussed above, comprise other enzyme (s) which provides cleaning performance and/or fabric care benefits. Such enzymes include other proteases, lipases, cutinases, amy- lases, cellulases, peroxidases, oxidases (e.g. laccases) . Other proteases : Any protease suitable for use in alkaline solutions can be used. Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically or genetically modified mutants are included. The protease may be a serine protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those derived from Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279) . Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270. Preferred commercially available protease enzymes include those sold under the trade names Alcalase, Savinase, Primase, Durazym, and Esperase by Novo Nordisk A/S (Denmark) , those sold under the tradename Maxatase, Maxacal, Maxapem, Properase, Purafect and Purafect OXP by Genencor International, and those sold under the tradename Opticlean and Optimase by Solvay Enzymes. Protease enzymes may be incorporated into the compositions in accordance with the invention at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition. Lipases : Any lipase suitable for use in alkaline solutions can be used. Suitable lipases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Examples of useful lipases include a Humicola lanuginosa lipase, e.g., as described in EP 258 068 and EP 305 216, a Rhizomucor miehei lipase, e.g., as described in EP 238 023, a Candida lipase, such as a C. antarctica lipase, e.g., the C. antarctica li- pase A or B described in EP 214 761, a Pseudomonas lipase such as a P. alcaligenes and P. pseudoalcaligenes lipase, e.g., as described in EP 218 272, a P. cepacia lipase, e.g., as described in EP 331 376, a P. stutzeri lipase, e.g., as disclosed in GB 1,372,034, a P. fluorescens lipase, a Bacillus lipase, e.g., a B_;_ subtilis lipase (Dartois et al . , (1993), Biochemica et Biophysica acta 1131, 253-260) , a B. stearothermophilus lipase (JP 64/744992) and a B. pumilus lipase (WO 91/16422) . Furthermore, a number of cloned lipases may be useful, including the Penicillium camembertii lipase described by Yamaguchi et al . , (1991), Gene 103, 61-67), the Geotricum candidum lipase (Schi- mada, Y. et al . , (1989), J. Biochem., 106, 383-388), and various Rhizopus lipases such as a R. delemar lipase (Hass, M.J et al . , (1991), Gene 109, 117-113), a R. niveus lipase (Kugimiya et al . , (1992), Biosci. Biotech. Biochem. 56, 716-719) and a R. oryzae lipase . Other types of lipolytic enzymes such as cutinases may also be useful, e.g., a cutinase derived from Pseudomonas mendocina as described in WO 88/09367, or a cutinase derived from Fusarium so- lani pisi (e.g. described in WO 90/09446) . Especially suitable lipases are lipases such as Ml Lipase™, Luma fast™ and Lipomax™ (Genencor) , Lipolase™ and Lipolase Ultra™ (Novo Nordisk A/S) , and Lipase P "Amano" (Amano Pharmaceutical Co. Ltd.) . The lipases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition. Amylases : Any amylase (α and/or β) suitable for use in alkaline solutions can be used. Suitable amylases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Amylases include, for example, α-amylases obtained from a special strain of B. licheniformis, described in more detail in GB 1,296,839. Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™ and BAN™ (available from Novo Nordisk A/S) and Rapidase™ and Maxamyl P™ (available from Genencor) . The amylases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more pref- erably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition. Cellulases : Any cellulase suitable for use in alkaline solutions can be used. Suitable cellulases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. Suitable cellulases are disclosed in US 4,435,307, which discloses fungal cellulases produced from Humicola insolens. Es- pecially suitable cellulases are the cellulases having colour care benefits. Examples of such cellulases are cellulases described in European patent application No. 0 495 257. Commercially available cellulases include Celluzyme™ produced by a strain of Humicola insolens, (Novo Nordisk A/S) , and KAC- 500(B)™ (Kao Corporation). Cellulases are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition. Peroxidases/Oxidases : Peroxidase enzymes are used in combination with hydrogen peroxide or a source thereof (e.g. a percarbonate, perborate or persulfate) . Oxidase enzymes are used in combination with oxygen. Both types of enzymes are used for "solution bleach- ing", i.e. to prevent transfer of a textile dye from a dyed fabric to another fabric when said fabrics are washed together in a wash liquor, preferably together with an enhancing agent as described in e.g. WO 94/12621 and WO 95/01426. Suitable per- oxidases/oxidases include those of plant, bacterial or fungal origin. Chemically or genetically modified mutants are included. Peroxidase and/or oxidase enzymes are normally incorporated in the detergent composition at a level of from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level of from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level of from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level of from 0.01% to 0.2% of enzyme protein by weight of the composition. Mixtures of the above mentioned enzymes are encompassed herein, in particular a mixture of a protease, an amylase, a lipase and/or a cellulase. In general, the amount of total enzyme, i.e. the amount of the subtilase variants discussed previously and any other (additional) enzyme, incorporated in the detergent composition, is normally at a level from 0.00001% to 2% of enzyme protein by weight of the composition, preferably at a level from 0.0001% to 1% of enzyme protein by weight of the composition, more preferably at a level from 0.001% to 0.5% of enzyme protein by weight of the composition, even more preferably at a level from 0.01% to 0.2% of enzyme protein by weight of the composition. Bleaching agents: Additional optional detergent ingredients that can be included in the detergent compositions of the present invention include bleaching agents such as PB1, PB4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components can include one or more oxygen bleaching agents and, depending upon the bleaching agent chosen, one or more bleach activators. When present oxygen bleaching compounds will typically be present at levels of from about 1% to about 25%. In general, bleaching compounds are optional added components in non-liquid formulations, e.g. granular detergents. The bleaching agent component for use herein can be any of the bleaching agents useful for detergent compositions including oxygen bleaches as well as others known in the art. The bleaching agent suitable for the present invention can be an activated or non-activated bleaching agent. One category of oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include magnesium mo- noperoxyphthalate hexahydrate, the magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diper- oxydodecanedioic acid. Such bleaching agents are disclosed in US 4,483,781, US 740,446, EP 0 133 354 and US 4,412,934. Highly pre- ferred bleaching agents also include 6-nonylamino-6- oxoperoxycaproic acid as described in US 4,634,551. Another category of bleaching agents that can be used encompasses the halogen bleaching agents. Examples of hypohalite bleaching agents, for example, include trichloro isocyanuric acid and the sodium and potassium dichloroisocyanurates and N-chloro and N- bromo alkane sulphonamides . Such materials are normally added at 0.5-10% by weight of the finished product, preferably 1-5% by weight . The hydrogen peroxide releasing agents can be used in combination with bleach activators such as tetra-acetylethylenediamine (TAED) , nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934), 3 , 5-trimethyl -hexsanoloxybenzenesulfonate (ISONOBS, described in EP 120 591) or pentaacetylglucose (PAG) , which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. In addition, very suitable are the bleach activators C8 (6-octanamido-caproyl) oxybenzene- sulfonate, C9 (6-nonanamido caproyl) oxybenzenesulfonate and CIO (6-decanamido caproyl) oxybenzenesulfonate or mixtures thereof. Also suitable activators are acylated citrate esters such as disclosed in European Patent Application No. 91870207.7. Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in cleaning compositions according to the invention are described in application USSN 08/136,626. The hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generation of hydrogen peroxide at the beginning or during the washing and/or rinsing process. Such enzymatic systems are disclosed in European Patent Application EP 0 537 381. Bleaching agents other than oxygen bleaching agents are also known in the art and can be utilized herein. One type of non- oxygen bleaching agent of particular interest includes photoacti- vated bleaching agents such as the sulfonated zinc and/or aluminium phthalocyanines . These materials can be deposited upon the substrate during the washing process. Upon irradiation with light, in the presence of oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is ac- tivated and, consequently, the substrate is bleached. Preferred zinc phthalocyanine and a photoactivated bleaching process are described in US 4,033,718. Typically, detergent composition will contain about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine. Bleaching agents may also comprise 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. Suds suppressors : Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-silicone mixtures. Silicones can generally be represented by alkylated polysiloxane materials, while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. Theses materials can be incorporated as particulates, in which the suds suppressor is advantageously releasably incorporated in a water-soluble or waterdispersible, substantially non surface- active detergent impermeable carrier. Alternatively the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or more of the other components. A preferred silicone suds controlling agent is disclosed in US 3,933,672. Other particularly useful suds suppressors are the self-emulsifying silicone suds suppressors, described in German Patent Application DTOS 2,646,126. An example of such a compound is DC-544, commercially available form Dow Corning, which is a siloxane-glycol copolymer. Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alkanols . Suitable 2-alkyl-alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R. Such suds suppressor system are described in European Patent Application EP 0 593 841. Especially preferred silicone suds controlling agents are described in European Patent Application No. 92201649.8. Said compositions can comprise a silicone/ silica mixture in combination with fumed nonporous silica such as Aerosil R . The suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight. Other components : Other components used in detergent compositions may be employed such as soil-suspending agents, soil-releasing agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, color- ing agents, and/or encapsulated or nonencapsulated perfumes. Especially suitable encapsulating materials are water soluble capsules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,616. Other suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester dextrins are, preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said encapsulation materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modi- fied by adding monofunctional substituted groups such as octenyl succinic acid anhydride. Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxy- methylcellulose and hydroxyethylcellulose, and homo- or co- polymeric polycarboxylic acids or their salts. Polymers of this type include the polyacrylates and maleic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copoly- mers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, more preferably form 0.75% to 8%, most preferably from 1% to 6% by weight of the composition. Preferred optical brighteners are anionic in character, examples of which are disodium 4 , 4 ' -bis- (2-diethanolamino-4-anilino -s- triazin-6-ylamino) stilbene-2 :2 ' disulphonate, disodium 4, - 4'- bis- (2 -morpholino-4 -anilino-s-triazin-6 -ylamino-stilbene-2 : 2 ' disulphonate, disodium 4,4' - bis- (2 , 4-dianilino-s-triazin-6- ylamino) stilbene-2 :2 ' - disulphonate, monosodium 4',4'' - bis- (2 , 4-dianilino-s-tri-azin-6-ylamino) stilbene-2 -sulphonate, disodium 4,4' -bis- (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s- triazin-6-ylamino) stilbene-2 , 2 ' - disulphonate, di-sodium 4,4' - bis- (4-phenyl-2, 1, 3-triazol-2-yl) -stilbene-2 ,2 ' disulphonate, disodium 4,4 'bis (2-anilino-4- (l-methyl-2-hydroxyethylamino) -s- triazin-6-ylami-no) stilbene-2 , 2 'disulphonate, sodium 2 (stilbyl- 4 ' ' - (naphtho-1 ' ,2 ' :4, 5) -1,2,3, - triazole-2 '' -sulphonate and 4,4' -bis (2-sulphostyryl) biphenyl . Other useful polymeric materials are the polyethylene glycols, particularly those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight. These polymers and the previously mentioned homo- or co-polymeric poly-carboxylate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizable soils in the pres- ence of transition metal impurities. Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in vari- ous arrangements. Examples of such polymers are disclosed in US 4,116,885 and 4,711,730 and EP 0 272 033. A particular preferred polymer in accordance with EP 0 272 033 has the formula: (CH 3 (PEG) 43 ) 0 . 75 (POH) 0 . 25 [T-PO) 2.8 (T-PEG) 0 . 4 ] T (POH) 0.2S ( (PEG) 43 CH 3 ) 0 . 7S where PEG is -(OC 2 H 4 )0-, PO is (OC 3 H 6 0) and T is (pOOC 6 H 4 CO) . Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene gly- col and 1, 2-propanediol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or 1, 2-propanediol . The target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of said copolymers herein will be endcapped by sul- phobenzoate groups. However, some copolymers will be less than fully capped, and therefore their end groups may consist of mono- ester of ethylene glycol and/or 1, 2-propanediol , thereof consist "secondarily" of such species. The selected polyesters herein contain about 46% by weight of dimethyl terephthalic acid, about 16% by weight of 1, 2-propanediol , about 10% by weight ethylene glycol, about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoi- sophthalic acid, and have a molecular weight of about 3.000. The polyesters and their method of preparation are described in detail in EP 311 342. Softening agents: Fabric softening agents can also be incorporated into laundry detergent compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic softening agents are exemplified by the smectite clays disclosed in GB-A-1 400898 and in US 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP 0 Oil 340 and their combination with mono Ci 2 -C 14 quaternary ammonium salts are disclosed in EP-B-0 026 528 and di-long-chain amides as disclosed in EP 0 242 919. Other use- ful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP 0 299 575 and 0 313 146. Levels of smectite clay are normally in the range from 5% to 15%, more preferably from 8% to 12% by weight, with the material being added as a dry mixed component to the remainder of the formulation. Organic fabric softening agents such as the water-insoluble tertiary amines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight, normally from 1% to 3% by weight whilst the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight. These materials are normally added to the spray dried portion of the composition, although in some instances it may be more con- venient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition. Polymeric dye-transfer inhibiting agents: The detergent compositions according to the present invention may also comprise from 0.001% to 10%, preferably from 0.01% to 2%, more preferably form 0.05% to 1% by weight of polymeric dye- transfer inhibiting agents. Said polymeric dye-transfer inhibiting agents are normally incorporated into detergent compositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability of complexing or adsorbing the fugitive dyes washed out of dyed fabrics before the dyes have the opportunity to become attached to other articles in the wash. Especially suitable polymeric dye-transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinyl-pyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxa- zolidones and polyvinylimidazoles or mixtures thereof. Addition of such polymers also may enhances the performance of the enzymes according the invention. Form and performance of the composition: The detergent composition according to the invention can be in liquid, paste, gels, bars, powder or granular forms. Non-dusting granulates may be produced, e.g., as disclosed 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 (poly- ethyleneglycol, 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 GB 1483591. Granular compositions according to the present invention can also be in "compact form", i.e. they may have a relatively higher density than conventional granular detergents, i.e. form 550 to 950 g/1; in such case, the granular detergent compositions according to the present invention will contain a lower amount of "Inor- ganic filler salt", compared to conventional granular detergents; typical filler salts are alkaline earth metal salts of sulphates and chlorides, typically sodium sulphate; "Compact" detergent typically comprise not more than 10% filler salt. The liquid compositions according to the present invention can also be in "con- centrated form", in such case, the liquid detergent compositions according to the present invention will contain a lower amount of water, compared to conventional liquid detergents. Typically, the water content of the concentrated liquid detergent is less than 30%, more preferably less than 20%, most preferably less than 10% by weight of the detergent compositions. The compositions of the invention may for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in general household hard surface cleaning operations and dishwashing operations. In order to enable the skilled person - at an early stage of his development work - to select effective and preferred subtilase variants as well as effective and preferred alkylpolysaccharides or polyhydroxy fatty acid amides to be incorporated in the deter- gent compositions of the invention, the present inventors have provided suitable tests which can easily be carried out by the skilled person in order to initially assess the performance of the above-mentioned components (i.e. the subtilase variants described herein as well as the specific surfactants described herein) in a detergent composition. Thus, the test "Wash Performance Test I" disclosed herein may be employed to assess the efficiency of the selected alkylpolysaccharides or the selected polyhydroxy fatty acid amide. In other words, the "Wash Performance Test I" may be employed to assess the increase in the ability of a model detergent composition (comprising the alkylpolysaccharide or the polyhydroxy fatty acid amide) to remove protein stains from a standard textile as compared to a similar model detergent composition, wherein the non- ionic tenside (Dobanol 25-7) has been partly or fully substituted for the alkylpolysaccharide or the polyhydroxy fatty acid amide. Using this test, the suitability of a alkylpolysaccharide or the polyhydroxy fatty acid amide as an nonionic surfactant in the composition of the invention can be initially assessed, the ra- tionale being that if a alkylpolysaccharide or a polyhydroxy fatty acid amide does not show significant effect in at least one of these tests, it is normally not necessary to carry out further test experiments. Therefore, alkylpolysaccharides or polyhydroxy fatty acid amides, which are interesting for the purposes described herein are such alkylpolysaccharides or polyhydroxy fatty acid amides, which - when formulated in model detergent composition A, B, C, D, and/or E (the compositions of model detergent compositions A, B, C, D, and E are described in Example 1 herein) and when tested in the Wash Performance Test I, described herein - said model detergent composition has a Performance Parameter, as defined herein, of at least 1.1 relative to a similar model detergent component compo- sition comprising 5% w/w nonionic tenside (Dobanol 25-7) but without alkylpolysaccharide or polyhydroxy fatty acid amide. In particular interesting embodiments of the invention the Performance Factor is at least 1.25, such as at least 1.5, e.g. at least 1.75, at least 2, such as at least 2.25. Evidently, it is preferred that the alkylpolysaccharide or the polyhydroxy fatty acid amide to be incorporated in the detergent compositions of the invention should fulfill the above criteria on at least the stated lowest level, more preferably at the stated intermediate level and most preferably on the stated highest level . In a similar way, the test "Wash Performance Test II" disclosed herein may be employed to assess the efficiency of the selected subtilase variants. Thus, the "Wash Performance Test II" may be employed to assess the increase in the ability of a subtilase variant (when tested together with a model detergent composition comprising alkylpolysaccharide or polyhydroxy fatty acid amide) to remove protein stains from a standard textile as compared to the parent subtilase tested under identical conditions, i.e. tested together with the same alkylpolysaccharide-containing or polyhydroxy fatty acid amide-containing model detergent composition as employed in the testing of the variant. Using this test, the suitability of the variant in the composition of the invention can be initially assessed, the rationale being that if the variant does not show significant effect in at least one of these tests, it is normally not necessary to carry out further test experiments. Thus, subtilase variants which are interesting for the purposes described herein are such subtilase variants which - when tested in the Wash Performance Test II, as described herein, together with a model detergent composition A, B, C, D and/or E (the compositions of model detergent compositions A, B, C, D, and E are described in Example 1 herein) - said subtilase variant has a Performance Factor, as defined herein, of at least 1.1. relative to the performance of the parent subtilase tested together with an identical model detergent composition, i.e. when tested together with model composition A, B, C, D, or E . In particular interesting embodiments of the invention the Performance Factor is at least 1.25, such as at least 1.5, e.g. at least 1.75, at least 2, such as at least 2.25. Evidently, it is preferred that the subtilase variants to be in- corporated in the detergent compositions of the invention should fulfill the above criteria on at least the stated lowest level, more preferably at the stated intermediate level and most preferably on the stated highest level . In order to enable the skilled person - at an early stage of his development work - to select effective and preferred subtilase variants as well as effective and preferred α-sulfonated fatty acid esters to be incorporated in the detergent compositions of the invention, the present inventors have provided suitable tests which can easily be carried out by the skilled person in order to initially assess the performance of the above-mentioned components (i.e. the subtilase variants described herein as well as the α-sulfonated fatty acid esters described herein) in a detergent composition. Thus, the test "Wash Performance Test III" disclosed herein may be employed to assess the efficiency of the selected α-sulfonated fatty acid esters. In other words, the "Wash Performance Test III" may be employed to assess the increase in the ability of a model detergent composition (comprising the α-sulfonated fatty acid ester) to remove protein stains from a standard textile as compared to a similar model detergent composition, wherein LAS has been partly or fully substituted for the α-sulfonated fatty acid ester. Using this test, the suitability of an α-sulfonated fatty acid ester as an anionic surfactant in the composition of the invention can be initially assessed, the rationale being that if an α-sulfonated fatty acid ester does not show significant effect in at least one of these tests, it is normally not necessary to carry out further test experiments. Therefore, α-sulfonated fatty acid esters which are interesting for the purposes described herein are such α-sulfonated fatty acid esters which - when formulated in model detergent composi- tion A*, B*, C*, D* , E*, and/or F* (the compositions of model detergent compositions A*, B* , C* , D* , E*, and F* are described in Example 2 herein) and when tested in the Wash Performance Test III, described herein - said model detergent composition has a Performance Parameter, as defined herein, of at least 1.1 rela- tive to a similar model detergent component composition comprising 20% w/w LAS (Nansa 80S) but without α-sulfonated fatty acid ester In particular interesting embodiments of the invention the Per- formance Factor is at least 1.25, such as at least 1.5, e.g. at least 1.75, at least 2, such as at least 2.25. Evidently, it is preferred that α-sulfonated fatty acid esters to be incorporated in the detergent compositions of the invention should fulfill the above criteria on at least the stated lowest level, more preferably at the stated intermediate level and most preferably on the stated highest level . In a similar way, the test "Wash Performance Test IV" disclosed herein may be employed to assess the efficiency of the selected subtilase variants. Thus, the "Wash Performance Test IV" may be employed to assess the increase in the ability of a subtilase variant (when tested together with a model detergent composition comprising α-sulfonated fatty acid ester) to remove protein stains from a standard textile as compared to the parent subtilase tested under identical conditions, i.e. tested together with the same α-sulfonated fatty acid ester-containing model detergent composition as employed in the testing of the variant. Using this test, the suitability of the variant in the composition of the invention can be initially assessed, the rationale being that if the variant does not show significant effect in at least one of these tests, it is normally not necessary to carry out further test experiments. Thus, subtilase variants which are interesting for the purposes described herein are such subtilase variants which - when tested in the Wash Performance Test IV, as described herein, together with a model detergent composition A*, B* , C* , D* , E* and/or F* (the compositions of model detergent compositions A*, B* , C*, D* , E* and F* are described in Example 2 herein) - said subtilase variant has a Performance Factor, as defined herein, of at least 1.1. relative to the performance of the parent subtilase tested together with an identical model detergent composition, i.e. when tested together with model composition A*, B* , C* , D* , E* or F* . In particular interesting embodiments of the invention the Performance Factor is at least 1.25, such as at least 1.5, e.g. at least 1.75, at least 2, such as at least 2.25. Evidently, it is preferred that the subtilase variants to be incorporated in the detergent compositions of the invention should fulfill the above criteria on at least the stated lowest level, more preferably at the stated intermediate level and most preferably on the stated highest level . Furthermore, it is contemplated that the composition of the invention may confer an increased stability to the subtilase vari- ants described herein and hence increase the shelf-life of the detergent compositions of the invention. Accordingly, in an interesting embodiment of the invention, the subtilase variant in the detergent composition of the invention exhibits an increase in the half-life of at least 10%, preferably at least 15%, e.g. at least 20%, when compared to the half-life in a similar detergent composition, wherein the non-ionic surfactant has been partly or fully substituted for the alkylpolysaccharide or the polyhydroxy fatty acid amide, or wherein the anionic surfactant 5 has been partly or fully substituted for the α-sulfonated fatty acid ester. Testing of the shelf-life may, for example, be performed such as described in EP 0 916 732. Other methods, which will be known to 10 the skilled person, may also be applicable. The invention is further illustrated by the following non- limiting examples. 15 In the detergent compositions, the abbreviated component identifications have the following meanings: LAS: Sodium linear C 12 alkyl benzene sulphonate 20 Nonionic: C 13 -C 15 mixed ethoxylated/propoxylated fatty alcohol with an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5 sold under the tradename Plurafax LF404 by BASF Gmbh 25 CMC: Sodium carboxymethyl cellulose EXAMPLE 1 Testing of wash performance of detergent compositions 30 A number of model detergent compositions (model detergent compositions A-E) may be prepared as described below: The composition of model detergent composition A is as follows: 35 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4 _ 10% w/w Na 2 C0 3; 20% w/w LAS (Nansa 80S) , 4.0% w/w Nonionic tenside (Dobanol 25-7), 1.0% w/w Alkylpolysaccharide or polyhydroxy fatty acid amide, 5.0% w/w Na 2 Si 2 0 5, 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. 5 The composition of model detergent composition B is as follows: 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4ι 10 10% w/w Na 2 C0 3 _ 20% w/w LAS (Nansa 80S) , 3.0% w/w Nonionic tenside (Dobanol 25-7), 2.0% w/w Alkylpolysaccharide or polyhydroxy fatty acid amide, 5.0% w/w Na 2 Si 2 0 5; 15 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. The composition of model detergent composition C is as follows: 20 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4r 10% w/w Na 2 C0 3 _ 20% w/w LAS (Nansa 80S) , 2.0% w/w Nonionic tenside (Dobanol 25-7), 25 3.0% w/w Alkylpolysaccharide or polyhydroxy fatty acid amide, 5.0% w/w Na 2 Si 2 0 5 _ 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. 30 The composition of model detergent composition D is as follows: 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4 _ 10% w/w Na 2 C0 3 35 20% w/w LAS (Nansa 80S) , 1.0% w/w Nonionic tenside (Dobanol 25-7), 4.0% w/w Alkylpolysaccharide or polyhydroxy fatty acid amide, 5.0% w/w Na 2 Si 2 0 5, 0.5% w/w Carboxymethylcellulose (CMC), and 9 . 5% w/w Water . The composition of model detergent composition E is as follows: 25% w/w STP (Na 5 P 3 o 10 ) 25% w/w Na 2 S0 4 10% w/w Na 2 C0 3ι 20% w/w LAS (Nansa 80S) , 5.0% w/w Alkylpolysaccharide or polyhydroxy fatty acid amide, 5.0% w/w Na 2 Si 2 0 5, 0.5% w/w Carboxymethylcellulose (CMC) , and 9.5% w/w Water. The below tests may then be employed in order to assess the wash- ing performance of selected alkylpolysaccharides or polyhydroxy fatty acid amides and subtilase variants, respectively. Wash Performance Test I In order to assess the effect of incorporating alkylpolysaccha- ride or polyhydroxy fatty acid amide in a detergent composition, standard washing experiments may be performed using the below experimental conditions: Detergent : Model detergent A, B, C, D, or E Detergent dose: 3.0 g/1 pH: 10.5 Wash time: 15 min. Temperature : 15°C Water hardness : 6°dH Enzymes: Any specific subtilase variant mentioned herein Enzyme concentration: 10 nM (in the detergent solution) Test system: 150 ml beakers with a stirring rod Textile/volume : 5 textile pieces (0 2.5 cm) /50 ml detergent solution Test material EMPA117 from Center of Testmaterials, Holland pH of the detergent solution is adjusted to 10.5 by addition of HCl. Water hardness is adjusted to 6°dH by addition of CaCl 2 and MgCl 2 (Ca 2+ :Mg 2+ = 2:1) to the test system. After washing the textile pieces were flushed in tap water and air-dried. 5 Measurement of the reflectance (R) on the test material is performed at 460 nm using a Macbeth Coloreye 7000 photometer (Macbeth, Division of Kollmorgen Instrumetns Corporation, Germany) . The measurements are performed in accordance with the manufac- 10 turer's protocol. In order to determine a blank value a similar wash experiment is performed without addition of enzyme. Measurement of the reflectance (R bιank ) on the test material is performed as described 15 above . A reference experiment is then performed (as described above) , wherein the wash performance of the subtilase variant in question is tested together with a standard model detergent not containing 20 alkylpolysaccharide or polyhydroxy fatty acid amide. The composition of the standard model detergent composition is as follows: 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4 25 10% w/w Na 2 C0 3 _ 20% w/w LAS (Nansa 80S) 5.0% w/w Nonionic tenside (Dobanol 25-7), 5.0% w/w Na 2 Si 2 0 5 _ 0.5% w/w Carboxymethylcellulose (CMC), and 30 9.5% w/w Water, i.e. the standard model detergent composition resembles model detergent compositions A,B,C,D, and E, the only difference being that Dobanol 25-7 is partly or completely substituted for the al- 35 kylpolysaccharide or polyhydroxy fatty acid amide present in the model detergent compositions A,B,C,D, and E. Subsequent measurement of the reflectance (R eference ) on tne test material is performed as described above . The wash performance is evaluated by means of the Performance Factor : P = (R 'blank -)' / ' i where P is the Performance Factor and R, R bιank and R reference are as defined above . The performance may conveniently be divided into "improvement classes" designated by the following capital letters: Class A 1 < P < 1.5 Class B 1.5 < P < 2 Class C P > 2 Wash Performance Test II In order to assess the effect of incorporating the subtilase variants described herein relative to the effect obtained when the parent subtilase is incorporated in a detergent composition according to the invention, standard washing experiments may be performed using the below experimental conditions: Detergent : Model detergent A, B, C, D or E Detergent dose: 3.0 g/1 pH: 10.5 Wash time: 15 min. Temperature : 15°C Water hardness: 6°dH Enzymes : Any specific subtilase variant mentioned herein Enzyme concentration: 10 nM (in the detergent solution) Test system: 150 ml beakers with a stirring rod Textile/volume : 5 textile pieces (0 2.5 cm) /50 ml detergent solution Test material : EMPA117 from Center of Testmaterials, Holland pH of the detergent solution is adjusted to 10.5 by addition of HCl. Water hardness is adjusted to 6°dH by addition of CaCl 2 and MgCl 2 (Ca + :Mg 2+ = 2:1) to the test system. After washing the textile pieces were flushed in tap water and air-dried. Measurement of the reflectance (R) on the test material is per- formed at 460 nm using a Macbeth Coloreye 7000 photometer (Macbeth, Division of Kollmorgen Instrumetns Corporation, Germany) . The measurements are performed in accordance with the manufacturer's protocol. In order to determine a blank value a similar wash experiment is performed without addition of enzyme. Measurement of the reflectance (Ri an ) on tne test material is performed as described above . A reference experiment is then performed, wherein the wash performance of the parent subtilase is tested. The parent subtilase is tested together with the same model detergent composition as employed in determination of R and R blank , i.e. the parent subtilase is tested together with model detergent composition A,B,C,D, or E. Subsequent measurement of the reflectance (R eference ) on tne test material is performed as described above. The wash performance is evaluated by means of the Performance Factor: P — (R Rblanl / (R-ref erence Rblank ' where P is the Performance Factor and R, R blank and eference are as defined above. The performance may conveniently be divided into "improvement classes" designated by the following capital letters: Class A 1 < P < 1.5 Class B 1.5 < P < 2 Class C P > 2 EXAMPLE 2 Testing of wash performance of detergent compositions A number of model detergent compositions (model detergent compo- 5 sitions A*-F*) may be prepared as described below: The composition of model detergent composition A* is as follows: 25% w/w STP (Na 5 P 3 O 10 ) , 10 25% w/w Na 2 S0 4 10% w/w Na 2 C0 3 _ 19% w/w LAS (Nansa 80S) , 1% w/w α-sulfonated fatty acid ester, 5.0% w/w Nonionic tenside (Dobanol 25-7), 15 5.0% w/w Na 2 Si 2 0 5ι 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. The composition of model detergent composition B* is as follows 20 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4/ 10% w/w Na 2 C0 3 ι 17 . 5% w/w LAS (Nansa 80S ) , 25 2 . 5% w/w α- sul fonated fatty acid ester , 5 . 0 % w/w Nonionic tenside (Dobanol 25 - 7 ) , 5 . 0% w/w Na 2 Si 2 0 5 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. 30 The composition of model detergent composition C* is as follows; 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4/ 35 10% w/w Na 2 C0 3ι 15% w/w LAS (Nansa 80S) , 5% w/w α-sulfonated fatty acid ester, 5.0% w/w Nonionic tenside (Dobanol 25-7), 5.0% w/w Na 2 Si 2 0 5 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. The composition of model detergent composition D* is as follows: 5 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4 ι 10 % w/w Na 2 C0 3 10 % w/w LAS (Nansa 80S ) , 10 10% w/w α- sulfonated fatty acid ester , 5 . 0% w/w Nonionic tenside (Dobanol 25 - 7 ) , 5 . 0% w/w Na 2 Si 2 0 5 _ 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. 15 The composition of model detergent composition E* is as follows: 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4 _ 20 10% w/w Na 2 C0 3ι 5% w/w LAS (Nansa 80S) , 15% w/w α-sulfonated fatty acid ester, 5.0% w/w Nonionic tenside (Dobanol 25-7), 5.0% w/w Na 2 Si 2 0 5 _ 25 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. ' The composition of model detergent composition F* is as follows 30 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4; 10% w/w Na 2 C0 3 _ 20% w/w α-sulfonated fatty acid ester, 5.0% w/w Nonionic tenside (Dobanol 25-7), 35 5.0% w/w Na 2 Si 2 0 5 0.5% w/w Carboxymethylcellulose (CMC), and 9.5% w/w Water. The below tests may then be employed in order to assess the washing performance of selected α-sulfonated fatty acid esters and subtilase variants, respectively. Wash Performance Test III In order to assess the effect of incorporating α-sulfonated fatty acid ester in a detergent composition, standard washing experiments may be performed using the below experimental conditions: Detergent: Model detergent A* ,B* , C* ,D* , E* or F* Detergent dose: 3.0 g/1 pH: 10.5 Wash time: 15 min. Temperature: 15°C Water hardness : 6°dH Enzymes: Any specific subtilase variant mentioned herein Enzyme concentration: 10 nM (in the detergent solution) Test system: 150 ml beakers with a stirring rod Textile/volume: 5 textile pieces (0 2.5 cm) /50 ml detergent solution Test material: EMPA117 from Center of Testmaterials, Holland pH of the detergent solution is adjusted to 10.5 by addition of HCl. Water hardness is adjusted to 6°dH by addition of CaCl 2 and MgCl 2 (Ca + :Mg 2+ = 2:1) to the test system. After washing the textile pieces were flushed in tap water and air-dried. Measurement of the reflectance (R) on the test material is performed at 460 nm using a Macbeth Coloreye 7000 photometer (Macbeth, Division of Kollmorgen Instrumetns Corporation, Germany) . The measurements are performed in accordance with the manufacturer's protocol. In order to determine a blank value a similar wash experiment is performed without addition of enzyme. Measurement of the reflectance ( i ank ) on the test material is performed as described above . A reference experiment is then performed (as described above) , wherein the wash performance of the subtilase variant in question is tested together with a standard model detergent not containing 5 α-sulfonayed fatty acid ester. The composition of the standard model detergent composition is as follows: 25% w/w STP (Na 5 P 3 O 10 ) , 25% w/w Na 2 S0 4ι 10 10% w/w Na 2 C0 3 20% w/w LAS (Nansa 80S) 5.0% w/w Nonionic tenside (Dobanol 25-7), 5.0% w/w Na 2 Si 2 0 5 0.5% w/w Carboxymethylcellulose (CMC), and 15 9.5% w/w Water, i.e. the standard model detergent composition resembles model detergent compositions A* , B* , C* , D* , E* and F*, the only difference being that LAS is partly or completely substituted for the α- 20 sulfonated fatty acid ester present in the model detergent compositions A*,B* , C*,D* ,E* and F* . Subsequent measurement of the reflectance (R eference ) on the test material is performed as described above . 25 The wash performance is evaluated by means of the Performance Factor: P = (R - R b ι ank ) / (R re ference ~ ^blank' 30 where P is the Performance Factor and R, R blank and R reference are as defined above. The performance may conveniently be divided into "improvement classes" designated by the following capital letters: 35 Class A 1 < P < 1.5 Class B 1.5 < P < 2 Class C P > 2 Wash Performance Test IV In order to assess the effect of incorporating the subtilase variants described herein relative to the effect obtained when the parent subtilase is incorporated in a detergent composition according to the invention, standard washing experiments may be performed using the below experimental conditions: Detergent: Model detergent A* ,B*, C*,D*,E* or F* Detergent dose: 3.0 g/1 pH: 10.5 Wash time: 15 min. Temperature: 15°C Water hardness : 6°dH Enzymes: Any specific subtilase variant mentioned herein Enzyme concentration: 10 nM (in the detergent solution) Test system: 150 ml beakers with a stirring rod Textile/volume: 5 textile pieces (0 2.5 cm) /50 ml detergent solution Test material: EMPA117 from Center of Testmaterials, Holland pH of the detergent solution is adjusted to 10.5 by addition of HCl. Water hardness is adjusted to 6°dH by addition of CaCl 2 and MgCl 2 (Ca 2+ :Mg 2+ = 2:1) to the test system. After washing the textile pieces were flushed in tap water and air-dried. Measurement of the reflectance (R) on the test material is performed at 460 nm using a Macbeth Coloreye 7000 photometer (Mac- beth, Division of Kollmorgen Instrumetns Corporation, Germany) . The measurements are performed in accordance with the manufacturer's protocol. In order to determine a blank value a similar wash experiment is performed without addition of enzyme. Measurement of the reflectance (R b i an ) on the test material is performed as described above . A reference experiment is then performed, wherein the wash performance of the parent subtilase is tested. The parent subtilase is tested together with the same model detergent composition as employed in determination of R and R bιan , i.e. the parent subti- lase is tested together with model detergent composition A*,B*, C*,D*,E* or F* . Subsequent measurement of the reflectance (R reference ) on the test material is performed as described above. The wash performance is evaluated by means of the Performance Factor: P = (R - Rblank' / '^reference " ^blank' where P is the Performance Factor and R, R blank and R eference are as defined above. The performance may conveniently be divided into "improvement classes" designated by the following capital letters: Class A 1 < P < 1.5 Class B 1.5 < .P < 2 Class C P > 2

Claims: CLAIMS 1. A detergent composition comprising an effective amount of a subtilase variant, where the subtilase variant comprises a modi- 5 fication of the amino acid sequence at a calcium binding site such that the electrostatic attractive interaction between the amino acids at the calcium binding site and the calcium ion is increased relative to that of the corresponding parent subtilase, and an effective amount of a surfactant selected from the group 10 consisting of an alkylpolysaccharide comprising a hydrophobic moiety having from about 6 to about 30 carbon atoms and a hydrophilic moiety derived from a polysachharide containing from about 1.3 to about 15 10 saccharide units; a polyhydroxy fatty acid amide of the general formula (I) : R 2 -C(=0) -N R 1 ) (Z) (I) 20 wherein R 1 is selected from the group consisting of hydrogen, C - C 4 -hydrocarbyl, 2-hydroxyethyl, and 2-hydroxypropyl; R 2 is C 5 -C 31 hydrocarbyl, such as C 5 -C 31 -alkyl or C 5 -C 31 -alkenyl; and Z is selected from the group consisting of glucose, fructose, maltose, 25 lactose, galactose, mannose and xylose; and an α-sulfonated fatty acid esters. 2. A detergent composition according to claim 1, wherein the 30 modification in the subtilase variant is a substitution of a neutral or negatively charged amino acid for a positively charged amino acid. 3. A detergent composition according to claim 1, wherein the 5 modification in the subtilase variant is a substitution of Asp or Glu for a neutral amino acid. 4. A detergent composition according to claim 1, wherein the modification in the subtilase variant is a substitution of Asp or Glu for a positively charged amino acid. 5 5. A detergent composition according to claim 1, wherein the modification in the subtilase variant is a deletion of a positively charged amino acid. 6. A detergent composition according to claim 1, wherein the 10 modification in the subtilase variant is an insertion of a neutral or negatively charged amino acid. 7. A detergent composition according to any of the preceding claims, wherein the calcium binding site being modified is the 15 calcium A binding site. 8. A detergent composition according to any of claims 1-6, wherein the calcium binding site being modified is the calcium B binding site. 20 9. A detergent composition according to any of claims 1-6, wherein the calcium binding site being modified is both the calcium A binding site and the calcium B binding site. 25 10. A detergent composition according to any of claims 1-9, wherein the parent subtilase is selected from the sub-group I-Sl. 11. A detergent composition according to claim 10, wherein the parent subtilase is selected from the group consisting of 30 ABSS168, BASBPN, BSSDY, BLSCAR, and functional variants thereof having retained the characteristic of sub-group I-Sl. 12. A detergent composition according to any of claims 1-9, wherein the parent subtilase is selected from the sub-group I-S2. 35 13. A detergent composition according to claim 12, wherein the parent subtilase is selected from the group consisting of BLS147, BLS309, BAPB92, TVTHER, BYSYAB, and functional variants thereof having retained the characteristic of sub-group I-S2. 14. A detergent composition according to any of the preceding claims, wherein said modification (s) is/are combined with one or more modification (s) in any other position (s) . 5 15. A detergent composition according to claim 14, wherein said modification (s) is/are combined with modification (s) in one or more of the positions 27, 36, 57, 76, 87, 97, 101, 103, 104, 120, 123, 159, 206, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 10 274. 16. A detergent composition according to claim 15, wherein said subtilase belongs to the I-S2 sub-group and said further change is selected from the group consisting of K27R, *36D, S57P, N76D, 15 S87N, G97N, S101G, S103A, V104A, V104N, V104Y, V104I, H120D, N123S, G159D, Q206E, N218S, M222S, M222A, T224S, A232V, K235L, Q236H, Q245R, N248D, N252K and T274A. 17. A detergent composition according to claim 15, wherein said 20 modification (s) is/are combined with the modification (s) S101G+V104N, S87N+S101G+V104N, K27R+V104Y+N123S+T274A, N76D+V104A, S101G+S103A+V104I+G159D+A232V+Q236H+Q245R+N248D+N252K or other combinations of these mutations (V104N, S101G, K27R, V104Y, N123S, T274A, N76D, V104A) , in combination with any one or 25 more of the substitutions, deletions and/or insertions mentioned in any of claims 1 to 16. 18. A detergent composition according to any of the preceding claims, wherein said modificaton (s) is/are combined with modifi- 30 cation (s) in one or more of the positions 129, 131, 133 and 194. 19. A detergent composition according to claim 18, wherein said subtilase belongs to the I-S2 sub-group and said further modification is selected from the group consisting of P129K, P131H, 35 A133P, A133D and A194P. 20. A detergent composition according to any of the preceding claims, wherein said polysaccharide contains from about 1.3 to about 3 saccharide units, preferably from about 1.3 to about 2.7 saccharide units. 21. A detergent composition according to claim 20, wherein the 5 saccharide units are derived from glucose. 22. A detergent composition according to claims 20 or 21, wherein the alkylpolysaccharide has the general formula I ιo R 3 0 (C n H 2n O) t (glycosyl ) , wherein R 3 is selected from the group consisting of alkyl, alkyl - phenyl, hydroxyalkyl, hydroxyalkylphenyl and mixtures thereof in which the alkyl group contains from about 10 to about 18 carbon 15 atoms atoms; n is 2 or 3; t is from 0 to 10; and x is from about 1.3 to 10. 23. A detergent composition according to claim 22, wherein x is from about 1.3 to about 3, preferably from about 1.3 to about 20 2.7. 24. A detergent composition according to claims 22 or 23, wherein t is 2. 25 25. A detergent composition according to any of claims 22-24, wherein n is 0. 26. A detergent composition according to any of claims 22-25, wherein the alkyl group contains from about 10 to 16 carbon at- 30 oms, preferably from about 12 to about 14 carbon atoms. 27. A detergent composition according to any of claims 1-19, wherein R 1 and R 2 are saturated. 35 28. A detergent composition according to claim 27, wherein R 1 is selected from the group consisting of methyl, ethyl, n-propyl and n-butyl . 29. A detergent composition according to claim 28, wherein R 1 is methyl . 30. A detergent composition according to any of claims 27-29, 5 wherein R 2 is C 10 -C 31 -alkyl or a mixture thereof. 31. A detergent composition according to claim 30, wherein R 1 is C 12 -C 18 -alkyl or a mixture thereof. 10 32. A detergent composition according to claim 31, wherein R 1 is C 12 -C 14 -alkyl or a mixture thereof. 33. A detergent composition according to claim 32, wherein R 1 is C 16 -C 18 -alkyl or a mixture thereof. 15 34. A detergent composition according to any of claims 27-33, wherein Z is glucose. 35. A detergent composition according to any of claims 27-34, 20 wherein the polyhydroxy fatty acid amide is selected from the group consisting of C 12 -C 14 -alkyl N-methyl glucamide and C 16 -C 18 - alkyl N-methyl glucamide . 36. A detergent composition according to any of claims 1-19, 25 wherein the α-sulfonated fatty acid ester has the general formula I R x -CH(S0 3 M) -C(=0) -OR y (I) 30 wherein R x is a C 8 -C 20 hydrocarbyl group, R y is a C 1 -C 6 hydrocarbyl group, and M is a cation which forms a water-soluble salt with the α-sulfonated fatty acid ester. 37. A detergent composition according to claim 36, wherein R x is 35 a C 8 -C 20 alkyl group. 38. A detergent composition according to claim 37, wherein R x is a C 10 -C 16 alkyl group. 39. A detergent composition according to any of claims 36-38, wherein the cation is selected from the group consisting of metal ions, such as sodium, potassium and lithium, and substituted and unsubstituted ammonium cations, such as monoethanolamine, dietha- 5 noleamine and triethanolamine . 40. A detergent composition according to any of claims 36-39, wherein R y is a C.-C 6 alkyl group. 10 41. A detergent composition according to claim 40, wherein R y is selected from the group consisting of methyl, ethyl, n-propyl and isopropyl . 42. A detergent composition according to claim 41, wherein R y is 15 methyl . 43. A detergent composition according to any of claims 36-42, wherein the α-sulfonated fatty acid ester is selected from the group consisting of α-sulfonated lauric acid methyl ester, α- 20 sulfonated tridecylic acid mehtyl ester, α-sulfonated myristic acid methyl ester, α-sulfonated pentadecylic acid methyl ester, α-sulfonated palmitic acid methyl ester, and mixtures thereof. 44. A detergent composition according to any of the preceding 25 claims, said detergent composition further comprises one or more cleaning adjuncts selected from the group consisting of other surfactants, solvents, buffers, enzymes, soil release agents, clay soil removal agents, dispersing agents, brighteners, suds suppressors, fabric softeners, suds boosters, enzyme stabilisers, 0 builders, other bleaching agents, dyes, perfumes, chelants and mixtures thereof . 45. A detergent composition according to claim 44 further comprising at least one additional enzyme selected from the group 5 consisting of cellulases, lipases, amylases, phospholipases, other subtilases, peroxidases and mixtures thereof. 46. A detergent composition according to any of the preceding claims, wherein the detergent composition is in the form of a liquid, granule, paste, bar, tablet, gel, powder or foam.

Inventors: MIKKELSEN FRANK F, VON DER OSTEN CLAUS, MIKKELSEN, FRANK, F., VON DER OSTEN, CLAUS
Applicants: NOVOZYMES AS, NOVOZYMES A/S
Application year: 2000
Main classification: C11D
IPC codes: C11D1, C11D3