DETERGENT COMPOSITIONS COMPRISING AN AMYLOGLUCOSIDASE ENZYME

Abstract: The present invention relates to detergent compositions, including laundry, dishwashing, and/or hard surface cleaner compositions, comprising an amyloglucosidase enzyme. Such compositions provide excellent removal of starch-containing stains and soils, and when formulated as laundry compositions, excellent whiteness maintenance and dingy cleaning.

Description: DETERGENT COMPOSITIONS COMPRISING AN AMY OGLUCOSIDASE ENZYME Field of the Invention The present invention relates to detergent compositions comprising an amyloglucosidase enzyme. Background of the invention Performance of a detergent product is judged by a number of factors, including the ability to remove soils. Therefore, detergent components such as surfactants, bleaching agents and enzymes, have been incorporated in detergents. One of such specific example is the use of proteases, lipases, amylases and/or cellulases. Proteases are commonly used enzymes in cleaning applications. Proteases are known for their ability to hydrolyse other proteins. This ability has been taken advantage of through the incorporation of naturally occurring or engineered protease enzymes in laundry detergent compositions. The inclusion of lipolytic enzymes in detergent compositions for improved cleaning performance is known, e.g. enhancement of removal of triglycerides containing soils and stains from the fabrics. The activity of cellulase is one in which cellulosic fibres or substrates are attacked by the cellulase and is depending on the particular function of the cellulase, which can be endo- or exo- cellulase, and of the respective hemicellulases. The cellulose structures are depolymerized or cleaved into smaller and thereby more soluble or dispersible fractions. This activity in particular on fabrics provides a cleaning, rejuvenation, softening and generally improved handfeel characteristics to the fabric structure. Amylase enzymes have long been recognised in detergent compositions to provide the removal of starchy food residues or starchy films from dishware or hard surfaces or to provide cleaning performance on starchy soils as well as other soils typically encountered in laundry and dishwashing applications. Indeed, starchy materials such as amylose and amylopectin, constitute one of the major components of the soils /stains encountered in laundry, dishwashing or hard surfaces cleaning operations. Moreover, the textile industry uses starchy materials in their textile finishing processes. Therefore, amylase enzymes have been since a long time incorporated into the detergent products for the removal of starch-containing stains. However, it has been surprisingly found that such commonly used detergent amylases could not hydrolyse retrograded starch. As studied in J. A. Radiey "Starch and its Derivatives" Fourth Edition Chapman and Hall Ltd p194-201 ; retrogradation is a term given to the changes which occur spontaneously in a starch paste, or gel on ageing. It arises from the inherent tendency of starch molecules to bind to one another and which leads to an increase in crystallinity. Solutions of low concentration become increasingly cloudy due to the progressive association of starch molecules into larger particles. Spontaneous precipitation takes place and the precipitated starch appears to be reverting to its original condition of cold-water insolubility. Pastes of higher concentration on cooling set to a gel, which on ageing becomes steadily firmer due to the increasing association of the starch molecules. This arises because of the strong tendency for hydrogen bond formation between hydroxy groups on adjacent starch molecules. The changes taking place during retrogradation are of considerable importance in the industrial uses of starch. It is believed to be an important factor in the staling of bread and in the textural changes of other starch-containing foods, e.g. canned soups, peas, meat preparations, etc. Starch and retrograded starch are also found in the textile, paper and adhesives industries. Indeed, fabrics are sized with starch in the textile process. Depending on the sizing process, retrograded starch can be formed on the fabrics and might not be removed in the ulterior desizing processes. Moreover, the majority of the stains/soils found on fabrics, dishware and other hard surfaces, especially those found in the kitchen, contain starch which upon ageing in for e.g., the laundry basket or dishwashing machine will retrograde to such associated starchy network. Hence, such retrograded starch containing materials are found later onto the fabric, dishware and/or other hard surfaces to be cleaned. Furthermore, it has been surprisingly found that such retrograded starch entraps further dirt and, when found a fabric surface, leads to a dingy appearance of the surface to be cleaned. Such retrograded starch shows an increased resistance to hydrolysis by amyiolytic enzymes, is only slightly soluble at ordinary temperatures and redispersed only with difficulty, especially if the retrograded starch has dried first and it further demonstrates a progressive increase in gel firmness. Indeed, it has been found that retrograded starch forms very stable structures and only melts at very high temperature such as 150°C for amylose, 60°C for amylopectin or 120°C for the complex amylose-lipid. The level and timing of retrogradation depends upon the starch type: it can vary from 10% to 90% of the starch content. It has been found that current detergent amylases have very little to no effect on retrograded starch. As can be seen from the above, there is a need to formulate detergent products which address the removal of such retrograded starch containing soils/stains. Accordingly, the above objective has been met by formulating a detergent composition comprising an amyloglucosidase enzyme. It has been further found that the performance of the detergent compositions of the present invention is synergistically enhanced by the addition of a further enzyme from the amylase class, such as an α-amylase; a neopullulanase, a pullulanase type II; a dextrin dextranase; a cyclomaltodextrin glucanotransferase and/or a starch debranching enzyme. Starch comprises mainly amylopectin which consists of α-1 ,4 and α-1 ,6 glucose linking. Therefore, it has been surprisingly found that the combination of the amyloglucosidase being an exo- amylase active on α-1 ,4 and α-1 ,6 bonds in starch, in combination with an enzyme from the amylase class, for example an endo α-amylase which is active on α-1 ,4 bonds in starch, gives a more effective breakdown of starch contained in stains and soils and gives improved release of glucose. Hence, it has been found that such a combination of enzymes within the detergent compositions of the present invention, will provide improved stain removal, and when formulated as a laundry detergent composition, whiteness maintenance and dingy clean up. Preferably, the detergent compositions of the present invention will further comprise a detergent ingredient selected from another detergent enzyme such as a protease and a lipase, a bleaching agent and/or a nonionic surfactant. US 5,665,585 is directed to an amino acid and DNA sequence of a unique glucoamylase P that has a high debranching activity, a Trichoderma host cell transformed with such sequences, the expression of such recombinant glucoamylase P and the industrial uses in particular the alcohol fermentation, for the recombinant enzymes and host transformed therewith. US 3,640,877 describes detergent preparation containing a system of glucose and glucose oxidase or starch, amyloglucosidase and glucose oxidase as precursor of hydrogen peroxide and a hydroxylamine which stabilises the hydrogen peroxide formed during the use of the detergent. WO95/29996 discloses a novel glucose oxidase, a process for its production and its use in bleaching and detergent compositions as well as its use as a dough strengthener. Said enzyme has many applications in the personal care area and the baking industry, preferably in combination with another enzyme selected from amyloglucosidase, lactoperoxidase, α-amylase or a maltogenic exo-amylase. However, the use of an amyloglucosidase for the removal of retrograded starch- containing stains-soils in a detergent composition, has never been previously recognised. Summary of the invention The present invention relates to detergent compositions, including laundry, dishwashing, and/or hard surface cleaner compositions, comprising an amyloglucosidase with the proviso that such detergent compositions do not comprise a glucose oxidase. Such compositions provide excellent removal of starch-containing stains and soils, and when formulated as laundry compositions, excellent whiteness maintenance and dingy cleaning. Detailed description of the invention The essential component of the detergent compositions of the present invention is an amyloglucosidase of the IUPAC Classification EC 3.2.1 .3. Such amyloglucosidase is a glucan 1 ,4-α-glucosidase; is also referred to as "glucoamylase, γ-amylase, iysosomal α-glucosidase, acid maltase or exo-1 ,4-α- glucosidase" and its systematic name is 1 ,4-α-D-glucan glucohydrolase. Amyioglucosidases hydrolyse both α-1 ,4 and α-1 ,6 linkages in polysaccharides such as starch, liberating glucose units from non-reducing ends of polysaccharides. These two activities are distinct. By hydrolysing α-1 ,4 and α-1 ,6 glucosidic bonds, amyioglucosidases liberate β-D-glucose units from terminal non-reducing ends of a glucose polymer such as starch. They differ considerably from starch debranching enzymes in their ability to hydrolyse α-1 ,6 glucosidic bonds. Such amyloglucosidase is generally comprised in the detergent compositions of the present invention at a level of from 0.0002% to 10%, preferably 0.001% to 2%, more preferably 0.001 % to 1 % pure enzyme by weight of the total detergent composition. Suitable amyloglucosidase for the purpose of the present invention are described below: Several genes coding for various glucoamylases have been cloned and expressed either in yeast or fungal expression systems. A procedure for purifying glucoamylase P as well as portions of its amino acid sequence have been published (Fagerstrδm et al., J. Gen. Microbiol. 136:913- 920 (1990)). In addition, a restriction map of two overlapping glucoamylase cDNA fragments has been published as well as evidence which suggests that recombinant laboratory yeast may be used to express this gene (Torkkeli et al., XIII International Specialized Symposium on Yeasts, Leuven, Belgium (1989)). The glucoamylase genes from both Aspergillus niger (WO 86/07091 ; WO 88/09795; U.S. Pat. No. 5,024,941 ) and from Aspergillus awamori (U.S. Pat. No. 4,794,175 and EP Patent No. 126206) have been cloned and expressed in yeast cells. The glucoamylase gene from a fungus of the genus Rhizopus has been expressed in Saccharomyces cerevisiae (EP Application Publication No. 186066). In addition, other types of amylolytic yeast have been constructed by the introduction of a modified Rhizopus glucoamylase gene (Ashikari et al., App. Microbiol. and Biotech. 32:129-133 (1989)). A recombinant Saccharomyces has been constructed by transforming S. cerevisiae with a glucoamylase gene from C. albicans resulting in the secretion of the α-(1 ,4)-glucosidic bond-cleaving enzyme (EP Patent Application Publication No. 0362179). The glucoamylase gene from Schwanniomyces castellii has been cloned and expressed in Saccharomyces cerevisiae as well as in other forms of yeast (EP Patent Application Publications No. 0260404 and No. 0257115). Brewing yeasts have been transformed with a recombinant plasmid having a gene coding for a glucoamylase of Saccharomyces diastaticus (Park et al., MBAA Technical Quarterly 27:1 12-116 (1990)). An amylolytic S. cerevisiae strain which is able to use starch as its sole source of carbon has been developed and used to express the α-amylase and glucoamylase genes of Schwanniomyces occidentalis (Hollenberg and Strasser, Food Biotechnology 4:527-534 (1990)). Dohmen et al., Gene 95:111-121 (1990), have expressed a Schwanniomyces occidentalis glucoamylase in S. cerevisiae cells by transforming the cells with centromere plasmids carrying the glucoamylase gene fused to different S. cerevisiae promoters. The amino acid sequences of several different microbiai glucoamylases have been determined. The complete sequences of Aspergillus niger (Svensson et al., Cahsberg Res. Comm. 48:529-544 (1983)) and Aspergillus awamori (Nunberg et al., Mol. and Cell. Biol. 4:2306-2315 (1984)) glucoamylases are identical. The glucoamylase enzymes from Rhizopus oryzae (Ashikah et al., Agricultural and Biological Chem. 50:957-964 (1986)), Saccharomyces diastaticus (Yamashita et al., J. Bacteriol. 161 :567-573 (1985)), Saccharomyces cerevisiae (Yamashita et al., J. Bacteriol. 169:2142-2149 (1987)); Aspergillus shirousami (Shibuya et al., Agric. Bio. Chem. 54:1905-1914 (1990)); Schwanniomyces occidentalis (Dohmen et al., Gene 95:111-121 (1987)); Clostridium sp. G0005 (Ohnishi et al., Eur. J. Biochem. 207:413-418 (1992)); and Saccharomycopis fibuligera (Itoh et al., J. Bacteriol. 169:4171-4176 (1987)) have also been sequenced. Further suitable amyioglucosidases for the purpose of the present invention are the amyioglucosidases described in WO92/00381 , WO99/28448 and WO00/4136. WO92/00381 describes glucoamylase including at least one mutation substituting an amino acid chosen by comparison with the structurally related regions of other enzymes that exclusively hydrolyze only a-(1®4)-glucosidic bonds, with increased selectivity of the enzymes for a-(1®4)-glucosidic bonds. More specifically, the mutation of the amino acids were made at positions corresponding to A. niger in Region 1 residues 109-122, Region 4 residues 172-184, and Region 6 residues 382-398 mutated to the amino acids of homologous position of the enzymes which selectively hydrolyze only a-(1®4)-glucosidic bonds. Specific mutations showing increased selectivity for maltose hydrolysis are made at positions 119, 182, 183 and 184. WO92/00381 further shows a significant increase in yield of glucose per unit amount of starch hydrolyzed by the mutated glucoamylase with Ala182 compared to the relative yield by the wild type glucoamylase with Asn182. This mutated glucoamylase with Ala182 provides a significantly higher maltose/isomaltose selectivity (selectivity for a-(1®4) glucosidic bond hydrolysis as compared to a-(1®6) glucosidic bond hydrolysis ) while having only a small decrease in activity. Moreover, isomaltose formation from 30% glucose by the mutated Asn182®Ala glucoamylase was only 20% that of wild-type glucoamylase, as measured by NMR demonstrated Asn182®Ala to reduce the initial rate by 80% compared to wild-type enzyme. After 33-1/3 hours of incubation, the isomaltose content reached in the presence of mutant enzyme was estimated to be approximately one third of that reached in the presence of the equivalent amount of wild-type enzyme. Further, a statistically significant increase in glucose yield is produced by the mutated glucoamylase Asn182®Ala compared to wild-type glucoamylase. WO99/28448 describes a novel thermostable glucoamylase. More specifically WO99/28448 describes a thermostable glucoamylase from a strain of Talaromyces emersonii now deposited with the Centraalbureau voor Schimmelcultures under the number CBS 793.97. The isolated glucoamylase has a very high thermal stability in comparison to prior art glucoamylases, such as the Aspergillus niger glucoamylase (available from Novo Nordisk A/S under the trade name AMG). The VA (half-life) was determined to be about 120 minutes at 70°C (pH 4.5) as described in Example 2 of W099/28448. The VA of the recombinant T. emersonii AMG expressed in yeast was determined to be about 110 minutes as described in Example 12 of W099/28448. Therefore, WO99/28448 relates to an isolated enzyme with glucoamylase activity having a T-ι 2 (half-life) of at least 100 minutes in 50 mM NaOAc, 0.2 AGU/ml, pH 4.5, at 70°C. In the second aspect WO99/28448 relates to an enzyme with glucoamylase activity comprising one or more of the partial sequences shown in SEQ ID Nos. 1-6 as shown in WO99/28448 or the full length enzyme shown in SEQ ID NO: 7 of WO99/28448 or an enzyme with glucoamylase activity being substantially homologous thereto. WOOO/04136 describes glucoamylase variants with improved thermostablility and/or increased specific activity. Glucoamylase variants with improved thermostability are variants having a higher T 1 2 (half-time) than the corresponding parent glucoamylase, as described in the "Materials & Methods" section of WOOO/04136. Glucoamylase variants with increased specific activity are variants having increased specific activity towards the α-1 ,4 linkages in the saccharide in question. The specific activity is determined as kcat or AGU/mg (measured as described in the "Materials & Methods" section of WOOO/04136). An increased specific activity means that the k cat or AGU/mg values are higher when compared to the k^ t or AGU/mg values, respectively, of the corresponding parent glucoamylase. WOOO/04136 provides a number of improved variants of a parent glucoamylase with improved thermostability and/or increased specific activity in comparison to the parent corresponding enzyme. The improved thermal stability is obtained by substituting selected positions in a parent glucoamylase. In particular, WOOO/04136 describes a variant of a parent glucoamylase comprising one or more mutation(s) in the following position(s) or region(s) in the amino acid sequence shown in NO: 2 of WOOO/04136: Region: 1-18, Region: 19- 35, Region: 40-62, Region: 73-80, Region: 93-127, Region: 170-184, Region: 200- 212, Region: 234-246, Region: 287-319, Region: 334-341 , Region: 353-374, Region: 388-414, Region: 445-470, and/or in a corresponding position or region in a homologous glucoamylase which displays at least 60% homology with the amino acid sequences shown in SEQ ID NO: 2 of WOOO/04136. WOOO/04136 also describes the variant of a parent glucoamylase with improved thermostability comprising one or more mutation(s) in the following position(s) or region(s) in the amino acid sequence shown in NO: 2 of WOOO/04136: Region: 1- 18, Region: 19-35, Region: 73-80, Region: 93-127, Region: 170-184, Region: 200- 212, Region: 234-246, Region: 287-319, Region: 334-341 , Region: 353-374, Region: 388-414., Region: 445-470, and/or in a corresponding position or region in a homologous glucoamylase which displays at least 60% homology with the amino acid sequences shown in SEQ ID NO: 2 of WOOO/04136. WOOO/04136 also describes the variant of a parent glucoamylase with increased specific activity comprising one or more mutation(s) in the following position(s) or region(s) in the amino acid sequence shown in NO: 2 of WOOO/04136: Region: 1- 18, Region: 40-62, Region: 93-127, Region: 170-184, Region: 200-212, Region: 234-246, Region: 287-319, Region: 388-414, and/or in a corresponding position or region in a homologous glucoamylase which displays at least 60% homology with the amino acid sequences shown in SEQ ID NO: 2 of WOOO/04136. Commercially available amyioglucosidases are the enzyme products sold under the trademane PALKODEX by MAPS; AMG300L by Novo Nordisk A/S, Optimax 7525 (Combinations of enzymes including amyloglucosidase) and Spezyme by Genencor. Further commercial available amyioglucosidases are those from Aspergillus niger obtainable from the following companies: Ambazyme, Amano, Boehringer, Fluka, Sigma, Aldomax, Genzyme, Nagase, UOP. Also suitable are the amyioglucosidases from Aspergillus species from the companies Biocatalysts or Danisco and the amyioglucosidases from Rhizopus delemar from Nagase; from Rhizopus niveus from Amano, ICN, Seikagaku; from Rhizopus oryzae from Enzyme Development Co-operation. Preferred amyioglucosidases for specific applications are alkaline amyioglucosidases, i.e. enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of their maximum activity at a pH ranging from 7 to 12, preferably 10.5. More preferred amyioglucosidases are enzymes having their maximum activity at a pH ranging from 7 to 12, preferably 10.5. In another embodiment of the present invention, the detergent compositions of the present invention might further comprise one or more starch-binding domain. Such starch binding domain might be added in the detergent compositions of the present invention, as such, or might be part of a chimeric amyloglucosidase hybrid. Indeed, the amyioglucosidases of the present inventions will preferably have or will be added a Starch Binding Domain (SBD). In general enzymes such as amylases, cellulases and xylanases have a modular structure consiting of a catalyst domain and at least one non-catalytic domain whose function is generally described as that of a polysaccharide-binding domain (PBD), starch- binding domain (SBD), cellulose-binding domain (CBD) and xylan-binding domain. The function of these binding domains is to bind selectively to the substrate of the enzyme, and in particular, the primary function of SBD is to bind to starch. It has been found surprisingly found that the detergent compositions of the present invention comprising one ore more SBD and/or wherein the amyioglucosidases comprise such a SBD will provide a more effective starch- containing soils/stains removal. It has further been found that such enzymes can be formulated in a more cost-effective manner. Without wishing to be bound by theory, it is beleived that such amyioglucosidases will be more effectively directed specifically to their substrate from the wash solutions and so have improved deposition onto the starch containing stains/soils for improved and/or new performance. Moreover, it is believed that the binding of the SBD will disurpt the surface of starch resulting in a higher hydrolytic rate. Suitable SBD for use in the present invention are the SBDs comprised in the glucoamylase from Aspergillus niger ( Sigma) and in the β-galactosidase from A. awamori. The recovery and fusion of SBDs can be achieved as described in Ford, C. et al., J. Cell. Biochem. (Suppl.) 14D:30 (1990) and in Chen, L. et al., Abst. Annu. Meet. Am. Soc. Microbiol. 90:269 (1990). The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / genetic engineering techniques in order to optimise their performance efficiency in the detergent compositions of the invention. For example, the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that the optimal pH, bleach or chelant stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular cleaning application. In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface charges for the surfactant compatibility. The isoelectric point of such enzymes may be modified by the substitution of some charged amino acids, e.g. an increase in isoelectric point may help to improve compatibility with anionic surfactants. The stability of the enzymes may be further enhanced by the creation of e.g. additional salt bridges and enforcing metal binding sites to increase chelant stability. Detergent components The detergent compositions of the invention must contain at least one additional detergent component. The precise nature of these additional component, and levels of incorporation thereof will depend on the physical form of the composition, and the nature of the cleaning operation for which it is to be used. The detergent compositions of the present invention will preferably comprise a further enzyme selected from a protease, a lipase or an enzyme of the amylase class - especially an α-amylase, a neopullulanase, a pullulanase type II, a dextrin dextranase, a cyclomaltodextrin glucanotransferase, a maltogenic alpha-amylase and/or a starch debranching enzyme, i.e. a pullulanase type I, isopullulanase and/or isoamylase; a bleaching agent and/or a nonionic surfactant. In a preferred embodiment, the present invention relates to a laundry and/or fabric care composition comprising an amyloglucosidase (Examples 1-16). In a second embodiment, the present invention relates to dishwashing or household cleaning compositions (Examples 17-23). The compositions of the invention may for example, be formulated as hand and machine dishwashing compositions, hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in general household hard surface cleaning operations. When formulated as compositions for use in manual dishwashing methods the compositions of the invention preferably contain a surfactant and preferably other detergent compounds selected from organic polymeric compounds, suds enhancing agents, group II metal ions, solvents, hydrotropes and additional enzymes. When formulated as compositions suitable for use in a laundry machine washing method, the compositions of the invention preferably contain both a surfactant and a builder compound and additionally one or more detergent components preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap dispersants, soil suspension and anti-redeposition agents and corrosion inhibitors. Laundry compositions can also contain softening agents, as additional detergent components. Such compositions containing an amyloglucosidase provide starch- containing stain removal, whiteness maintenance and dingy cleaning when formulated as laundry detergent compositions. The compositions of the invention can also be used as detergent additive products. Such additive products are intended to supplement or boost the performance of conventional detergent compositions. The detergent compositions according to the invention can be liquid, paste, gels, bars, tablets, spray, foam, powder or granular. Granular compositions can also be in "compact" form and the liquid compositions can also be in a "concentrated" form. If needed the density of the laundry detergent compositions herein ranges from 400 to 1200 g/litre, preferably 500 to 950 g/litre of composition measured at 20°C. The "compact" form of the compositions herein is best reflected by density and, in terms of composition, by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition. In the compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, most preferably not exceeding 5% by weight of the composition. The inorganic filler salts, such as meant in the present compositions are selected from the alkali and alkaline-earth-metal salts of sulphates and chlorides. A preferred filler salt is sodium sulphate. Liquid detergent compositions according to the present invention can also be in a "concentrated form", in such case, the liquid detergent compositions according 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 preferably less than 40%, more preferably less than 30%, most preferably less than 20% by weight of the detergent composition. Suitable detergent compounds for use herein are selected from the group consisting of the below described compounds. Surfactant system The detergent compositions according to the present invention generally comprise a surfactant system wherein the surfactant can be selected from nonionic and/or anionic and/or cationic and/or amphoiytic and/or zwitterionic and/or semi-polar surfactants. Preferably, the detergent compositions of the present invention will comprise a nonionic surfactant, preferably a nonionic surfactant based upon polyoxyethylene condensates with alcohols, indeed, it has been surprisingly found that the detergent compositions of the present invention further comprising a nonionic surfactant provide improved removal of starch from fabrics, dishware and other hard surfaces. Without wishing to be bound by theory, it is believed that the nonionic surfactant adsorbs onto the granular surface of the starch thereby disrupting the starch structure and influencing and preventing the retrogradation process of the starch. Such disruption of the structure increases the enzyme accessibility to its substrate. Moreover, nonionic surfactants can be used also in a pre-treatment process and therefore can reduce the retrogradation process of starch. Hence, the starch-containing stains / soils is more easily hydrolysed by the enzyme and a synergistic breakdown of the starch soil by the amyloglucosidase and the non-ionic surfactant occurs. The surfactant is typically present at a level of from 0.1 % to 60% by weight. More preferred levels of incorporation are 1 % to 35% by weight, most preferably from 1% to 30% by weight of detergent compositions in accord with the invention. The surfactant is preferably formulated to be compatible with enzyme components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated such that it promotes, or at least does not degrade, the stability of any enzyme in these compositions. Nonionic surfactants: Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being preferred. These compounds include the condensation products of alkyl phenols 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™ χ_45 τ χ. 14, χ_ιoo and X-102, all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkyl phenol ethoxylates). The condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide are suitable 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 present in said condensation products. Examples of commercially available nonionic surfactants of this type include TergitolT 15-S-9 (the condensation product of C « | -|-C-| 5 linear alcohol with 9 moles ethylene oxide), TergitolT 24-L-6 NMW (the condensation product of C-12- 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 C14-C15 linear alcohol with 9 moles of ethylene oxide), Neodol™ 23-3 (the condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide), Neodof " M 45-7 (the condensation product of C14-C15 linear alcohol with 7 moles of ethylene oxide), Neodol^ 45.5 (the condensation product of C-14-C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company, Kyro™ EOB (the condensation product of C13-C15 alcohol with 9 moles ethylene oxide), marketed by The Procter & Gamble Company, and Genapol LA 030 or 050 (the condensation product of C12- 4 alcohol with 3 or 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. Also useful as the nonionic surfactant of the surfactant systems of the present invention are the alkyipolysaccharides disclosed in U.S. Patent 4,565,647, Llenado, issued January 21 , 1986, having a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group 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. The preferred alkylpolyglycosides have the formula R2θ(C n H 2n O)t(glycosyl) > wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x is 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. 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 predominately the 2-position. 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 of 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 polyoxyethyiene 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 PlurafacT LF404 and Pluronic™ surfactants, marketed by BASF. Other suitable nonionic surfactants 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 generally 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 polyoxyethyiene 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 nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides, and mixtures thereof. Most preferred are C8-C14 alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and Cs-C-is alcohol ethoxylates (preferably C-|rj avg.) having from 2 to 10 ethoxy groups, and mixtures thereof. Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula. R2 - C - N - Z, II I O R 1 wherein R 1 is H, or R 1 is C^_4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R2 is C5.31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof. Preferably, R 1 is methyl, R 2 is a straight C- j 1_15 alkyl or C16-I8 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction. Anionic surfactants: Suitable anionic surfactants to be used are linear alkyl benzene suifonate, alkyl ester sulfonate surfactants including linear esters of Cβ- C20 carboxylic acids (i.e., fatty acids) which are sulfonated with gaseous SO3 according to "The Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329. Suitable starting materials would include natural fatty substances as derived from tallow, palm oil, etc. The preferred alkyl ester sulfonate surfactant, especially for laundry applications, comprise alkyl ester sulfonate surfactants of the structural formula: O || R3 - CH - C - OR 4 SO3M wherein R3 is a C8-C20 hydrocarbyl, preferably an alkyl, or combination thereof, R 4 is a C1-C6 hydrocarbyl, preferably an alkyl, or combination thereof, and M is a cation which forms a water soluble salt with the alkyl ester sulfonate. Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethanolamine, and triethanolamine. Preferably, R3 is C10- 16 alkyl, and R 4 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonates wherein R 3 is C10- 16 alkyl. Other suitable anionic surfactants include the alkyl sulfate surfactants which are water soluble salts or acids of the formula ROSO3M wherein R preferably is a C-10-C24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C10- 20 alkyl component, more preferably a C12- 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 ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like). Typically, alkyl chains of C12- 16 are preferred for lower wash temperatures (e.g. below about 50°C) and C-|6-18 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 detergent compositions of the present invention. These can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di- and triethanolamine salts) of soap, C8-C22 primary of secondary alkanesulfonates, C8-C24 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, C8-C-24 alkylpolyglycolethersulfates (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 succinamates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C-12-C18 monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated Cg-Ci2 diesters), acyl sarcosinates, sulfates of alkylpoiysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsulfated compounds being described below), branched primary alkyl sulfates, and alkyl polyethoxy carboxyiates such as those of the formula RO(CH2CH2θ)|<-CH2COO-M+ wherein R is a C8-C22 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. Further examples are described in "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perry and Berch). A variety of such surfactants are also generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975 to Laughlin, et al. at Column 23, line 58 through Column 29, line 23 (herein incorporated by reference). When included therein, the laundry detergent compositions of the present invention typically comprise from about 1% to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants. Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants hereof are water soluble salts or acids of the formula RO(A) m S03M wherein R is an unsubstituted C-10-C24 alkyl or hydroxyalkyl group having a C10- 24 alkyl component, preferably a C-12- 20 alkyl or hydroxyalkyl, more preferably C12- C<| 8 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 substituted-ammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples 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 surfactants are C-12-C18 alkyl polyethoxylate (1.0) sulfate (C-|2- i8E( -0)M), C-12-C18 alkyl polyethoxylate (2.25) sulfate (C-| 2-Ci 8E(2.25)M), C12-C18 alkyl polyethoxylate (3.0) sulfate (C-|2-Ci8E(3.0)M), and C12-C18 alkyl polyethoxylate (4.0) sulfate (Ci2-C-| 8E(4.0)M), wherein M is conveniently selected from sodium and potassium. The 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 surfactants: Cationic surfactants suitable for use in the 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 alkyltrimethylammonium halogenides, and those surfactants having the formula : [R2(OR 3 )y][R 4 (OR3) y ] 2 R 5 N+X- wherein R2 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 from the group consisting of -CH 2 CH 2 -, -CH 2 CH(CH 3 )- T -CH2CH(CH 2 OH)-, -CH 2 CH2CH 2 -, and mixtures thereof; each R 4 is selected from the group consisting of C1 -C4 alkyl, C1-C4 hydroxyalkyl, benzyl ring structures formed by joining the two R 4 groups, - CH2CHOH-CHOHCOR 6 CHOHCH2θH 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 of 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. Quaternary ammonium surfactant suitable for the present invention has the formula (I): Formula I whereby R1 is a short chainiength alkyl (C6-C10) or alkylamidoalkyl of the formula (II) : Formula II y is 2-4, preferably 3. whereby R2 is H or a C1-C3 alkyl, whereby x is 0-4, preferably 0-2, most preferably 0, whereby R3, R4 and R5 are either the same or different and can be either a short chain alkyl (C1-C3) or alkoxylated alkyl of the formula III, whereby X- is a counterion, preferably a halide, e.g. chloride or methylsulfate. R6 is C < |-C4 and z is 1 or 2. Preferred quat ammonium surfactants are those as defined in formula I whereby R-| is C8, C-)o ° r mixtures thereof, x=o, R3, R4 = CH3 and R5 = CH2CH2OH. Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition having the formula: R 1 R 2 R3R4N + X " (i) wherein R-| is C8-C-| 6 alkyl, each of R2, R3 and R4 is independently C1 -C4 alkyl, C-1-C4 hydroxy alkyl, benzyl, and -(C2H4o) x H where x has a value from 2 to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl. The preferred alkyl chain length for R-j is C12- 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 OXO alcohols synthesis. Preferred groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosulphate, 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 di hydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; C-12-15 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 CH2-CH2-O-C-C12-I4 alkyl and R2R3R4 are methyl). II o di-alkyl imidazolines [compounds of formula (i)]. Other cationic surfactants useful herein are also described in U.S. Patent 4,228,044, Cambre, issued October 14, 1980 and in European Patent Application EP 000,224. Typical cationic fabric softening components include the water-insoluble quaternary-ammonium fabric softening actives or thei corresponding amine precursor, the most commonly used having been di-long alkyl chain ammonium chloride or methyl sulfate. Preferred cationic softeners among these include the following: 1 ) ditallow dimethylammonium chloride (DTDMAC); 2) dihydrogenated tallow dimethylammonium chloride; 3) dihydrogenated tallow dimethylammonium methylsulfate; 4) distearyl dimethylammonium chloride; 5) dioleyl dimethylammonium chloride; 6) dipalmityl hydroxyethyl methylammonium chloride; 7) stearyl benzyl dimethylammonium chloride; 8) tallow trimethylammonium chloride; 9) hydrogenated tallow trimethylammonium chloride; 10) C-|2 _ 14 alkyl hydroxyethyl dimethylammonium chloride; 1 1 ) C-J 2-18 a'kyl di hydroxyethyl methylammonium chloride; 12) di(stearoyioxyethyl) dimethylammonium chloride (DSOEDMAC); 13) di(tallow-oxy-ethyl) dimethylammonium chloride; 14) ditallow imidazolinium methylsulfate; 15) 1-(2-tallowylamidoethyl)-2-tallowyl imidazolinium methylsulfate. Biodegradable quaternary ammonium compounds have been presented as alternatives to the traditionally used di-long alkyl chain ammonium chlorides and methyl sulfates. Such quaternary ammonium compounds contain long chain alk(en)yl groups interrupted by functional groups such as carboxy groups. Said materials and fabric softening compositions containing them are disclosed in numerous publications such as EP-A-0,040,562, and EP-A-0,239,910. The quaternary ammonium compounds and amine precursors herein have the formula (I) or (II), below: (i) o wherein Q is selected from -O-C(O)-, -C(0)-0-, -0-C(0)-0-, -NR 4 -C(0)-, -C(O)- NR 4 -; R1 is (CH 2 ) n -Q-T 2 or T 3 ; R2 is (CH 2 )m-Q-T 4 or T5 or R 3 ; R 3 is C1-C4 alkyl or C-1-C4 hydroxyalkyl or H; R 4 is H or C1-C4 alkyl or C1-C4 hydroxyalkyl; T " ! , T 2 , T 3 , T 4 , T 5 are independently C11-C22 alkyl or alkenyl; n and m are integers from 1 to 4; and X * is a softener-compatible anion. Non-limiting examples of softener-compatible anions include chloride or methyl sulfate. The alkyl, or alkenyl, chain T 1 , τ2, T 3 , T 4 , T^ must contain at least 11 carbon atoms, preferably at least 16 carbon atoms. The chain may be straight or branched. Tallow is a convenient and inexpensive source of long chain alkyl and alkenyl material. The compounds wherein Tl , T2, T 3 , T 4 , T^ represents the mixture of long chain materials typical for tallow are particularly preferred. Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening compositions herein include: 1 ) N,N-di(tallowyl-oxy-ethyl)-N,N-dimethyl ammonium chloride; 2) N,N-di(tallowyl-oxy-ethyl)-N-methyl, N-(2-hydroxyethyl) ammonium methyl sulfate; 3) N,N-di(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl ammonium chloride; 4) N,N-di(2-tailowyl-oxy-ethylcarbonyl-oxy-ethyl)-N,N-dimethyl ammonium chloride; 5) N-(2-tallowyl-oxy-2-ethyl)-N-(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl ammonium chloride; 6) N,N,N-tri(tallowyi-oxy-ethyl)-N-methyl ammonium chloride; 7) N-(2-tallowyl-oxy-2-oxo-ethyl)-N-(tallowyl-N,N-dimethyl-ammonium chloride; and 8) 1 ,2-ditallowyl-oxy-3-trimethylammoniopropane chloride; and mixtures of any of the above materials. When included therein, the 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: Ampholytic surfactants are also suitable for use in the 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 water-solubilizing group, e.g. carboxy, sulfonate, sulfate. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, lines 18-35, for examples of ampholytic surfactants. When included therein, the 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: Zwitterionic surfactants are also suitable for use in 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 U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, line 38 through column 22, line 48, for examples of zwitterionic surfactants. When included therein, the 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: 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; water-soluble 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 of 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 0 R 3 (OR 4 )xN(R5)2 wherein R 3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof containing from about 8 to about 22 carbon atoms; 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^ 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 R5 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-ιo-C-|8 alkyl dimethyl amine oxides and C8-C12 alkoxy ethyl dihydroxy ethyl amine oxides. When included therein, the cleaning 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. Co-surfactants: The detergent composition of the present invention may further comprise a cosurfactant selected from the group of primary or tertiary amines. Suitable primary amines for use herein include amines according to the formula R1 NH2 wherein R < | is a C5-C12 . preferably CQ-C^ Q alkyl chain or R4X(CH2)n- is -0-,-C(0)NH- or -NH- t R4 is a C6-C12 alkyl chain n is between 1 to 5, preferably 3. R<| alkyl chains may be straight or branched and may be interrupted with up to 12, preferably less than 5 ethylene oxide moieties. Preferred amines according to the formula herein above are n-alkyl amines. Suitable amines for use herein may be selected from 1-hexylamine, 1- octylamine, 1-decylamine and laurylamine. Other preferred primary amines include C8-C10 oxypropylamine, octyloxypropylamine, 2-ethylhexyl- oxypropylamine, lauryl amido propylamine and amido propylamine. Suitable tertiary amines for use herein include tertiary amines having the formula R1 R2 3N wherein R1 and R2 are C-j-Cs alkylchains or τ s — ( c H 2 — CH θ )χH R3 is either a C6-C-12, preferably C-6-C10 alkyl chain, or R3 is R4X(CH2) n . whereby X is -0-, -C(0)NH- or -NH- R4 is a C4-C12, n is between 1 to 5, preferably 2-3. R5 is H or C1-C2 alkyl and x is between 1 to 6 . R3 and R4 may be linear or branched; R3 alkyl chains may be interrupted with up to 12, preferably less than 5, ethylene oxide moieties. Preferred tertiary amines are R1 R2R3N where R1 is a C6-C12 alkyl chain, R2 and R3 are C1-C3 alkyl or τ s — ( CH 2 — CH θ )χH where R5 is H or CH3 and x = 1-2. Also preferred are the amidoamines of the formula: o II Ri — C— NH — ( CH 2 )— N— ( R 2 ) n 2 wherein Ri is C6-C12 alkyl; n is 2-4, preferably n is 3; R2 and R3 is C1-C4 Most preferred amines of the present invention include 1-octylamine, 1- hexylamine, 1-decylamine, 1-dodecylamine,C8-10oxypropylamine, N coco 1- 3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles propoxylated, octyl amine 2 moles propoxylated, lauryl amidopropyldimethylamine, C8-10 amidopropyldimethylamine and C10 amidopropyldimethylamine. The most preferred amines for use in the compositions herein are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n- dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7 times ethoxylated, lauryl amido propylamine and cocoamido propylamine. Conventional detergent enzymes The detergent compositions of the present invention can comprise in addition to the amyloglucosidase, one or more enzymes which provide cleaning performance, fabric care and/or sanitisation benefits. Said enzymes include enzymes selected from cellulases, hemicellulases, peroxidases, proteases, gluco-amylases, amylases, mannanases, xyloglucanases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, β-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase or mixtures thereof. Preferably, the detergent compositions of the present invention will comprise an enzyme selected from an enzyme from the amylase class, a protease and/or a lipase. Such "enzyme of the amylase class" encompassed α-amylases, neopullulanases, pullulanases type II, dextrin dextranases, cyclomaltodextrin glucanotransferases, maltogenic alpha-amylase and/or a starch debranching enzymes. Suitable starch debranching enzymes are the pullulanase type I, isopullulanase and/or isoamylase enzymes. Indeed, it has been found that the combination of an amyloglucosidase with an enzyme from the amylase class within the detergent compositions of the present invention, provides a synergistic removal of retrograded starch. Hence, the detergent compositions comprising such combination of enzyme provide enhanced removal of starch-containing stains and soils and when formulated as a laundry detergent composition, enhanced whiteness maintenance and dingy cleaning. More preferably, the detergent compositions of the present invention will comprise further a pullulanase type II, an α-amylase, a maltogenic alpha- amylase and/or a starch debranching enzyme. Even more preferred for the purpose of the present invention are the combinations of the amyloglucosidase enzyme of the present invention with an α-amylase and a starch debranching enzyme. It has been found that such ternary enzymatic system provide an excellent synergistic removal of retrograded starch. Therefore, the detergent compositions with such enzyme systems provide excellent removal of starch- containing stains and soils and when formulated as a laundry detergent composition, excellent whiteness maintenance and dingy cleaning. Furthermore, the stains most commonly encountered in laundry, dishwashing and hard surface cleaning, generally comprise a significant amount of proteins and triglyceride compounds. In particular, it has been found that starch materials are usually associated with lipid compounds. Therefore, the detergent compositions will preferably comprise a protease and/or lipase enzyme in order to enhance the removal of such complex stains. Alpha-amylase As indicated above, the detergent compositions of the present invention will preferably comprise an α-amylase. Suitable α-amylases for the purpose of the present invention are described in the following : WO94/02597, Novo Nordisk A/S published February 03, 1994, describes cleaning compositions which incorporate mutant amylases. See also WO95/10603, Novo Nordisk A/S, published April 20, 1995. Other amylases known for use in cleaning compositions include both α- and β-amylases. α-Amylases are known in the art and include those disclosed in US Pat. no. 5,003,257; EP 252,666; WO91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341 ; and British Patent specification no. 1 ,296,839 (Novo). Other suitable amylases are stability- enhanced amylases described in W094/18314, published August 18, 1994 and WO96/05295, Genencor, published February 22, 1996 and amylase variants having additional modification in the immediate parent available from Novo Nordisk A/S, disclosed in WO95/10603, published April 95. Also suitable are amylases described in EP 277 216, W095/26397 and W096/23873 (all by Novo Nordisk). Examples of commercial α-amylases products are Purafect Ox Am® from Genencor and Termamyl®, Ban® ,Fungamyl® and Duramyl®, all available from Novo Nordisk A/S Denmark. W095/26397 describes other suitable amylases: α-amylases characterised by having a specific activity at least 25% higher than the specific activity of Termamyl® at a temperature range of 25°C to 55°C and at a pH value in the range of 8 to 10, measured by the Phadebas® α- amyiase activity assay. Preferred are variants of the above enzymes, described in W096/23873 (Novo Nordisk). Preferably, the variants are those demonstrating improved thermal stability, more preferably those wherein at least one amino acid residue equivalent to F180, R181 , G182, T183, G184, or K185 has been deleted from the parent α-amylase. Particularly preferred are those variants having improved thermal stability which comprise the amino acid deletions R181 + G182 * or T183 * + G184 * . Other amylolytic enzymes with improved properties with respect to the activity level and the combination of thermal stability and a higher activity level are described in W095/35382. Further suitable amylases are the H mutant α-amylase enzymes exhibiting improved stability described in WO98/26078 by Genencor. The amylolytic enzymes are incorporated in the detergent compositions of the present invention a level of from 0.0001 % to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition. Starch debranching enzymes Starch debranching enzymes to be used in the composition of the invention, can be obtained from various sources. Generally, however, it is derived from microorganisms. Preferred species of the starch debranching enzyme are pullulanase type I, isopullulanase and isoamylase. These enzymes are commercially obtainable and examples thereof include SPLENTASE ® (manufactured by Amano Pharmaceuticla Co., Ltd.) and PROMOZYME ® 200L (manufactured by Novo Industri A/S), as for pullulanase; and "isoamylase" (reagent, manufactured by Seikagaku Kogyo Co., Ltd.), as for isoamylase. Such starch debranching enzymes are supplied generally in the form of granules and have an enzymatic activity of about 10 5 to 10 8 units per liter. The starch debranching enzyme is generally comprised in the detergent composition of the invention in an amount of 0.0001 % to 10% by weight, preferably 0.001 % to 0.5% by weight. Pullulanase type I enzymes are classified under the IUPAC classification EC 3.2.1.41 and the systematic name α-Dextrin 6-glucanohydrolase. Pullulanase enzymes hydrolyses the 1 ,6-α-D-glucosidic linkages in pullulan, amylopectin and glycogens and in the α- and β-amylase limit dextrins of amylopectin and glycogen as well as against branched oligosaccharides produced by their partial decomposition. Because of this characteristic, pullulanase is called a "debranching enzyme". Indeed, pullulanase is an enzyme which breaks only α- 1 ,6-glycosidic linkage of puliulan and finally produces maltotriose. Microbial sources include Aerobacter Aerogenes, Pseudomonas stutzeri, Bacillus polymyxa, B.maceranas, Klebsiella pneumonia and Streptomyces sp. The activity of this enzyme is standardised at 200 PUN/g (Pullulanase Unit Novo). 1 UPN is defined as the amount of enzyme which under standard conditions hydrolyses puliulan liberating reduced carbohydrate, with a reducing power equivalent to 1μ- mole glucose per minute. Also preferred is pullulanase isolated from a strain of Bacillus No. 202-1 as described in Biochimica et Biophysica Acta, 397 (1985) 188-193. This pullulanase has an optimum pH of about 8.55-9.0, and is therefore of particular interest in more alkaline detergent compositions. Pullulanase was first discovered from a strain belonging to Aerobacter aerogenes by Bender and Wallenfels in 1961 [Biochem. Z., 334, 79, (1961 )]. Recently, various microorganisms capable of producing pullulanase have been reported. These microorganisms are, for example, Bacillus sp. [J. Jpn. Soc. Starch Sci., 30, 200, (1983)]; Bacillus acidopullulyticus [Agric. Biol. Chem., 52, 2293, (1984)]; Bacillus stearothermophilus [Eur. J. Appl. Microbiol. Biotechnol., 17, 24, (1983)]; Streptococcus mitis - [Biochem, J., 108, 33, (1968)]; Lactobacillus [Denpun Kagaku, 28, 72 (1981 )]; Clostπdium sp. [Appl., Environ. Microb., 53, 7 (1987)]; Clostπdium thermohydrosulfuricum [Appl. Environ. Microb., 49, 5, (1985), J. Bacteriol., 164, 3, (1985), Biochem. J., 246, (1987)], Thermus aquaticus [Enzyme Microb. Technol., 8, (1986)]; Thermus sp. [J. Jpn. Soc. Starch Sci., 34, 1 , (1987)] and Clostπdium thermosulfurogenes [Appl. Microb. Biotechnol., 33, 511 , (1990)].. Furthermore, two publications have reported a method of producing alkaline or alkalin-resistant pullulanases: Horikoshi et al. cultured an alkalophilic strain of the genus Bacillus (Bacillus sp. 202-1 ) and produced alkaline pullulanase (Japanese Patent Publication (Kokoku) No. 277786/1978); and the alkaline pullulanase from Bacillus sp. KSM-AP 1876 described in W094/19468 (Japanese Patent Application Laid-open (Kokai) No. 87176/1991 ). Relevant pullulanase include for example, pullulanases obtainable from Bacillus species (e.g. B. acidopullulyticus as described in EP 063 909, such as PromozymeTM from Novo Nordisk A/S.) Further pullulanase suitable for the detergent compositions of the present invention is the alkaline pullulanase described in EP 450 627 by the Kao Corporation, which has an optimum pH in the alkaline range and is stable against surfactants. Such alkaline pullulanase includes an alkaline pullulanase A and an alkaline pullulanase B, both suitable for the purpose of the present invention. Another alkaline pullulanase suitable for detergents is described in W094/19468 by the Kao Corporation. Also suitable are the pullulanase enzymes described in the following Japanese patent/applications: JP04073298 which is directed to an automiatic dishwashing detergent composition comprising a nonionic surfactant, a calcium chelating agent, a lipase and an alkali pullulanase for high detergency, JP06264094 which describes a laundry detergent compsoition comprising soaps, surfactants and alkali-resistant pullulanase having high detergency; all by the Kao Corporation. Particularly preferred is the Pullulanase Promozyme (Trade Mark of Novo), isolated from Bacillus sp. Pullulanase. Isopullulanase enzymes are classified under the IUPAC classification EC 3.2.1.57 and the systematic name Puliulan 4-glucanohydrolase. The isopullulanase enzymes hydrolyse puliulan to isopanose (6-α-maltosylglucose). Isoamylase enzymes : Isoamylases have the ability to debranch glycogen. The enzymes have been detected in a variety of microorganisms including B. amyloliquefacines, Cytophaga sp., P. amyloderamosa and Streptomyces sp. No.28. The activity of the enzyme is given in MU (maltose units). 1MU is defined as the amount of enzyme which under standard conditions hydrolyses isoamylose liberating reduced carbohydrate, with a reducing power equivalent to 1μ-mole maltose per minute. Isoamylases are classified under the IUPAC classification EC 3.2.1.68 and the systematic name glycogen 6-glucanohydrolase. The isoamylase enzymes hydrolyse the 1 ,6-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins. The isoamylases are distinguished from the pullulanase enzyme by their inability to attack puliulan, by limited action on α-limit dextrins and by their complete action on glycogen. Relevant isoamylases include for example isoamylases obtainable from Pseudomonas species (e.g. Pseudomonas sp. SMP1 or Pseudomonas amyloderomosa SB15), Bacillus species (e.g. B. amyloliquefaciens), Flavobacteπum species or Cytophaga (Lysobacter) species. Isoamylase is commercially available from Sigma, ICN and Hayashibara. Also suitable are the pullulanase, isopullulanase and iso-amylases enzymes described as starch debranching enzymes in the following Japanese patent applications: JP07179900, JP06172796, JP06172792, JP04065494, JP02132193 and JP02132192, all by the Kao Corporation. Neopullulanase A further suitable enzyme from the amylase class for the purpose of the present invention are the neopullulanase enzymes. Neopullulanase enzymes are defined as enzymes that degrade puliulan to form panose and these are classified under the IUPAC classification EC 3.2.1.135. Neopullulanase enzyme, which is puliulan 4-D-glucanohydrolase, have an ability to cleave both 1 ,4- and 1 ,6- glucosidic bonds found in common starch and carbohydrate type stains or soils. For example, this enzyme hydrolyzes puliulan to panose (6-alpha-D- glucosyimaltose). Specifically, the neopullulanse enzyme can catalyze four types of reactions including the hydrolysis of alpha-(1 ->4)-glucosidic bond, the hydrolysis of alpha-(1 ->6)-glucosidic bond, the transglycosylation to form alpha- (1 - 4)-glucosidic bond, and the transglycosylation to form alpha-(1 - 6)-glucosidic bond. In contrast, other known enzymes catalyse only one of these reactions or it two reactions are catalysed, the second is weak. Also, the four types of reactions are catalyzed by the same mechanism. Neopullulanase enzymes are described in the following publications: Enzyme Chemistry and Molecular Biology of Amylases and Related Enzyme, pages 28-32 (1995), edited by the Amylases research Society of Japan; H. Takata, et al. J. Biol. Chem., volume 267, number 26, pages 15447-15452 (1992). Neopullulanase enzyme can be produced by the so called wild-type organism or by any host organism in which the gene responsible for the production of the neopullulanase, has been cloned and expressed. For example, the enzyme can be isolated from the culture supernatant of Bacillus stearothermophilus (B. stearothermophilus) TRS40 and purified to homogeneity using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Another enzyme having a molecular weight of 62,000 was cloned and expressed in Bacillus subtilis. This type of enzyme is fairly thermostable, particularly at an optimum temperature of from 60°C to 65°C at pH 6, and about 90% of the enzyme activity is retained. Bacteroides thetaiotaomicron 95-1 (B. thetaiotaomicron 95-1 ) is another type of enzyme, found in the human colon in high numbers. B. thetaiotaomicron 95-1 can ferment a wide variety of polysaccharides. Also suitable neopullulanase for use in the present invention is the new neopullulanase Y377F, S422V or M375L which is originated from Bacillus staerotermophilus as described in JP07177891 ; is the neopullulanase from B. subtilisis as described in JP06121681 ;is the neopullulanase from Bacillus stearothermophilus TRS (FERM9690), Thermoactinomyces vulgaris, Bacillus stearothermophilus KP1064, Bacteroides thetiaotaomicron 95-1 and others as described in JP05316992; is the variation-type neopullulanase described in JP04020291 and the neopullulanase described in JP02276578. The neopullulanase is generally comprised in the detergent composition of the invention in an amount of 0.0001 % to 10% by weight, preferably 0.001 % to 0.5% by weight. Pullulanase type II Pullulanase type II enzymes are defined as amylopullulanases and hydroiyzes randomly the α,1-4 linkages in addition to the branching points (α-1 ,6-linkages) in polysaccharides and dextrins, in contrast to pullulanase type I enzymes which only hydrolyse α,1-6 linkages in branched polysaccharides. The pullulanase type II can originate from extremophiles, especially extreme thermophiles and hyperthermophiles such as those isolated from Pyrococcus woesei, P. furiosus, Thermococcus litoralis, Thermococcus celer, Desulfurococcus mucosus, Bacteroides thetiaotaomicron, Staphylotherrmus marinus, Pyrodictium abysii, Bacillus stearothermophilus such as described in "A new Bacterial World", Extremophiles, 1997, 1 :2-13. Other suitable pullulanase for the purpose of the present invention is the alkaline pullulanase exhibiting alkaline α-amylase activity described in W096/35794. Also suitable is the alkaline pullulanase Y having an α-amylase activity as described in EP 418 835, having an optimum pH at higher alkaline range than conventional alkaline pullulanases and exhibiting excellent pH stability in a wide pH range and strong resistance to almost all detergent ingredients such as surfactants, chelating agents and proteases. Also suitable is a combined enzyme of pullulanase-amylase produced by Bacillus subtilis TU (Agric. Biol. Chem., 51 , 9. (1987); Japanese Patent Publication No. 18717/1989) and the enzyme described in JP04072397 directed to an automatic dishwashing detergent compositions comprising a nonionic surfactant, a calcium capturing agent, a lipase, alkali and an alkali-resistant pullulanase having an α- amylase activity. The pullulanase type II is generally comprised in the detergent composition of the invention in an amount of 0.0001% to 10% by weight, preferably 0.001 % to 0.5% by weight. Dextrin dextranase A further suitable enzyme from the amylase class, is the dextrin dextranase. Dextrin dextranase (EC 2.4.1.2) is an enzyme that produces Dextran and low MW oligosaccharides from starch. Dextran dextrinase is reported to be found in Acetobacter capsulatus and A. viscosus. Dextrin dextranase is described in Enzyme Chemistry and Molecular Biology of Amylases and Related enzymes, edited by the Amylase Research Society of Japan, 1995 CRC Press. The dextrin dextranase is generally comprised in the detergent composition of the invention in an amount of 0.0001% to 10% by weight, preferably 0.001% to 0.5% by weight. Cyclomaltodextrin qlucanotransferase Also suitable is the cyclomaltodextrin glucanotransferase, EC 2.4.1.19, which is an enzyme that cyclizes part of a 1 ,4-α-D-glucan chain by formation of a 1 ,4-α-D- glucosidic bond and has the systematic name of 1 ,4-α-D-glucan 4-α-D-(1 ,4-α-D- glucano)-transferase (cyclizing). Commercially available cyclomaltodextrin glucanotransferase enzymes are sold under the tradenames CGTase by Amano; EN301 by Hayashibara and Toruzyme by Novo Nordisk A S. The cyclomaltodextrin glucanotransferase is generally comprised in the detergent composition of the invention in an amount of 0.0001% to 10% by weight, preferably 0.001 % to 0.5% by weight. Maltogenic alpha-amylase Also suitable is a maltogenic alpha amylase of the IUPAC Classification EC 3.2.1.133 that hydrolyses 1 ,4-α-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose units from the nonreducing ends of the chains. Suitable maltogenic alpha-amylases are the amylase cloned from Bacillus as described in EP 120 693 commercailly available under the tradename Novamyl from Novo Nordisk A/S; the variants of maltogenic alpha-amylase having CGT-ase activity and variants of CGT-ase having maltogenic alpha-amylase activity, as well as constructed hybrid enzymes described in W099/43793 and the maltogenic alpha-amylases variants with improved properties (altered physicochemical properties., e.g. an altered pH optimum, improved thermostability, increased specific activity, an altered cleavage pattern or an increased ability to reduce retrogradation of starch or staling of bread), based on the three-dimensional structure of the maltogenic alpha-amylase Novamyl described in W099/47394. Such maltogenic alpha-amylase is generally comprised in the detergent compositions of the present invention at a level of from 0.0002%-10%, preferably 0.001 %-2%, more preferably 0.001 %-1% pure enzyme by weight of the total detergent composition. As indicated above, the detergent compositions of the present invention will preferably further comprise a protease and/or a lipase enzyme. Suitable lipase enzymes include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1 ,372,034. Suitable lipases include those which show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano," hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. Especially suitable lipases are lipases such as M1 Lipase^ and LipomaxR (Gist-Brocades) and Lipolase^ and Lipolase UltraR(Novo) which have found to be very effective when used in combination with the compositions of the present invention. Also suitables are the lipolytic enzymes described in EP 258 068, WO92/05249 and W095/22615 by Novo Nordisk and in WO94/03578, W095/35381 and WO96/00292 by Unilever. Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special kind of lipase, namely lipases which do not require interfacial activation. Addition of cutinases to detergent compositions have been described in e.g. WO-A- 88/09367 (Genencor); WO90/09446 (Plant Genetic System) and W094/14963 and W094/14964 (Unilever). The lipases and/or cutinases are normally incorporated in the detergent composition at levels from 0.0001 % to 2% of pure enzyme by weight of the detergent composition. Suitable proteases are the subtilisins which are obtained from particular strains of B. subtilis and B. licheniformis (subtiiisin BPN and BPN'). One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASE® by Novo Industries A/S of Denmark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1 ,243,784 to Novo. Other suitable proteases include ALCALASE®, DURAZYM® and SAVINASE® from Novo and MAXATASE®. MAXACAL®, PROPERASE® and MAXAPEM® (protein engineered Maxacal) from Gist-Brocades. Also suitable for the present invention are proteases described in patent applications EP 251 446 and WO91/06637, protease BLAP® described in WO91/02792 and their variants described in W095/23221. See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO93/18140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO92/03529 A to Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO95/07791 to Procter & Gamble. A recombinant trypsin-like protease for detergents suitable herein is described in W094/25583 to Novo. Other suitable proteases are described in EP 516 200 by Unilever. Proteolytic enzymes also encompass modified bacterial serine proteases, such as those described in European Patent Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called "Protease A" herein. Suitable is what is called herein "Protease C", which is a variant of an alkaline serine protease from Bacillus in which lysine replaced arginine at position 27, tyrosine replaced valine at position 104, serine replaced asparagine at position 123, and alanine replaced threonine at position 274. Protease C is described in WO91/06637. Genetically modified variants, particularly of Protease C, are also included herein. A preferred protease referred to as "Protease D" is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a position in said carbonyl hydrolase equivalent to position +76, preferably also in combination with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +101 , +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274 according to the numbering of Bacillus amyloliquefaciens subtiiisin, as described in WO95/10591 and WO95/10592. The "protease D" variants have preferably the amino acid substitution set 76/103/104, more preferably the substitution set N76D/S103A/V104I. Also suitable is a carbonyl hydrolase variant of the protease described in WO95/10591 , having an amino acid sequence derived by replacement of a plurality of amino acid residues replaced in the precursor enzyme corresponding to position +210 in combination with one or more of the following residues: +33, +62, +67, +76, +100, +101 , +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, +218, and +222, where the numbered position corresponds to naturally- occurring subtiiisin from Bacillus amyloliquefaciens or to equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtiiisin (co-pending patent application published under W098/55634). More preferred proteases are multiply-substituted protease variants. These protease variants comprise a substitution of an amino acid residue with another naturally occuring amino acid residue at an amino acid residue position corresponding to position 103 of Bacillus amyloliquefaciens subtiiisin in combination with a substitution of an amino acid residue positions corresponding to positions 1 , 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21 , 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61 , 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 101 , 102, 104, 106, 107, 109, 11 1 , 114, 116, 1 17, 1 19, 121 , 123, 126, 128, 130, 131 , 133, 134, 137, 140, 141 , 142, 146, 147, 158, 159, 160, 166, 167, 170, 173, 174, 177, 181 , 182, 183, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206, 209, 210, 211 , 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251 , 252, 253, 254, 255, 256, 257, 258, 259, 260, 261 , 262, 263, 265, 268, 269, 270, 271 , 272, 274 and 275 of Bacillus amyloliquefaciens subtiiisin; wherein when said protease variant includes a substitution of amino acid residues at positions corresponding to positions 103 and 76, there is also a substitution of an amino acid residue at one or more amino acid residue positions other than amino acid residue positions corresponding to positions 27, 99, 101 , 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens subtiiisin and/or multiply-substituted protease variants comprising a substitution of an amino acid residue with another naturally occuring amino acid residue at one or more amino acid residue positions corresponding to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtiiisin as described in PCT application Nos. PCT/US98/22588, PCT/US98/22482 and PCT/US98/22486 all filed on October 23, 1998 from The Procter & Gamble Company. Preferred multiply substituted protease variants have te amino acid substitution set 101/103/104/159/232/236/245/248/252, more preferably 101 G/103A/1041/159D/232V/236H/245R/248D/252K according to the numbering of Bacillus amyloliquiefaciens subtiiisin. The protease enzymes are normally incorporated in the detergent composition at levels from 0.0001 % to 2% of pure enzyme by weight of the detergent composition. The cellulases usable in the present invention include both bacterial or fungal cellulases. Preferably, they will have a pH optimum of between 5 and 12 and a specific activity above 50 CEVU/mg (Cellulose Viscosity Unit). Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and WO96/02653 which discloses fungal cellulase produced respectively from Humicola insolens, Trichoderma, Thielavia and Sporotrichum. EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and W095/26398. Examples of such cellulases are cellulases produced by a strain of Humicola insolens (Humicola grisea var. thermoidea), particularly the Humicola strain DSM 1800. Other suitable cellulases are cellulases originated from Humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a " 43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. W091/17243. Also suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum described in WO94/21801 , Genencor, published September 29, 1994. Especially suitable cellulases are the cellulases having color care benefits. Examples of such cellulases are cellulases described in European patent application No. 91202879.2, filed November 6, 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A S) are especially useful. See also W091/17244 and WO91/21801. Other suitable cellulases for fabric care and/or cleaning properties are described in WO96/34092, W096/17994 and W095/24471. Said cellulases are normally incorporated in the detergent composition at levels from 0.0001 % to 2% of pure enzyme by weight of the detergent composition. Peroxidase enzymes are used in combination with oxygen sources, e.g. percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a phenolic substrate as bleach enhancing molecule. They are used for "solution bleaching", i.e. to prevent transfer of dyes or pigments removed from substrates during wash operations to other substrates in the wash solution. Peroxidase enzymes are known in the art, and include, for example, horseradish peroxidase, ligninase and haloperoxidase such as chloro- and bromo-peroxidase. Peroxidase-containing detergent compositions are disclosed, for example, in PCT International Application WO89/099813, WO89/09813 and in European Patent application EP No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme. Enhancers are generally comprised at a level of from 0.1% to 5% by weight of total composition. Preferred enhancers are substitued phenthiazine and phenoxasine 10-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4- carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10- methylphenoxazine (described in WO 94/12621 ) and substitued syringates (C3- C5 substitued alkyl syringates) and phenols. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide. Said peroxidases are normally incorporated in the detergent composition at levels from 0.0001% to 2% of pure enzyme by weight of the detergent composition. The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / genetic engineering techniques in order to optimise their performance efficiency in the detergent compositions of the invention. For example, the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that the optimal pH, bleach or chelant stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular cleaning application. In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface charges for the surfactant compatibility. The isoelectric point of such enzymes may be modified by the substitution of some charged amino acids, e.g. an increase in isoelectric point may help to improve compatibility with anionic surfactants. The stability of the enzymes may be further enhanced by the creation of e.g. additional salt bridges and enforcing calcium binding sites to increase chelant stability. Special attention must be paid to the cellulases as most of the cellulases have separate binding domains (CBD). Properties of such enzymes can be altered by modifications in these domains. The enzymes can be added as separate single ingredients (prills, granulates, stabilized liquids, etc... containing one enzyme ) or as mixtures of two or more enzymes ( e.g. cogranulates ). Other suitable detergent ingredients that can be added are enzyme oxidation scavengers which are described in Copending European Patent application 92870018.6 filed on January 31 , 1992. Examples of such enzyme oxidation scavengers are ethoxylated tetraethylene polyamines. A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO93/07263 A and WO93/07260 A to Genencor International, WO89/08694 A to Novo, and U.S. 3,553,139, January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S. 4,101 ,457, Place et al, July 18, 1978, and in U.S. 4,507,219, Hughes, March 26, 1985. Enzyme materials useful for liquid detergent formulations, and their incorporation into such formulations, are disclosed in U.S. 4,261 ,868, Hora et al, April 14, 1981. Enzymes for use in detergents can be stabilised by various techniques. Enzyme stabilisation techniques are disclosed and exemplified in U.S. 3,600,319, August 17, 1971 , Gedge et al, EP 199,405 and EP 200,586, October 29, 1986, Venegas. Enzyme stabilisation systems are also described, for example, in U.S. 3,519,570. A useful Bacillus, sp. AC13 giving proteases, xylanases and cellulases, is described in WO94/01532 A to Novo. Bleaching agent A further preferred ingredient of the detergent compositions of the present invention include bleaching agents. Indeed, it has been found that the oxidisation of the starch material by a bleaching agent solubilises the starch materials, which are therefore more easily removed. Hence, the compositions of the present invention further comprising a bleaching agent will provide improved removal of starch-containing stains and soils, and when formulated as laundry compositions, improved whiteness maintenance and dingy cleaning. Suitable bleaching agents for the purpose of the present invention include hydrogen peroxide, 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%. 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 monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino-4- oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents are disclosed in U.S. Patent 4,483,781 , U.S. Patent Application 740,446, European Patent Application 0,133,354 and U.S. Patent 4,412,934. Highly preferred bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid as described in U.S. Patent 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 tetraacetylethyienediamine (TAED), nonanoyloxybenzene- sulfonate (NOBS, described in US 4,412,934), 3,5,- trimethylhexanoloxybenzenesuifonate (ISONOBS, described in EP 120,591 ) or pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6- aminocaproic acid (NACA-OBS, described in WO94/28106), which are perhydroiyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. Also suitable activators are acylated citrate esters such as disclosed in Copending European Patent Application No. 91870207.7 and unsymetrical acyclic imide bleach activator of the following formula as disclosed in the Procter & Gamble co-pending patent applications US serial No. 60/022,786 (filed July 30, 1996) and No. 60/028,122 (filed October 15, 1996) : wherein R-| is a C7-C13 linear or branched chain saturated or unsaturated alkyl group, R2 is a C-|-C8 j linear or branched chain saturated or unsaturated alkyl group and R3 is a C1-C4 linear or branched chain saturated or unsaturated alkyl group. Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in detergent compositions according to the invention are described in our co- pending applications USSN 08/136,626, PCT/US95/07823, W095/27772, W095/27773, W095/27774 and W095/27775. The hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generating hydrogen peroxide at the beginning or during the washing and/or rinsing process. Such enzymatic systems are disclosed in EP Patent Application 91202655.6 filed October 9, 1991. Metal-containing catalysts for use in bleach compositions, include cobalt- containing catalysts such as Pentaamine acetate cobalt(lll) salts and manganese-containing catalysts such as those described in EPA 549 271 ; EPA 549 272; EPA 458 397; US 5,246,621 ; EPA 458 398; US 5,194,416 and US 5,114,611. Bleaching composition comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent is described in the patent application No 94870206.3. The bleaching compounds can be catalyzed by means of a manganese compound. Such compounds are well known in the art and include, for example, the manganese-based catalysts disclosed in U.S. Pat. 5,246,621 , U.S. Pat. 5,244,594; U.S. Pat. 5,194,416; U.S. Pat. 5,114,606; and European Pat. App. Pub. Nos. 549,271 A1 , 549.272A1 , 544.440A2, and 544,490A1 ; Preferred examples of these catalysts include Mn'V2(u-0)3(1 ,4,7- trimethyl-1 ,4,7-triazacyclononane)2(PF5)2, Mn"'2(u-0)ι (u-OAc)2(1 ,4,7-trimethyl- 1 ,4,7-triazacyclononane)2(CI04)2, Mn' V 4(u-0)6(1 ,4,7- triazacyclononane)4(CI04)4, Mn'llMn' 4(u-0)i (u-OAc)2-(1 ,4,7-trimethyl-1 ,4,7- triazacyclononane)2(Clθ4)3, Mn' v (1 ,4,7-trimethyl-1 ,4,7-triazacyclononane)- (OCH3)3(PFβ), and mixtures thereof. More preferred for use therein are the transition -metal bleach catalysts being complexes of a transition metal and a cross bridged macropolycyclic ligands such as described in Procter & Gamble patent applications WO98/39405, WO 98/39406 and WO98/39098. Most preferred is the Mn Complex Bleach Catalyst of the formula [Mn(Bcyclam)Cl 2 ] illustrated as: "Bcyclam" (5,12-dimethyM ,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane). Such transition -metal bleach catalyst can be prepared according to Procter & Gamble patent application W098/39335 or according to J.Amer.Chem.Soα, (1990), 112, 8604. 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 photoactivated bleaching agents such as the sulfonated zinc and/or aluminum 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 activated and, consequently, the substrate is bleached. Preferred zinc phthalocyanine and a photoactivated bleaching process are described in U.S. Patent 4,033,718. Typically, detergent compositions will contain about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine. Colour care and fabric care benefits Technologies which provide a type of colour care benefit can also be included. Examples of these technologies are metallo catalysts for colour maintenance. Such metallo catalysts are described in copending European Patent Application No. 92870181.2. Dye fixing agents, polyolefin dispersion for anti-wrinkles and improved water absorbancy, perfume and amino-functional polymer (PCT/US97/16546) for colour care treatment and perfume substantivity are further examples of colour care / fabric care technologies and are described in the co-pending Patent Application No. 96870140.9, filed November 07, 1996. Fabric softening agents can also be incorporated into 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-1 400 898 and in USP 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP-B0 011 340 and their combination with mono C12-C14 quaternary ammonium salts are disclosed in EP-B-0 026 527 and EP-B-0 026 528 and di- long-chain amides as disclosed in EP-B-0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0 313 146. Levels of smectite clay are normally in the range from 2% to 20%, more preferably from 5% to 15% 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 convenient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition. 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, alkyl- or alkenyl- succinic acid and fatty acids, materials such as ethylenediamine tetraacetate, diethylene triamine pentamethyleneacetate, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid. Phosphate builders can also be used herein. Suitable builders can be an inorganic ion exchange material, commonly 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 disclosed 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) diacetic acid, maleic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in German Offenlegenschrift 2,446,686, and 2,446,687 and U.S. Patent No. 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-1 ,1 ,3-propane tricarboxylates described in British Patent No. 1 ,387,447. Polycarboxylates containing four carboxy groups include oxydisuccinates disclosed in British Patent No. 1 ,261 ,829, 1 ,1 ,2,2-ethane tetracarboxyiates, 1 ,1 ,3,3-propane tetracarboxyiates and 1 ,1 ,2,3-propane tetracarboxyiates. Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in British Patent Nos. 1 ,398,421 and 1 ,398,422 and in U.S. Patent No. 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 pentacarboxylates, 2,3,4,5-tetrahydro-furan - cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan -cis - dicarboxylates, 2,2,5,5- tetrahydrofuran - tetracarboxyiates, 1 ,2,3,4,5,6-hexane -hexacar-boxylates and and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic poly-carboxylates 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 hydroxycarboxylates 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. Other preferred builder systems include a mixture of a water-insoluble aluminosilicate builder such as zeolite A, and a watersolubie carboxylate chelating agent such as citric acid. Preferred builder systems for use in liquid detergent compositions of the present invention are soaps and polycarboxylates. 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 polyaikylene 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 from 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 copolymers 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 preferably from 10% to 70% and most usually from 30% to 60% by weight. Chelating Agents The detergent compositions herein may also optionally contain one or more iron and/or manganese chelating agents. Such chelating agents can be selected from the group consisting of amino carboxylates, amino phosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures therein, all as hereinafter defined. Without intending to be bound by theory, it is believed that the benefit of these materials is due in part to their exceptional ability to remove iron and manganese ions from washing solutions by formation of soluble chelates. Amino carboxylates useful as optional chelating agents include ethylenediaminetetracetates, N-hydroxyethylethylenediaminetriacetates, nitrilotriacetates, ethylenediamine tetraproprionates, triethylenetetraaminehexacetates, diethylenetriaminepentaacetates, and ethanoldiglycines, alkali metal, ammonium, and substituted ammonium salts therein and mixtures therein. Amino phosphonates are also suitable for use as chelating agents in the compositions of the invention when at lease low levels of total phosphorus are permitted in detergent compositions, and include ethylenediaminetetrakis (methylenephosphonates) as DEQUEST. Preferred, these amino phosphonates to not contain alkyl or alkenyl groups with more than about 6 carbon atoms. Polyfunctionally-substituted aromatic chelating agents are also useful in the compositions herein. See U.S. Patent 3,812,044, issued May 21 , 1974, to Connor et al. Preferred compounds of this type in acid form are dihydroxydisulfobenzenes such as 1 ,2-dihydroxy-3,5-disulfobenzene. A preferred biodegradable chelator for use herein is ethylenediamine disuccinate ("EDDS"), especially the [S,S] isomer as described in U.S. Patent 4,704,233, November 3, 1987, to Hartman and Perkins. The compositions herein may also contain water-soluble methyl glycine diacetic acid (MGDA) salts (or acid form) as a chelant or co-builder useful with, for example, insoluble builders such as zeolites, layered silicates and the like. If utilized, these chelating agents will generally comprise from about 0.1% to about 15% by weight of the detergent compositions herein. More preferably, if utilized, the chelating agents will comprise from about 0.1 % to about 3.0% by weight of such compositions. Suds suppressor Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-silicone mixtures. Silicones can be generally 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. These materials can be incorporated as particulates in which the suds suppressor is advantageously reieasably incorporated in a water-soluble or water-dispersible, 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 Bartollota et al. U.S. Patent 3 933 672. Other particularly useful suds suppressors are the self- emulsifying silicone suds suppressors, described in German Patent Application DTOS 2 646 126 published April 28, 1977. An example of such a compound is DC-544, commercially available from 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-alcanols. Suitable 2-alkyl- alkanois are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R. Such suds suppressor system are described in Copending European Patent application N 92870174.7 filed 10 November, 1992. Especially preferred silicone suds controlling agents are described in Copending European Patent application N°92201649.8. Said compositions can comprise a silicone/silica mixture in combination with fumed nonporous silica such as AerosilR. 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. Others Other components used in detergent compositions may be employed, such as soil-suspending agents, soil-release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or non- encapsulated 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 encapsulating materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modified by adding monofunctional substituted groups such as octenyl succinic acid anhydride. Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose 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 copolymers 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 from 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-aniiino-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, di-so-dium 4,4'bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-6- ylami-no)stiibene- 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. Highly preferred brighteners are the specific brighteners disclosed in EP 753 567. 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 polycarboxylate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizable soils in the presence 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 various arrangements. Examples of such polymers are disclosed in the commonly assigned US Patent Nos. 4116885 and 4711730 and European Published Patent Application No. 0 272 033. A particular preferred polymer in accordance with EP-A-0 272 033 has the formula (CH 3 (PEG)43)o.75(POH)o.25F-PO)2.8(T-PEG)o.4]T(PO- H)o.25((P G)43CH 3 )o.75 where PEG is -(OC2H4)0-,PO is (OC3H 6 0) and T is (PCOC6H4CO). Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propane diol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or propane-diol. 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 end-capped by sulphobenzoate groups. However, some copolymers will be less than fully capped, and therefore their end groups may consist of monoester of ethylene glycol and/or propane 1-2 diol, thereof consist "secondarily" of such species. The selected polyesters herein contain about 46% by weight of dimethyl terephthalic acid, about 16% by weight of propane -1.2 diol, about 10% by weight ethylene glycol about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000. The polyesters and their method of preparation are described in detail in EPA 311 342. It is well known in the art that free chlorine in tap water rapidly deactivates the enzymes comprised in detergent compositions. Therefore, using chlorine scavenger such as perborate, ammonium sulfate, sodium sulphite or polyethyleneimine at a level above 0.1% by weight of total composition, in the formulas will provide improved through the wash stability of the detergent enzymes. Compositions comprising chlorine scavenger are described in the European patent application 92870018.6 filed January 31 , 1992. Alkoxylated polycarboxylates such as those prepared from polyacrylates are useful herein to provide additional grease removal performance. Such materials are described in WO91/08281 and PCT 90/01815 at p. 4 et seq., incorporated herein by reference. Chemically, these materials comprise polyacrylates having one ethoxy side-chain per every 7-8 acrylate units. The side-chains are of the formula -(CH2CH2θ) m (CH2) n CH3 wherein m is 2-3 and n is 6-12. The side- chains are ester-linked to the polyacrylate "backbone" to provide a "comb" polymer type structure. The molecular weight can vary, but is typically in the range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can comprise from about 0.05% to about 10%, by weight, of the compositions herein. Dispersants The detergent composition of the present invention can also contain dispersants: 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 from 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 copolymers with maleic anhydride, such copolymers having a molecular weight of from 1 ,000 to 100,000. Especially, copolymer of acrylate and methylacrylate such as the 480N having a molecular weight of 4000, at a level from 0.5-20% by weight of composition can be added in the detergent compositions of the present invention. The compositions of the invention may contain a lime soap peptiser compound, which has preferably a lime soap dispersing power (LSDP), as defined hereinafter of no more than 8, preferably no more than 7, most preferably no more than 6. The lime soap peptiser compound is preferably present at a level from 0% to 20% by weight. A numerical measure of the effectiveness of a lime soap peptiser is given by the lime soap dispersant power (LSDP) which is determined using the lime soap dispersant test as described in an article by H.C. Borghetty and CA. Bergman, J. Am. Oil. Chem. Soc, volume 27, pages 88-90, (1950). This lime soap dispersion test method is widely used by practitioners in this art field being referred to, for example, in the following review articles; W.N. Linfield, Surfactant science Series, Volume 7, page 3; W.N. Linfield, Tenside surf, det., volume 27, pages 159-163, (1990); and M.K. Nagarajan, W.F. Master, Cosmetics and Toiletries, volume 104, pages 71-73, (1989). The LSDP is the % weight ratio of dispersing agent to sodium oleate required to disperse the lime soap deposits formed by 0.025g of sodium oleate in 30ml of water of 333ppm CaCθ3 (Ca:Mg=3:2) equivalent hardness. Surfactants having good lime soap peptiser capability will include certain amine oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated alcohols. Exemplary surfactants having a LSDP of no more than 8 for use in accord with the present invention include C16-C18 dimethyl amine oxide, C12- 18 alkyl ethoxysulfates with an average degree of ethoxylation of from 1 -5, particularly C-12- 15 alkyl ethoxysulfate surfactant with a degree of ethoxylation of amount 3 (LSDP=4), and the C14-C-15 ethoxylated alcohols with an average degree of ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol A012 and Lutensol A030 respectively, by BASF GmbH. Polymeric lime soap peptisers suitable for use herein are described in the article by M.K. Nagarajan, W.F. Masler, to be found in Cosmetics and Toiletries, volume 104, pages 71-73, (1989). Hydrophobic bleaches such as 4-[N-octanoyi-6-aminohexanoyl]benzene sulfonate, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl-6- aminohexanoyl]benzene sulfonate and mixtures thereof; and nonanoyloxy benzene sulfonate together with hydrophilic / hydrophobic bleach formulations can also be used as lime soap peptisers compounds. Dye transfer inhibition The detergent compositions of the present invention can also include compounds for inhibiting dye transfer from one fabric to another of solubilized and suspended dyes encountered during fabric laundering operations involving colored fabrics. Polymeric dye transfer inhibiting agents The detergent compositions according to the present invention also comprise from 0.001% to 10 %, preferably from 0.01% to 2%, more preferably from 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 to complex or adsorb 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-vinylpyrroiidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. Addition of such polymers also enhances the performance of the enzymes according the invention. a) Polyamine N-oxide polymers The polyamine N-oxide polymers suitable for use contain units having the following structure formula : P I (I) A x I R wherein P is a polymerisable unit, whereto the R-N-0 group can be attached to or wherein the R-N-0 group forms part of the polymerisable unit or a combination of both. O O O II II II A is NC, CO, C, -0-,-S-, -N- ; x is O or 1 ; R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or alicyclic groups or any combination thereof whereto the nitrogen of the N-0 group can be attached or wherein the nitrogen of the N-0 group is part of these groups. The N-0 group can be represented by the following general structures: 0 o 1 I (R1 )x -N- (R2)y =N- (R1 )x I (R3)z wherein R1 , R2, and R3 are aliphatic groups, aromatic, heterocyclic or alicyclic groups or combinations thereof, x or/and y or/and z is 0 or 1 and wherein the nitrogen of the N-0 group can be attached or wherein the nitrogen of the N-0 group forms part of these groups. The N-0 group can be part of the polymerisable unit (P) or can be attached to the polymeric backbone or a combination of both. Suitable polyamine N-oxides wherein the N-0 group forms part of the polymerisable unit comprise polyamine N-oxides wherein R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups. One class of said polyamine N-oxides comprises the group of polyamine N- oxides wherein the nitrogen of the N-0 group forms part of the R-group. Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof. Another class of said polyamine N-oxides comprises the group of polyamine N- oxides wherein the nitrogen of the N-0 group is attached to the R-group. Other suitable polyamine N-oxides are the polyamine oxides whereto the N-0 group is attached to the polymerisable unit. Preferred class of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the N-0 functional group is part of said R group. Examples of these classes are polyamine oxides wherein R is a heterocyclic compound such as pyrridine, pyrrole, imidazole and derivatives thereof. Another preferred class of polyamine N-oxides are the polyamine oxides having the general formula (I) wherein R are aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the N-0 functional group is attached to said R groups. Examples of these classes are polyamine oxides wherein R groups can be aromatic such as phenyl. Any polymer backbone can be used as long as the amine oxide polymer formed is water-soluble and has dye transfer inhibiting properties Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamide, polyimides, polyacrylates and mixtures thereof The amine N-oxide polymers of the present invention typically have a ratio of amine to the amine N-oxide of 10 1 to 1 1000000 However the amount of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymenzation or by appropriate degree of N-oxidation Preferably, the ratio of amine to amine N-oxide is from 2:3 to 1 1000000 More preferably from 1 4 to 1 1000000, most preferably from 17 to 1 -1000000. The polymers of the present invention actually encompass random or block copolymers where one monomer type is an amine N-oxide and the other monomer type is either an amine N-oxide or not The amine oxide unit of the polyamine N-oxides has a PKa < 10, preferably PKa < 7, more preferred PKa < 6 The polyamine oxides can be obtained in almost any degree of polymerisation The degree of polymerisation is not critical provided the material has the desired water-solubility and dye-suspending power. Typically, the average molecular weight is within the range of 500 to 1000,000; preferably from 1 ,000 to 50,000, more preferably from 2,000 to 30,000, most preferably from 3,000 to 20,000 b) Copolymers of N-vinylpyrrohdone and N-vinylimidazole The N-vinylimidazole N-vinylpyrrolidone polymers used in the present invention have an average molecular weight range from 5,000-1 ,000,000, preferably from 5,000-200,000. Highly preferred polymers for use in detergent compositions according to the present invention comprise a polymer selected from N-vinylimidazole N- vinylpyrrolidone copolymers wherein said polymer has an average molecular weight range from 5,000 to 50,000 more preferably from 8,000 to 30,000, most preferably from 10,000 to 20,000. The average molecular weight range was determined by light scattering as described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113,"Modem Methods of Polymer Characterization". Highly preferred N-vinylimidazole N-vinyipyrrolidone copolymers have an average molecular weight range from 5,000 to 50,000; more preferably from 8,000 to 30,000; most preferably from 10,000 to 20,000. The N-vinylimidazole N-vinylpyrrolidone copolymers characterized by having said average molecular weight range provide excellent dye transfer inhibiting properties while not adversely affecting the cleaning performance of detergent compositions formulated therewith. The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, more preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4 . c) Polyvinyipyrrolidone The detergent compositions of the present invention may also utilize polyvinyipyrrolidone ("PVP") having an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000. Suitable polyvinylpyrrolidones are commercially vailable from ISP Corporation, New York, NY and Montreal, Canada under the product names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K-60 (average molecular weight of 160,000), and PVP K-90 (average molecular weight of 360,000). Other suitable polyvinylpyrrolidones which are commercially available from BASF Cooperation include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones known to persons skilled in the detergent field (see for example EP-A-262,897 and EP-A- 256,696). d) Polyvinyloxazolidone : The detergent compositions of the present invention may also utilize polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said polyvinyloxazolidones have an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000. e) Polyvinylimidazole The detergent compositions of the present invention may also utilize polyvinylimidazole as polymeric dye transfer inhibiting agent. Said polyvinylimidazoles have an average about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000. f) Cross-linked polymers : Cross-linked polymers are polymers whose backbone are interconnected to a certain degree; these links can be of chemical or physical nature, possibly with active groups n the backbone or on branches; cross-linked polymers have been described in the Journal of Polymer Science, volume 22, pages 1035-1039. In one embodiment, the cross-linked polymers are made in such a way that they form a three-dimensional rigid structure, which can entrap dyes in the pores formed by the three-dimensional structure. In another embodiment, the cross- linked polymers entrap the dyes by swelling. Such cross-linked polymers are described in the co-pending patent application 94870213.9 Method of washing The compositions of the invention may be used in essentially any washing or cleaning methods, including soaking methods, pretreatment methods and methods with rinsing steps for which a separate rinse aid composition may be added. The process described herein comprises contacting fabrics, dishware or any other hard surface with a cleaning solution in the usual manner and exemplified hereunder. A conventional laundry method comprises treating soiled fabric with an aqueous liquid having dissolved or dispensed therein an effective amount of the laundry detergent and/or fabric care composition. A preferred machine dishwashing method comprises treating soiled articles with an aqueous liquid having dissolved or dispensed therein an effective amount of the machine diswashing or rinsing composition. A conventional effective amount of the machine dishwashing composition means from 8-60 g of product dissolved or dispersed in a wash volume from 3-10 litres. According to a manual dishwashing method, soiled dishes are contacted with an effective amount of the diswashing composition, typically from 0.5-20g (per 25 dishes being treated). Preferred manual dishwashing methods include the application of a concentrated solution to the surfaces of the dishes or the soaking in large volume of dilute solution of the detergent composition. A conventional hard surface method comprises treating soiled hard items with e.g. a sponge, brush, clothe, etc. with an aqueous liquid having dissolved or dispensed therein an effective amount of the hard surface cleaner and/or with such composition undiluted. It also encompasses or the soaking in a concentrated solution or in a large volume of dilute solution of the detergent composition. The process of the invention is conveniently carried out in the course of the cleaning process. The method of cleaning is preferably carried out at 5°C to 95°C, especially between 10°C and 60°C. The pH of the treatment solution is preferably from 7 to 12. The following examples are meant to exemplify compositions of the present invention, but are not necessarily meant to limit or otherwise define the scope of the invention. In the detergent compositions, the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total compositions. The abbreviated component identifications therein have the following meanings: LAS Sodium linear C-| 1- 3 alkyl benzene sulphonate. TAS Sodium tallow alkyl sulphate. CxyAS Sodium C-| x - C-jy alkyl sulfate. CxySAS Sodium C-|χ - C<| v secondary (2,3) alkyl sulfate. CxyEz C-|χ - C^y predominantly linear primary alcohol condensed with an average of z moles of ethylene oxide. CxyEzS C-j - C-|y sodium alkyl sulfate condensed with an average of z moles of ethylene oxide. CxEOy Cy alcohol with an average of ethoxylation of y. Nonionic Mixed ethoxylated/propoxylated fatty alcohol e.g. Plurafac LF404 being an alcohol with an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5. QAS R 2 .N+(CH3)2(C2H OH) with R2 = C 12 -C 1 . QAS 1 R2.N+(CH 3 )2(C2H 4 OH) with R 2 = C 8 -C-| -| . SADS Sodium C14-22 alkyl disulphate of fromula 2-(R).C4H7- 1 ,4-(S04-)2 where R=C10-18 MBAS C12-18 mid branched alkyl sulphate surfactant with an average branching of 1.5 methyl or ethyl branching groups MES x-Sulpho methylester of C18 fatty acid APA C8-10 amido propyl dimethyl amine. Soap Sodium linear alkyl carboxylate derived from a 80/20 mixture of tallow and coconut fatty acids. STS Sodium toluene sulphonate. TFAA C-15-C18 alkyl N-methyl glucamide. TPKFA C12- 4 topped whole cut fatty acids. DEQA Di-(tallow-oxy-ethyl) dimethyl ammonium chloride. DEQA (2) Di-(soft-tallowyloxyethyl) hydroxyethyl methyl ammonium methylsulfate. SDASA 1 :2 ratio of stearyldimethyl amine:triple-pressed stearic acid. DTMAMS Ditallow dimethyl ammonium methylsulfate. Silicate Amorphous Sodium Silicate (Siθ2:Na2θ ratio = 1.6- 3.2:1 ). Metasiiicate Sodium metasiiicate (Siθ2:Na2θ ratio = 1.0). Zeolite A Hydrated Sodium Aluminosilicate of formula Na-|2(A1θ2Siθ2)i2- 27H2O having a primary particle size in the range from 0.1 to 10 micrometers (Weight expressed on an anhydrous basis). SKS-6 Crystalline layered silicate of formula δ-Na2Si2θ5 Citrate Tri-sodium citrate dihydrate. Citric Anhydrous citric acid. Carbonate Anhydrous sodium carbonate. Bicarbonate Sodium hydrogen carbonate. Sulphate Anhydrous sodium sulphate. Mg Sulphate Anhydrous magnesium sulfate. STPP Sodium tripolyphosphate. TSPP Tetrasodium pyrophosphate. MA/AA Random copolymer of 4:1 acrylate/maleate, average molecular weight about 70,000-80,000. MA/AA 1 Random copolymer of 6:4 acrylate/maleate, average molecular weight about 10,000. AA Sodium polyacrylate polymer of average molecular weight 4,500. Polycarboxylate Copolymer comprising mixture of carboxylated monomers such as acrylate, maleate and methyacrylate with a MW ranging between 2,000-80,000 such as Sokolan commercially available from BASF, being a copolymer of acrylic acid, MW4.500. Clay Bentonite or smectite clay. PB1 Anhydrous sodium perborate monohydrate. PB4 Sodium perborate tetrahydrate of nominal formula NaBθ3_4H 2 0. Percarbonate Anhydrous sodium percarbonate of nominal formula Na2Cθ3.3H2θ2 . NaDCC Sodium dichloroisocyanurate. TAED Tetraacetyl ethylene diamine. NOBS Nonanoyloxybenzene sulfonate in the form of the sodium salt. NACA-OBS (6-nonamidocaproyl) oxybenzene sulfonate. LOBS Dodecanoyloxybenzene sulfonate in the form of the Na salt. DOBA Dodecanoylbenzoic acid DTPA Diethylene triamine pentaacetic acid. HEDP 1 ,1-hydroxyethane diphosphonic acid. DETPMP Diethyltriamine penta (methylene) phosphonate, marketed by Monsanto under the Trade name Dequest 2060. EDDS Ethylenediamine-N,N'-disuccinic acid, (S,S) isomer in the form of its sodium salt MnTACN Manganese 1 ,4,7-trimethyl-1 ,4,7-triazacyciononane. Photoactivated Sulfonated zinc or alumino phtalocyanine encapsulated Bleach in dextrin soluble polymer. PAAC Pentaamine acetate cobalt(lll) salt. Paraffin Paraffin oil sold under the tradename Winog 70 by Wintershall. NaBz Sodium benzoate. Protease Proteolytic enzyme sold under the tradename Savinase, Alcalase by Novo Nordisk A/S, the "protease D" variant with the substitution set N76D/S103A/V104I and the protease described in PCT application Nos. PCT/US98/22588, PCT/US98/22482 and PCT/US98/22486 with the amino acid substitution set 101 G/103A/1041/159D/232V/236H/245R 248D/252K. Amylase Amylolytic enzyme sold under the tradename Termamyl ® and Duramyl® available from Novo Nordisk A/S and those variants having improved thermal stability with amino acid deletions R181 * + G182 * or T183 * + G184 * as described in W095/35382. Lipase Lipolytic enzyme sold under the tradename Lipolase, Lipolase Ultra by Novo Nordisk A/S and Lipomax by Gist- Brocades. AMG Amyloglucosidase sold under the tradename AMG by Novo Nordisk A/S or under Spezyme ® by Genencor. Isoamylase Isoamylase sold under the name isoamylase by Sigma Pullulanase Pullulanase type I sold under the trade name Promozyme by Novo Nordisk A/S Cellulase Cellulytic enzyme sold under the tradename Carezyme, Celluzyme and/or Endolase by Novo Nordisk A/S. CMC Sodium carboxymethyl cellulose. PVP Polyvinyl polymer, with an average molecular weight of 60,000. PVNO Polyvinylpyridine-N-Oxide, with an average molecular weight of 50,000. PVPVI Copolymer of vinylimidazole and vinylpyrrolidone, with an average molecular weight of 20,000. Brightener 1 Disodium 4,4'-bis(2-sulphostyryl)biphenyl. Brightener 2 Disodium 4,4'-bis(4-anilino-6-morpholino-1.3.5-triazin-2- yl) stilbene-2:2'-disulfonate. Brightener 3 Disodium 4,4'bιs (4,6-dιanιlιno-1 ,3,5-trιazιn-2-yl)amιno stιlbene-2-2'-dιsulfonate Silicone antifoam Polydimethyisiloxane foam controller with siloxane- oxyalkylene copolymer as dispersing agent with a ratio of said foam controller to said dispersing agent of 10:1 to 100:1. Suds Suppressor 12% Silicone/silica, 18% stearyl alcohol, 70% starch in granular form. Thickener High molecular weight cross nked polyacrylates such as Carbopol offered by B.F Goodrich Chemical Company and Polygel. SRP 1 Anionically end capped poly esters. SRP 2 Soil Release Polymer selected from 1 ) Non-cotton soil release polymer according to U.S. Patent 5,415,807, Gosselink, Pan, Kellett and Hall, issued May 16, 1995 or and/or from 2) Non-cotton soil release polymer according to US application no.60/051517. QEA bis((C 2 H5θ)(C2H4θ) n )(CH 3 ) -N + -C 6 H 12 -N + -(CH 3 ) bis((C2H5θ)-(C2H4θ)) n , wherein n = from 20 to 30. PEI Polyethyleneimine with an average molecular weight of between 600-1800 and an average ethoxylation degree of 7-20 ethyleneoxy residues per nitrogen. SCS Sodium cumene sulphonate. HMWPEO High molecular weight polyethylene oxide. PEG X Polyethylene glycol, of a molecular weight of X PEO Polyethylene oxide, with an average molecular weight of 5,000. TEPAE Tetreaethylenepentaamine ethoxylate. BTA Benzotriazole. PH Measured as a 1% solution in distilled water at 20°C. Example 1 The following granular laundry detergent compositions were prepared according to the present invention : I II III IV V I II III IV V Spray-dried Granules LAS 10.0 10.0 15.0 5.0 5.0 TAS - 1.0 - - - MBAS - - - 5.0 5.0 C45AS - - 1.0 - 2.0 C45AE3S - - - 1.0 - QAS - - 1.0 1.0 ' - DTPA, HEDP and/or EDDS 0.3 0.3 0.5 0.3 - Mg Sulfate 0.5 0.5 0.1 - Citrate - - - 3.0 5.0 Carbonate 10.0 7.0 15.0 - - Sulphate 5.0 5.0 - - 5.0 Silicate - - - - 2.0 Zeolite A 16.0 18.0 20.0 20.0 - SKS-6 - - - 3.0 5.0 MA/AA or AA 1.0 2.0 11.0 - - PEG 4000 - 2.0 - 1.0 - QEA 1.0 - - - 1.0 Brightener 1 or 2 or 3 0.05 0.05 0.05 - 0.05 Silicone oil 0.01 0.01 0.01 - - Aqqlomerate Carbonate - - - - 4.0 SKS-6 6.0 - - - 6.0 LAS 4.0 5.0 - - 5.0 Drv-add particulate components Maleic acid / carbonate / bicarbonate 8.0 10.0 10.0 4.0 - (40:20:40) QEA - - - 0.2 0.5 NACA-OBS 3.0 - - 4.5 - NOBS 1.0 3.0 3.0 - - TAED 2.5 - - 1.5 2.5 MBAS - - - 8.0 - LAS (flake) 10.0 10.0 - - - Sorav-on Brightener 1 or 2 or 3 0.2 0.2 0.3 0.1 0.2 1 II Ill IV V Perfume 1.0 0.5 1.1 0.8 0.3 Drv-add Citrate - - 20.0 4.0 - Percarbonate 15.0 3.0 6.0 10.0 - Perborate - - - - 6.0 Photoactivated bleach 0.02 0.02 0.02 0.1 0.05 Enzymes (cellulase, amylase, 0.04 0.01 0.02 0.02 0.05 protease and/or lipase) AMG 1.0 0.05 0.002 0.001 0.05 Carbonate 0.0 10.0 - - - Perfume (encapsulated) - 0.5 0.5 - 0.3 Suds suppressor 1.0 0.6 0.3 - 0.10 Soap 0.5 0.2 0.3 3.0 0.5 Citric - - - 6.0 6.0 SKS-6 . . - 4.0 - Fillers up to 100% Example 2 The following granular laundry detergent compositions were prepared according to the present invention : I II III IV Blown powder MES 2.0 0.5 1.0 - SADS - - - 2.0 LAS 6.0 5.0 11.0 6.0 TAS 2.0 - - 2.0 Zeolite A 24.0 - - 20.0 STPP - 27.0 24.0 - Sulfate 4.0 6.0 13.0 - MA/AA 1.0 4.0 6.0 2.0 Silicate 1.0 7.0 3.0 3.0 CMC 1.0 1.0 0.5 0.6 Brightener 1 0.2 0.2 0.2 0.2 Silicone antifoam 1.0 1.0 1.0 0.3 I II III IV DTPMP 0.4 0.4 0.2 0.4 Spray on Brightener 1 or 2 or 3 0.02 - - 0.02 C45E7 - - - 5.0 C45E2 2.5 2.5 2.0 - C45E3 2.6 2.5 2.0 - Perfume 0.5 0.3 0.5 0.2 Silicone antifoam 0.3 0.3 0.3 - Dry additives QEA - - - 1.0 EDDS 0.3 - - - Sulfate 2.0 3.0 5.0 10.0 Carbonate 6.0 13.0 15.0 14.0 Citric 2.5 - - 2.0 QAS 0.5 - - 0.5 SKS-6 10.0 - - - Percarbonate 4.0 3.0 - 1.9 PB4 - - - NOBS 0.5 - - 0.3 TAED 0.75 4.5 - 0.5 Clay - - 10.0 - Protease 0.03 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 0.004 AMG 0.001 0.01 0.01 0.004 Pullulanase - - 0.01 - Isoamylase - - - 0.002 Amylase 0.003 - 0.003 0.006 Brightener 1 0.05 - - 0.05 Misc/minor and speckles up to 100% Example 3 The following granular laundry detergent compositions were prepared according to the invention : I II III IV V VI IV VI Blown powder LAS 23.0 8.0 7.0 9.0 7.0 7.0 QAS - - - - 1.0 - C45AS 6.0 6.0 5.0 8.0 - - C45AE11 S - 1.0 1.0 1.0 - - MES 2.0 - - - 2.0 4.0 Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0 MA/AA - 0.5 - - - 2.0 MA/AA 1 7.0 - - - - - AA - 3.0 3.0 2.0 3.0 3.0 Sulfate 5.0 6.3 11.1 11.0 11.0 18.1 Silicate 10.0 1.0 1.0 1.0 1.0 1.0 Carbonate 15.0 20.0 10.0 20.7 8.0 6.0 PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0 DTPA - 0.9 0.5 - - 0.5 Brightener 2 0.3 0.2 0.3 - 0.1 0.3 Spray on C45E7 - 2.0 - - 2.0 2.0 C25E9 3.0 - - - - - C23E9 - - 1.5 2.0 - 2.0 Perfume 0.3 0.3 0.3 2.0 0.3 0.3 Aqqlomerates C45AS - 5.0 5.0 2.0 - 5.0 LAS - 2.0 2.0 - - 2.0 Zeolite A - 7.5 7.5 8.0 - 7.5 Carbonate - 4.0 4.0 5.0 - 4.0 PEG 4000 - 0.5 0.5 - - 0.5 Misc (water etc) - 2.0 2.0 2.0 - 2.0 Dry additives QAS I - - - - 1.0 - Citric - - - - 2.0 - PB4 - - - - 5 - PB1 - - 4 1.0 - - Percarbonate 2.0 - - 1.0 - 2.0 Carbonate . 5.3 1.8 - 4.0 4.0 I II Ill IV V VI NOBS 0.5 - 0.4 0.3 - - Clay - - - - - 10.0 TAED 0.6 0.4 0.6 0.3 0.9 - Methyl cellulose 0.2 - - - - 0.5 DTPA 0.7 0.5 1.0 0.5 0.5 1.2 speckle - - - 0.2. 0.5 - SKS-6 8.0 - - - - - STS - - 2.0 - 1.0 - Cumene sulfonic - 1.0 - - - 2.0 acid Lipase 0.004 - 0.004 - 0.004 0.008 Cellulase 0.0005 0.0005 0.0005 0.0007 0.0005 0.0005 Amylase 0.003 - 0.001 - 0.003 - Pullulanase - 0.01 - - 0.001 - Isoamylase - - - - 0.001 0.01 AMG 0.01 5.0 0.05 0.002 0.001 0.05 Protease 0.01 0.015 0.015 0.009 0.01 0.01 PVPVI - - - - 0.5 0.1 PVP - - - - 0.5 - PVNO - - 0.5 0.3 - - QEA - - - - 1.0 - SRP1 0.2 0.5 0.3 - 0.2 - Silicone antifoam 0.2 0.4 0.2 0.4 0.1 - Mg sulfate - - 0.2 - 0.2 - Misc/minors up to 100% Example 4 The following granular laundry detergent compositions were prepared according to the present invention: I II III IV Base granule STPP _ 22.0 . 15.0 Zeolite A 30.0 - 24.0 5.0 Sulfate 5.5 5.0 7.0 7.0 I II III IV MA AA 3.0 AA - 1.6 2.0 - MA/AA 1 - 12.0 - 6.0 LAS 14.0 10.0 9.0 20.0 C45AS 8.0 7.0 9.0 7.0 C45AE11S - 1.0 - 1.0 MES 0.5 4.0 6.0 ' SADS 2.5 - - 1.0 Silicate - 1.0 0.5 10.0 Soap - 2.0 - - Brightener 1 0.2 0.2 0.2 0.2 Carbonate 6.0 9.0 8.0 10.0 PEG 4000 - 1.0 1.5 - DTPA - 0.4 - - Spray on C25E9 _ _ . 5.0 C45E7 1.0 1.0 - - C23E9 - 1.0 2.5 - Perfume 0.2 0.3 0.3 - Dry additives Carbonate 5.0 10.0 13.0 8.0 PVPVI/PVNO 0.5 - 0.3 - Protease 0.03 0.03 0.03 0.015 Lipase 0.008 - - 0.008 AMG 0.01 3.0 0.05 0.005 Pullulanase _ - 0.02 0.001 Isoamylase . - - 0.005 Amylase 0.002 - - 0.002 Cellulase 0.0002 0.0005 0.0005 0.0003 DTPA 0.5 0.3 0.5 1.0 LOBS - 0.8 - 0.3 PB1 5 3.0 10 4.0 DOBA 1.0 - 0.4 - TAED 0.5 0.3 0.5 0.6 Sulfate 4.0 5.0 - 5.0 IV SRP 1 0.4 Suds supressor 0.5 speckle 09 2.7 1.2 Misc/minor to 100% Example 5 The following granular laundry detergent compositions were prepared according to the present invention : I II III IV IV V VI C 13 LAS 12.0 16.0 23.0 19.0 18.0 20.0 16.0 C45 AS 4.5 - - - 4.0 C4 5 AE (3)S - - 2.0 - 1.0 1.0 1.0 C4 5 AE (3.0) 2.0 2.0 - 1.3 - - 0.6 Cg-Cu alkyl dimethyl hydroxy - - 1.0 0.5 2.0 ethyl quaternary ammonium salt Tallow fatty acid - - - - - - 1.0 STPP 23.0 25.0 24.0 22,0 20.0 15.0 20.0 Carbonate 15.0 12.0 15.0 10.0 13.0 11.0 10.0 AA 0.5 0.5 0.5 0.5 - MA/AA - - 1.0 1.0 1.0 2.0 0.5 Silicate 3.0 6.0 9.0 8.0 9.0 6.0 8.0 Sulfate 25.0 18.0 20.0 18.0 20.0 22.0 13.0 Sodium perborate 5.0 5.0 10.0 8.0 3.0 1.0 2.0 PEG 4000 1.5 1.5 1.0 1.0 - - 0.5 CMC 1.0 1.0 1.0 - 0.5 0.5 0.5 Citric NOBS/ DOBS 0.5 1.0 0.5 0.5 1.0 0.7 0.3 TAED 1.5 1.0 2.5 3.0 0.3 0.2 0.5 SRP 2 1.5 1.5 1.0 1.0 1.0 1.0 1.0 Moisture 7.5 7.5 6.0 7.0 5.0 3.0 5.0 Mg . . . . 1.0 0.5 1.5 DTPA, HEDP and/or EDDS . . . . 0.8 0.6 1.0 AMG 0.01 0.01 .005 0.05 1.0 1.0 .001 III IV IV V VI Enzymes (amylase, 0.05 0.04 0.05 cellulaseand/or protease) Minors, e.g. perfume, Up to 100% Brightener, photo-bleach, speckles Example 6 The following granular laundry detergent compositions were prepared according to the present invention: I II Ill IV C 1 3 LAS 13.3 13.7 10.4 8.0 C45 AS 3.9 4.0 4.5 - C45 AE (0.5)S 2.0 2.0 - - C45 AE (6.5) 0.5 0.5 0.5 5.0 Cg-Cu alkyl dimethyl hydroxy 1.0 - - 0.5 ethyl quaternary ammonium salt Tallow fatty acid 0.5 - - - Tallow alcohol ethoxylate (50) - - 1.0 0.3 STPP - 41.0 - 20.0 Zeolite A 26.3 - 21.3 1.0 Carbonate 23.9 12.4 25.2 17.0 AA 3.4 0.0 2.7 - MA/AA - - 1.0 1.5 Silicate 2.4 6.4 2.1 6.0 Sulfate 10.5 10.9 8.2 15.0 Sodium perborate 1.0 1.0 1.0 2.0 PEG 4000 1.7 0.4 1.0 - CMC 1.0 - - 0.3 Citric - - 3.0 - NOBS/ DOBS 0.2 0.5 0.5 0.1 TAED 0.6 0.5 0.4 0.3 SRP 2 1.5 1.5 1.0 1.0 Moisture 7.5 3.1 6.1 7.3 Mg sulphate - - - 1.0 1 II III IV DTPA, HEDP and/or EDDS - - 0.5 Enzymes (amylase, cellulase, - 0.025 0.04 protease and/or lipase) AMG 0.02 0.05 0.005 o.ooε Misc / Minors including perfume, Up to 100% brightener, photo-bleach Example 7 The following laundry detergent compositions in the form of a tablet or granular formulation were prepared according to the present invention : I II Ill IV V VI C 13 AS 20.0 16.0 8.5 5 20.0 6.0 C45 AS - 4.0 - - - C45 AE(3)S 1.0 1.0 - - - - C45 E - 5.0 5.5 4.0 - Cg-Cu alkyl dimethyl hydroxy 0.5 2.0 - - - - ethyl quaternary ammonium salt Tallow fatty acid - 1.0 - - - - STPP / Zeolite 10.0 20.0 30.0 20.0 25.0 25.0 Carbonate 41.0 30.0 30.0 25.0 45.0 24.0 AA - - - - - - MA/AA 2.0 0.5 0.5 1.0 - - Silicate 6.0 8.0 5.0 6.0 8.0 5.0 Sulfate 2.0 3.0 - - - 8.0 Sodium perborate/ 1.0 - 20.0 14.0 - - percarbonate PEG 4000 - 0.5 - - - 0.5 CMC 0.5 0.5 0.5 0.5 - 0.5 Citric - - - - - - NOBS/ DOBS 0.7 - - - - - TAED / Preformed peracid 0.7 - 4.5 5.0 - - DTPA, HEDP and/or EDDS - - 0.5 0.5 - SRP 1.0 - 1.0 1.0 - - 1 II Ill IV V VI Clay 4.0 3.0 7.0 10.0 6.0 8.0 PEO 1.0 0.5 2.0 0.5 1.0 0.5 Humectant 0.5 - - 0.5 - - wax 0.5 - - 0.5 - - Cellulose 2.0 - - 1.5 - 1.0 Sodium acetate - - 1.0 0.5 4.0 1.0 Moisture 3.0 5.0 5.0 5.0 8.0 10.0 Mg sulphate 0.5 1.5 - - - - Soap/ suds suppressor 0.6 1.0 1.0 0.8 0.5 - Enzymes (amylase, , cellulase, 0.04 0.04 0.01 0.02 0.02 0.03 protease and/or lipase) AMG 0.03 0.01 0.05 .003 0.1 .005 Pullulanase - - 0.02 - - .002 Isoamylase - - - - - .002 Minors, e.g. perfu me, PVP, Up to 100% PVPVI/PVNO, brightener, photo-bleach, speckles,.. Example 8 The following laundry detergent compositions were prepared according to the present invention : I II III IV V C13 LAS 12.0 16.0 23.0 19.0 18.0 C45 AS - 4.5 - - - C45 AE(3)S - - 2.0 - 1.0 C45 AE 2.0 2.0 - 1.3 - Cg-Cu alkyl dimethyl hydroxy - - - - 1.0 ethyl quaternary ammonium salt STPP / Zeolite 23.0 25.0 14.0 22,0 20.0 Carbonate 25.0 22.0 35.0 20.0 28.0 AA 0.5 0.5 0.5 0.5 - MA/AA - - 1.0 1.0 1.0 Silicate 3.0 6.0 9.0 8.0 9.0 1 II Ill IV V Sodium perborate/ 5.0 5.0 10.0 - 3.0 percarbonate PEG 4000 1.5 1.5 1.0 1.0 - CMC 1.0 1.0 1.0 - 0.5 NOBS/ DOBS - 1.0 - - 1.0 TAED / Preformed peracid 1.5 1.0 2.5 - 3.0 DTPA, HEDP and/or EDDS 0.5 0.5 0.5 - ' 1.0 SRP 1.5 1.5 1.0 1.0 - Clay 5.0 6.0 12.0 7.0 10.0 Flocculating agent PEO 0.2 0.2 3.0 2.0 0.1 Humectant - - - - 0.5 wax 0.5 - - - - Cellulose 0.5 2.0 - - 3.0 Sodium acetate 2.0 1.0 3.0 - - Moisture 7.5 7.5 6.0 7.0 5.0 Soap/ suds suppressor - - 0.5 0.5 0.8 AMG 0.02 0.02 .005 .005 0.01 Enzymes (amylase, cellulase, - - - - 0.045 protease and/or lipase) Misc / Minors, e.g. perfume, Up to 100% PVP, PVPVI/PVNO, speckles, brightener, photo-bleach,... Example 9 The following liquid laundry detergent compositions were prepared according to the present invention : I II III IV V VI LAS . . . 1.0 2.0 C25AS 16.0 13.0 14.0 5.0 - 6.5 I II III IV V VI C25AE3S 5.0 1.0 - 10.0 19.0 3.0 C25E7 2.0 3.5 - 2.5 2.0 5.0 TFAA 5.0 4.5 4.5 6.5 4.0 - APA 2.0 1.0 - 3.0 - 0.5 QAS - - 2.0 - 1.5 - TPKFA 4.5 8.0 15.0 - 5.0 5.0 Citric 2.2 3.0 - 0.5 1.0 2.0 Rapeseed fatty acid 2.0 - - 3.0 6.0 1.5 Ethanol 3.2 2.0 2.5 2.2 - 0.5 1 ,2 Propandiol 5.7 8.5 6.5 7.0 7.0 5.5 Monoethanolamine 5.0 7.5 - 5.0 1.0 2.0 TEPAE - 1.2 - 0.5 0.5 - PEI2 - 1.5 - 1.0 0.8 - DTPMP 1.3 0.5 0.8 0.5 - 0.2 HEDP - 0.5 0.2 1.0 - - Protease 0.02 0.03 0.02 0.02 0.02 0.01 AMG 0.01 0.02 0.005 0.01 0.005 0.002 Pullulanase - - 0.2 0.05 - - Isoamylase - - - - - 0.01 Lipase 0.002 0.001 0.001 - 0.001 - Amylase .0008 .0006 .0006 0.002 0.001 0.001 Cellulase 0.002 0.002 - 0.002 0.001 - SRP1 0.20 0.15 0.10 - 0.17 0.04 PVNO - - - 0.05 0.10 - Brightener 3 0.20 0.15 0.10 0.05 - 0.05 Suds Suppressor 0.25 0.20 0.15 0.15 0.30 0.10 Calcium Chloride 0.02 0.02 - 0.01 0.01 - Boric acid 2.5 2.0 1.5 2.2 1.5 1.2 Bentonite Clay - - 5.5 - - - NaOH to pH 8.0 7.5 7.7 8.0 7.0 7.5 Water/minors to 100% Example 10 The following non-aqueous liquid detergent compositions were prepared in accordance with the present invention . I II III LAS 16.0 16.0 16.0 C23 E05S 21.5 21.5 19.0 Butoxy Propoxy Propanol 18.5 - 16.0 Hexylene Glycol - 18.5 5.0 Sodium citrate dihydrate 6.8 6.8 3.8 [4-[N-nonanoyl-6-amιnohexanoyloxy] 6.0 6.0 6.0 benzene sulfonate] Na salt Methyl sulfate salt of methyl quaternized 1.3 1.3 1.3 poiyethoxylated hexamethylene diamine EDDS 1.2 1.2 1.2 MA/AA - - 3.0 Sodium Carbonate 10.0 10.0 10.0 Protease 0.05 0.02 0.02 Pullulanase - - 0.05 Isoamylase - - 0.05 AMG 1.0 0.01 0.02 Amylase 0.01 0.01 0.01 Cellulase 0.0001 0.0001 0.0001 PB1 12.0 12.0 12.0 Silicone antifoam 0.75 0.75 1.1 Perfume 1.7 1.7 1.7 Titanium Dioxide 0.5 0.5 0.5 Dichloro -5,12-Dimethyl-1 ,5,8,12- - 0.03 0.03 tetraazabicyclo [6.6.2] hexadecane Manganese (II) Brightener 2 0.2 0.2 0.2 Sodium hydrogenated C16-18 fatty soap 1 1 0.5 Colored Speckles 0.4 0.4 0.4 Miscellaneous up to 100% Example 11 The following laundry detergent compositions in the form of a tablet were prepared according to the present invention ι) a detergent base powder of composition I was prepared as follows all the particulate material of base composition I were mixed together in a mixing drum to form a homogenous particulate mixture During this mixing, the spray- ons were carried out II) Tablets were then made the following way 50g of the matrix was introduced into a mould of circular shape with a diameter of 5.5 cm, and compressed to give a tablet tensile strength (or diametrical fracture stress) of 10kPa in) The tablets were then dipped in a bath comprising 90 parts of sebacic acid and 10 parts per weight of Nymcel-ZSB16™ by Metsa Serla at 140 °C The time the tablet was dipped in the heated bath was adjusted to allow application of 4g of the bath mixture The tablet was then left to cool at ambient temperature of 25°C for 24 hours The tensile strength of the coated tablet was increased to a tensile strength of 30 kPa. I Anionic agglomerates 1 (40% anionic, 27% zeolite and 33% 21.5 carbonate) Anionic agglomerates 2 (40% anionic, 28% zeolite and 32% 13.0 carbonate) Cationic agglomerates (20% cationic, 56% zeolite and 24% 5.5 sulphate) Layered silicate (95% SKS 6 and 5% silicate) 10.8 Sodium percarbonate 14.2 Bleach activator agglomerates (81% TAED, 17% acrylic/maleic 5.5 copolymer (acid form) and 2% water) Carbonate 10.98 EDDS/Sulphate particle (58% of EDDS, 23% of sulphate and 19% 0 5 water) HEDP 0.8 SRP 0.3 Fluorescer 0-2 Photoactivated bleach (Zinc phthalocyanine sulphonate 10% active) 0.02 Soap powder 1.4 Suds suppressor (11.5% silicone oil; 59% of zeolite and 29.5% of 1.9 water) Citric 7.1 AMG 0.05 Protease 0.03 Lipase 0.006 Cellulase 0.0005 Amylase 0.02 Binder spray-on system (25% of Lutensit K-HD 96;75% by weight of 4.0 PEG) Example 12 The following laundry detergent compositions in the form of a tablet were prepared according to the present invention : I II III IV V VI First Phase Percarbonate 45.0 45.0 45.0 45.0 45.0 45.0 TAED 9.7 9.7 9.7 9.7 9.7 9.7 Citric acid 10.0 15.0 20.0 15.0 15.0 15.0 STPP - - - - - 6.0 MA/AA 6.0 6.0 1.0 5.0 - - Silicates - - - - 6.0 - Bicarbonate 15.0 15.0 10.0 15.0 15.0 15.0 Carbonate 5.0 - - - - - Brightener 1 or 2 0.1 0.1 0.1 0.1 0.1 0.1 Perfume 0.2 0.2 0.2 0.2 0.2 0.2 C12-16 Fatty acid - - - 1.0 - - Protease 0.03 0.03 0.03 0.03 0.03 0.03 Amylase 0.02 0.02 - 0.02 - - Second phase AMG 0.01 0.02 0.04 0.01 0.1 0.5 Protease 0.04 0.04 0.04 0.04 0.04 0.04 Amylase 0.02 0.02 - - - - Speckles 0.09 0.09 0.09 0.09 0.09 0.09 PEG 4000 0.33 0.33 0.33 0.33 0.33 0.33 Citric 1.06 1.06 1.06 1.06 1.06 1.06 Bicarbonate 2.87 2.87 2.87 2.87 2.87 2.87 Example 13 The following laundry bar detergent compositions were prepared according to the present invention (Levels are given in parts per weight, enzyme are expressed in pure enzyme) : I II III VI V III VI V LAS - - 19.0 15.0 21.0 6.75 8.8 - C28AS 30.0 13.5 - - - 15.75 11.2 22.5 Na Laurate 2.5 9.0 - - - - - - Zeolite A 2.0 1.25 - - - 1.25 1.25 1.25 Carbonate 20.0 3.0 13.0 8.0 10.0 15.0 15.0 10.0 Ca Carbonate 27.5 39.0 35.0 - - 40.0 - 40.0 Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0 TSPP 5.0 - - - - 5.0 2.5 - STPP 5.0 15.0 10.0 - - 7.0 8.0 10.0 Bentonite clay - 10.0 - - 5.0 - - - DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7 CMC - 1.0 1.0 1.0 1.0 - - 1.0 Talc - - 10.0 15.0 10.0 - - - Silicate - - 4.0 5.0 3.0 - - - PVNO 0.02 0.03 - 0.01 - 0.02 - - MA/AA 0.4 1.0 - - 0.2 0.4 0.5 0.4 SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3 Amylase - - 0.01 - - - 0.002 - AMG 0.01 0.1 0.02 0.002 0.5 0.01 0.01 0.002 Pullulanase - - - 0.001 - - 0.02 - Isoamylase - - - - - - 0.02 0.001 Protease . 0.004 _ 0.003 0.003 - - 0.003 I II III VI V III VI V Lipase - 0.002 - 0.002 . . . . Cellulase - .0003 - - .0003 .0002 PEO - 0.2 - 0.2 0.3 - - 0.3 Perfume 1.0 0.5 0.3 0.2 0.4 - - 0.4 Mg sulfate - - 3.0 3.0 3.0 - - - Brightener 0.15 0.1 0.15 - - - - 0.1 Photoactivated - 15.0 15.0 15.0 15.0 - - 15.0 bleach (ppm) Example 14 The following granular fabric detergent compositions which provide "softening through the wash" capability were prepared according to the present invention : I II C45AS - 10.0 LAS 7.6 - C68AS 1.3 - C45E7 4.0 - C25E3 - 5.0 Coco-alkyl-dimethyl hydroxy1.4 1.0 ethyl ammonium chloride Citrate 5.0 3.0 Na-SKS-6 - 11.0 Zeolite A 15.0 15.0 MA/AA 4.0 4.0 DETPMP 0.4 0.4 PB1 15.0 - Percarbonate - 15.0 TAED 5.0 5.0 Smectite clay 10.0 10.0 HMWPEO - 0.1 Protease 0.02 0.01 Lipase 0.02 0.01 AMG 0.05 0.02 Amylase 0.03 0.005 Cellulase 0.001 - Silicate 3.0 5.0 Carbonate 10.0 10.0 Suds suppressor 1.0 4.0 CMC 0.2 0.1 Miscellaneous and minors Up to 100% Example 15 The following rinse added fabric softener composition was prepared according to the present invention : DEQA (2) 20.0 Cellulase 0.001 AMG 0.005 HCL 0.03 Antifoam agent 0.01 Blue dye 25ppm CaCl2 0.20 Perfume 0.90 Miscellaneous and water Up to 100% Example 16 The following fabric softener and dryer added fabric conditioner compositions were prepared according to the present invention : I II III IV V DEQA 2.6 19.0 DEQA(2) . . . . 52.0 DTMAMS - - - 26.0 SDASA - - 70.0 42.0 40.2 I II III IV V Stearic acid of IV=0 0.3 C45E01-3 - - 13.0 HCL 0.02 0.02 Ethanol - - 1.0 Perfume 0.3 1.0 0.75 1.0 1.5 Glycoperse S-20 - - - - 15.4 Glycerol monostearate - - - 26.0 Digeranyl Succinate - - 0.38 Silicone antifoam 0.01 0.01 - - - Electrolyte - 0.1 - - - Amylase - 0.2 - 0.2 0.2 AMG 1.0 0.2 0.1 0.01 0.01 Clay - - - 3.0 - Dye lOppm 25ppm 0.01 - - Water and minors 100% 100% - - - Example 17 The following compact high density (0.96Kg/l) dishwashing detergent compositions were prepared according to the present invention : I II Ill IV V VI STPP - 51.0 51.0 - - 44.3 Citrate 17.0 - - 50.0 40.2 - Carbonate 17.5 14.0 20.0 - 8.0 33.6 Bicarbonate - - - 26.0 - - Silicate 15.0 15.0 8.0 - 25.0 3.6 Metasiiicate 2.5 4.5 4.5 - - - PB1 10.0 8.0 8.0 - - - PB4 - - - 10.0 - - Percarbonate - - - - 11.8 4.8 Nonionic 2.0 1.5 1.5 3.0 1.9 5.9 TAED 2.0 - - 4.0 - 1.4 HEDP 1.0 - - - - - DETPMP 0.6 - - - - - MnTACN . . - - 0.01 - IV V VI PAAC - 0.01 0.01 - - - Paraffin 0.5 0.4 0.4 0.6 - - Protease 0.07 0.05 0.05 0.03 0.06 0.01 Amylase 0.01 0.01 0.01 0.02 0.02 0.006 AMG 0.02 0.2 2.0 1.0 0.002 0.02 Pullulanase - - - - - 0.02 Lipase - 0.001 - 0.005 - - BTA 0.3 0.2 0.2 0.3 0.3 0.3 Polycarboxylate 6.0 - - - 4.0 0.9 Perfume 0.2 0.1 0.1 0.2 0.2 0.2 pH 11.0 11.0 11.3 9.6 10.8 10.9 Miscellaneous, sulfate and water Up to 100% Example 18 The following granular dishwashing detergent compositions of bulk density 1.02Kg/L were prepared according to the present invention : I II III IV V VI STPP 30.0 33.5 27.9 29.6 33.8 22.0 Carbonate 30.5 30.5 30.5 23.0 34.5 45.0 Silicate 7.0 7.5 12.6 13.3 3.2 6.2 Metasiiicate - 4.5 - - - - Percarbonate - - - - 4.0 - PB1 4.4 4.5 4.3 - - - NADCC - - - 2.0 - 0.9 Nonionic 1.0 0.7 1.0 1.9 0.7 0.5 TAED 1.0 - - - 0.9 - PAAC - 0.004 - - - - Paraffin 0.25 0.25 - - - - Protease 0.036 0.021 0.03 - 0.006 - Amylase 0.03 0.005 0.004 - 0.005 - AMG 0.2 0.02 2.0 2.0 0.02 0.005 Pullulanase - - - - - 0.002 Isoamylase - - - - - 0.01 Lipase 0.005 - 0.001 - - - BTA 0.15 0.15 - - 0.2 - I II III IV V VI Perfume 0.2 0.2 0.05 0.1 0.2 pH 10.8 11.3 11.0 10.7 11.5 10.9 Miscellaneous, sulfate and water Up to 100% Example 19 The following tablet detergent compositions were prepared according to the present invention by compression of a granular dishwashing detergent composition at a pressure of 13KN/cm2 using a standard 12 head rotary press: I II Ill IV V VI VII VIII STPP - 48.8 54.7 38.2 - 52.4 56.1 36.0 Citrate 20.0 - - - 35.9 - - - Carbonate 20.0 5.0 14.0 15.4 8.0 23.0 20.0 28.0 Silicate 15.0 14.8 15.0 12.6 23.4 2.9 4.3 4.2 Protease 0.042 0.072 0.042 0.031 0.052 0.023 0.023 0.029 Amylase 0.012 0.012 0.012 0.007 0.015 0.003 0.017 0.002 AMG 0.02 0.01 0.002 0.5 0.008 0.002 1.0 0.02 Pullulanase 0.002 - - 0.002 - - - 0.02 Isoamylase 0.001 - - - - 0.03 - - Lipase 0.005 - - - - - - - PB1 14.3 7.8 11.7 12.2 - - 6.7 8.5 PB4 - - - - 22.8 - 3.4 - Percarbonate - - - - - 10.4 - - Nonionic 1.5 2.0 2.0 2.2 1.0 4.2 4.0 6.5 PAAC - - 0.02 0.009 - - - - MnTACN - - - - 0.007 - - - TAED 2.7 2.4 - - - 2.1 0.7 1.6 HEDP 1.0 - - 0.9 - 0.4 0.2 - DETPMP 0.7 - - - - - - - Paraffin 0.4 0.5 0.5 0.5 - - 0.5 - BTA 0.2 0.3 0.3 0.3 0.3 0.3 0.3 - Polycarboxylate 4.0 - - - 4.9 0.6 0.8 - PEG 4,000- - - - - - 2.0 - 2.0 30,000 Glycerol - - - - - 0.4 - 0.5 I II III IV V VI VII VIII Perfume - - 0.05 0.2 0.2 0.2 0.2 Weight of tablet 20g 25g 20g 30g 18g 20g 25g 24g pH 10.7 10.6 10.7 10.7 10.9 11.2 11.0 10.8 Miscellaneous, sulfate and water Up to 100% I Example 20 The following liquid dishwashing detergent compositions of density 1.40Kg/L were prepared according to the present invention : I II III IV STPP 17.5 17.2 23.2 23.1 Carbonate - 2.4 - - Silicate 6.1 24.9 30.7 22.4 NaOCI 1.1 1.1 1.1 1.2 Thickener 1.0 1.1 1.1 1.0 Nonionic - 0.1 0.06 0.1 NaBz 0.7 - - - AMG 0.005 1.0 0.005 0.02 NaOH 1.9 - - - KOH 3.6 3.0 - - Perfume 0.05 - - - PH 11.7 10.9 10.8 11.0 Water up to 100% Example 21 The following dishwashing compositions in the tablet form were prepared according to the present invention (Levels are indicated in g): I II III IV V VI Phase 1 STPP 9.6 9.6 10.4 9.6 9.6 11.5 Silicate 0.5 0.7 1.6 1.0 1.0 2.4 SKS-6 1.5 1.50 2.30 2.25 Carbonate 2.3 2.7 3.5 3.6 4.1 5.2 HEDP 0.2 0.2 0.2 0.3 0.3 0.3 I II III IV V VI PB1 2.4 2.4 2.4 3.7 3.7 3.7 PAAC 0.002 0.002 0.002 0.003 0.004 0.004 AMG 0.01 0.02 0.05 0.002 0.001 1.0 Pullulanase - - 0.01 - - 0.02 Isoamylase - - - 0.01 - 0.01 Amylase 0.002 0.001 0.001 0.004 0.003 0.003 Protease 0.002 0.002 0.002 0.003 0.003 0.003 Nonionic 0.4 0.8 0.8 1.2 1.2 1.2 PEG 6000 0.4 0.3 0.3 0.4 0.4 0.4 BTA 0.04 0.04 0.04 - 0.06 0.06 Paraffin 0.1 0.1 0.1 0.15 0.15 0.15 Perfume 0.02 0.02 0.02 0.01 0.01 0.01 Sulphate - - - 0.5 0.05 2.3 Phase 2 AMG 0.003 0.003 0.002 0.01 0.01 0.01 Amylase 0.0005 0.0005 0.0004 0.0005 0.006 0.0004 Protease 0.009 0.008 0.01 0.009 0.008 0.01 Citric 0.3 0.3 0.3 0.30 Sulphamic acid - 0.3 - - 0.3 - Bicarbonate 1.1 0.4 0.4 1.1 0.4 0.4 Carbonate - 0.5 - - 0.5 - Silicate - - 0.6 - - 0.6 CaCI 2 - 0.07 - - 0.07 - PEG 3000 0.06 0.06 0.06 0.06 0.06 0.06 The multi-phase tablet compositions are prepared as follows. The detergent active composition of phase 1 is prepared by admixing the granular and liquid components and is then passed into the die of a conventional rotary press. The press includes a punch suitably shaped for forming the mould. The cross-section of the die is approximately 30x38 mm. The composition is then subjected to to a compression force of 940 kg/cm 2 and the punch is then elevated exposing the first phase of the tablet containing the mould in its upper surface. The detergent active composition of phase 2 is prepared in similar manner and is passed into the die. The particulate active composition is then subjected to a compression force of 170 kg/cm 2 , the punch is elevated, and the multi-phase tablet ejected from the tablet press. The resulting tablets dissolve or disintegrate in a washing machine as described above within 12 minutes, phase 2 of the tablets dissolving within 5 minutes. The tablets provide excellent dissolution and cleaning characteristics together with good tablet integrity and strength. Example 22 The following manual dishwashing compositions were prepared according to the present invention : I II Ill IV V VI VII VIII C12-14E0-3S 26.0 34.2 25.0 26.0 37.0 26.0 22.0 32.0 C11LAS - - - - - - 13.0 - C12-14 amine oxide 2.0 4.9 2.1 6.5 5.5 6.5 1 - C12-14 betaine 2.0 5.0 2.1 - - - - 4.0 C12-14 glucose amide 1.5 1.5 3.1 - - - - - C9-11E8-9 4.5 1 4.1 3.0 1.0 3.0 - 1.0 Alkyl Polyglucoside - - - - - - 12.0 3.0 C1 -20 Mono Ethanol - - - - - - 1.5 - Amine DTPA - 0.1 0 0-500 0-500 0-500 0 0 ppm ppm ppm Succinic acid - - - - - 0 - 4.5 Cumene sulphonate - - 4.5 1 to 6 - 1 to 6 - - Ca ou Na xyiene - 5.0 - - 4.0 - 2.5 - Sulphonate Mg salts (in % Mg) 0.5 0.7 0.5 0.04 0.6 0.04 0.3 0 1 ,3 bis (methylamino) - - - 0.5 - 0.5 - - cyclohexane N.N-dimethylamino - - - 0.2 - 0.2 - - ethyl methacrylate homopolymer Citric - - - 0-3.5 0-3.5 - - Ethanol 6-8 5-8 6-9 4-10 7.0 4-10 4.0 4.0 Protease - - - 0-0.08 - 0-0.08 - - AMG 0.05 .002 .005 0.01 0.4 0.05 0.002 0.01 Amylase - - - 0.002 - 0.005 0.04 0.05 I II III IV V VI VII VIII Carbonate - 2.5 Poly Propylene Glycol - - 0 to 2 (MW2000-4000) pH 7-8 7- 8 7-8 8.5-11 7-8 8.5-11 7 7 Perfume 0.1-0.7 Balance (water and minors) Up to 100% Example 23 The following fabric and hard surface cleaner composition was prepared according to the present invention : Sulphate 18.5 Bicarbonate 18.6 Polycarboxylate 4.1 C18 Alpha Olefin 0.2 Enzyme (lipase, protease and/or cellulase) 0.004 Amylase 0.003 AMG 0.05 Brigthener 2 0.1 Photoactivated bleach 0.04 Coated sodium percarbonate 45.0 TAED 8.8 Citric 2.5 Perfume 0.1 Miscellaneous and water up to 100%

Claims: CLAIMS 1 . A detergent composition comprising a detergent ingredient and an amyloglucosidase enzyme with the proviso that such composition does not comprise a glucose oxidase enzyme. 2. A detergent composition according to claim 1 wherein said amyloglucosidase enzyme is comprised at a level of from 0.0002% to 10%, preferably 0.002% to 2%, more preferably 0.002% to 1 % pure enzyme by weight of the total detergent composition. 3. A detergent composition according to claims 1-2 wherein said amyloglucosidase enzyme has or has been added a starch binding domain. 4. A detergent composition according to claims 1-3 further comprising an enzyme selected from a lipase, a protease, an enzyme from the amylase class and/or mixtures thereof, preferably an enzyme from the amylase class. 5. A detergent compositions according to claim 4 wherein said enzyme from the amylase class is selected from an α-amylase, a maltogenic alpha- amylase, a neopullulanase, a pullulanase type II, a dextrin dextranase, a cyclomaltodextrin transferase, a starch debranching enzyme and/or mixtures thereof 6. A detergent composition according to claim 5 wherein said starch debranching enzyme is selected from a pullulanase type I, an isoamylase, an isopullulanase and/or mixtures thereof. 7. A detergent composition according to claims 4-5 wherein said enzyme from the amylase class is selected from an α-amylase, a maltogenic alpha- amylase, a pullulanase type II, and/or mixtures thereof. 8. A detergent composition according to claim 7 further comprising a starch debranching enzyme, preferably an isoamylase. 9. A detergent composition according to any of the preceding claims wherein said detergent ingredient is selected from nonionic surfactants, bleaching agents, and/or mixtures thereof. 10. Use of an amyloglucosidase enzyme in a detergent composition for the hydrolysis of retrograded starch. 11. Use according to claim 10 for the removal of starch-containing stains and soils, and when formulated as laundry compositions, for excellent whiteness maintenance and dingy cleaning.

Inventors: SMETS JOHAN, SMETS, JOHAN
Applicants: PROCTER & GAMBLE, SMETS JOHAN, SMETS, JOHAN, THE PROCTER & GAMBLE COMPANY
Application year: 2000
Main classification: C11D3
IPC codes: C11D3, C11D17