MIXED PROTEASE ENZYME SYSTEMS FOR CLEANING PROTEIN BASED SOILS AND COMPOSITIONS INCORPORATING SAME

Abstract: The present invention comprises a cleaning composition, particularly an automatic dishwashing composition, comprising an effective amount of a protease enzyme cleaning system comprising the combination of at least one chymotrypsin-like protease enzyme and at least one trypsin-like protease enzyme, where the at least one chymotrypsin-like protease has an enzyme activity ratio of sAAPF-pNA activity/bVGR-pNA activity of at least about 15 and the trypsin-like protease enzyme having an enzyme activity ratio of sAAPF-pNA activity/bVGR-pNA activity of less than about 10.0; and cleaning adjunct materials.

Description: MIXED PROTEASE ENZYME SYSTEMS FOR CLEANING PROTEIN BASED SOILS AND COMPOSITIONS INCORPORATING SAME FIELD OF THE INVENTION The present invention relates to mixed protease enzymes for cleaning protein based soils via various compositions and methods for their use. More particularly, this invention relates to combinations of protease enzymes for tough food cleaning and reduced spotting and filming in automatic dishwashing compositions. BACKGROUND OF THE INVENTION Various types of enzymes have long been used in laundry detergents to assist in the removal of certain stains from fabrics. Each class of enzyme (amylase, protease, etc.) generally catalyzes a different chemical reaction. For example, protease enzymes are known for their ability to hydrolyze (break down a compound into two or more simpler compounds) other proteins. This ability has been taken advantage of through the incorporation of naturally occurring or engineered protease enzymes to laundry detergent compositions. In recent years the use of enzymes has also been investigated for automatic dishwashing where consumers desire cleaning without spotting and filming of glasses and dishes. Unfortunately, many enzymes, especially protease enzymes, do not translate well into the wash environment. Specifically, thermal stability, pH stability, oxidative stability and substrate specificity need to be optimized to ensure satisfactory performance. Additionally, consumers interest in automatic dishwashing compositions which deliver tough food cleaning is increasing. Dairy products and cartenoid stains on ceramics and plastics have long been difficult to remove via automatic dishwashing. Removal of milk-based soils, such as pudding, cheese and milk, has also been problematic. Accordingly, the need remains for compositions which can deliver tough cleaning without spot/film formation. More particularly, the need remains for automatic dishwashing compositions which can deliver tough food cleaning and reduced spot/film formation via protease enzymes systems designed to deliver such benefits. BACKGROUND ART The following documents contain information which may or may not be relevant to the present invention: WO 95/10615 to Genecor International, Inc.; WO 89/06270 to Novo Nordisk A/S; Kirk-Othmer, Encyclopedia of Chemical Technology, 4th. Ed., Vol. 9, Wiley 1994, pages 567-620, titled "Enzyme Applications-Industrial", Nielsen et al and the references therein. WO 95/10591 and WO 95/10592 to the Procter & Gamble Company. SUMMARY OF THE INVENTION This need is met via the present invention whereby compositions having a protease enzyme system capable of tough food cleaning and reduced spotting/filming are provided. In particular, the present invention provides an protease enzyme system that is particularly effective at cleaning protein based soils, and particular in automatic dishwashing compositions without developing spotting/filming problems. The invention comprises the combination of at least one enzyme having chymotrypsin-like specificity with at least one enzyme having trypsin-like specificity. Trypsin-like and chymotrypsin-like refer to proteases which have specificity profiles similar to the enzymes Trypsin and Chymotrypsin. That is, a trypsin-like protease enzyme refers to an enzyme that hydrolyzes proteins by preferentially cleaving the peptide bonds of charged amino acid residues, more specifically residues such as arginine and lysine, rather than preferentially cleaving the peptide bonds of hydrophobic amino acid residues, more specifically phenylalanine, tryptophan and tyrosine. Enzymes having the latter profile are referred to as having a chymotrypsin-like specificity. Thus, the present invention involves mixed protease enzyme systems having at least one trypsin-like protease and at least one chymotrypsin-like protease to deliver superior cleaning and spotting/filming benefits. According to a first embodiment of the present invention, a cleaning composition is provided. The cleaning composition comprises: a) from about 0.0001% to about 10% by weight of the composition of a protease enzyme cleaning system comprising the combination of at least one chymotrypsin-like protease enzyme and at least one trypsin-like protease enzyme, where the at least one chymotrypsin-like protease has an enzyme activity ratio of sAAPF-pNA (N-succinyl-ala-ala-pro-phe-p-Nitroanilide, hereinafter suc-AAPF- pNA) activity /bVGR-pNA (benzyl-val-ara-lys-p-Nitroanilide, hereinafter bVGR4 pNA) activity of at least about 15 and the trypsin-like protease enzyme has an enzyme activity ratio of sAAPF-pNA activity /bVGR-pNA activity of less than about 10.0; and (b) from about 0.1% to about 99% by weight of the composition of cleaning adjunct materials. In preferred embodiments, the chymotrypsin-like protease enzyme has an enzyme activity ratio of sAAPF-pNA activity /bVGR-pNA activity of at least about 17.5 and the trypsin-like protease enzyme has an enzyme activity ratio of sAAPF- pNA activity/bVGR-pNA activity of less than about 8.0. The chymotrypsin-like enzyme is preferably a carbonyl hydrolase variant having an amino acid sequence not found in nature with the carbonyl hydrolase being derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a position in the carbonyl hydrolase equivalent to position +76, and at least one position being selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +195, +197, +204, +206, +216, +217, +218, +222, +260, +265, +274 and mixtures thereof according to the numbering of Bacillus amyloliquefaciens subtilisin with positions +76, +103 and +104 being the most preferred. The trypsin-like protease enzyme is preferably either the protease enzyme obtained from Bacillus Lentus or 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 precursor carbonyl hydrolase equivalent to position +210 in combination with one or more amino acid residue position equivalent to those selected from the group consisting of +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 in Bacillus amyloliquefaciens subtilisin with positions +210, +76, +103, +104, +156, and +166 being most preferred. In preferred embodiments the weight ratio of the chymotrypsin-like protease enzyme to the trypsin-like protease enzyme is from about 0.5:1 to about 10:1 and more preferably from about 1:1 to about 5:1. In optional embodiments, an amylase enzyme may be included or the cleaning adjunct ingredients are selected from the group consisting of builders, silicates, low-foaming nonionic surfactants, peroxide bleach sources, bleach activators, bleach catalysts and mixtures thereof. In a second embodiment of the present invention, an automatic dishwashing composition having improved spotting/filming benefits is provided. The automatic dishwashing composition comprises the protease enzyme system substantially as described above or in preferred embodiments an automatic dishwashing composition comprising: a) from about 0.0001% to about 10% by weight of the composition of a protease enzyme cleaning system comprising the combination of at least one chymotrypsin-like protease enzyme and at least one trypsin-like protease enzyme with the at least one chymotrypsin-like protease having an enzyme activity ratio of sAAPF-pNA activity /bVGR-pN A activity of at least about 15 and the trypsin-like protease enzyme having an enzyme activity ratio of sAAPF-pNA activity bVGR- pNA activity of less than about 10.0; (b) from about 0.1% to about 20% by weight of the composition of a low foaming nonionic surfactant; (c) from about 10% to about 50% by weight of the composition of SL detergency builder; and (d) from about 0.0005% to about 30% by weight of the composition of a bleaching agent. In yet another embodiment according to the present invention, a method for cleaning dishes while preventing spotting or filming on the dishes comprising providing soiled dishes having milk-based food soils and treating the dishes with the compositions as disclosed above. Accordingly, it is an object of the present invention to provide a protease enzyme system which delivers superior cleaning performance yet also provides superior spotting and filming benefits. It is a further object of the present invention to provide a cleaning composition including this superior protease enzyme system. It is a further object of the present invention to provide an automatic dishwashing composition including the protease enzyme system. And, it is still further an object of the present invention to provide a method for cleaning dishes by employing the superior protease enzyme system. These, and other, objects, features and advantages will be clear from the following detailed description and the appended claims. All percentages, ratios and proportions herein are on a weight basis unless otherwise indicated. All documents cited herein are hereby incorporated by reference. DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENTS Protease Enzyme System: The present invention involves a mixed protease enzyme system that is designed to deliver superior performance benefits in an automatic dishwashing environment. The mixed protease enzyme system involves the use of at least two different classes of protease enzyme. The first class is that of chymotrypsin-like protease enzymes. That is, protease enzymes which hydrolyze proteins by preferentially cleaving the peptide bonds of hydrophobic amino acid residues such as, for example, phenylalanine, tryptophan and tyrosine. These chymotryptic-like proteases are used in conjunction with the second class of protease enzyme, the trypsin-like proteases. Trypsin-like protease enzymes hydrolyze proteins by preferentially cleaving the peptide bonds of charged amino acid residues, such as arginine and lysine. The combination of enzymes from these two classes of protease provides a superior enzyme cleaning system for the automatic dishwashing environment. Substrate specificity, as discussed above, is generally illustrated by the action of an enzyme on two synthetic substrates. An enzyme is placed in a solution with one of the two synthetic substrates. The capability of the enzyme in question to hydrolyze the synthetic substrate is then measured. For the purposes of the present invention, the synthetic substrates employed to measure the specificity of the enzymes of the present invention are the synthetic substrate suc-AAPF-pNA and the synthetic substrate bVGR-pNA, both of which are available from SIGMA Chemicals. Both of these synthetic substrates are well-known to one of ordinary skill in the art. A protease in the class of enzymes having trypsin-like specificity preferentially hydrolyze the synthetic substrate bVGR-pNA but hydrolyze the synthetic substrate sucAAPF-pNA to a much lesser extent. Conversely, chymotrypsin-like protease enzymes preferentially hydrolyze the synthetic substrate bVGR-pNA but hydrolyze suc-AAPF-pNA to a much lesser extent. The overall specificity of a protease enzyme can then be determined by measuring that enzyme's specificity against each of the synthetic substrates and then taking a ratio of that enzyme's activity on the two synthetic substrates. Accordingly, for the purposes of the present invention, the activity specificity ratio is determined by the formula: [activity on suc-AAPF-pNA]/[activity on bVGR-pNA] An enzyme having a ratio of less than about 10, more preferably less than about 8 and most preferably less than about 7 may then be considered to demonstrate trypsin-like specificity for the purposes of the present invention while an enzyme having a ratio greater than about 15, preferably greater than about 17.5 and most preferably greater than about 20 may be considered to demonstrate chymotrypsin- like specificity for the purposes of the present invention. Specificity Measurement For the purposes of the present invention, specificity is measured and determined against the two synthetic substrates as detailed above. The following test was employed. A 5 mis of a Trisma buffer at a pH of 8.6 (prepared from a combination of 12.109 g Tris Base (0.1M), 1.471 g CaCl 2 «2H 2 O (0.01 M), 3.1622 g NaS 2 O 3 (0.02 M) pH adjusted with IN H2SO4) and a temperature of 25 °C is added to a standard 10 ml test tube. 0.5 ppm of the active enzyme in a pH 10 glycine buffer to be tested in a 1M glycine buffer is added to the test tube. Approximately, 1.25 mg of the synthetic substrate per mL of buffer solution is added to the test tube. The • mixture is allowed to incubate for 15 minutes at 25 °C. Upon completion of the incubation period, an enzyme inhibitor, PMSF, is added to the mixture at a level of 0.5 mg per mL of buffer solution. The absorbency or OD value of the mixture is determined on a Gilford Response UV spectrometer, Model # 1019 read at a visible light 410 nm wavelength. The absorbance then indicates the activity of the enzyme on the synthetic substrate. The greater the absorbance, the higher the level of activity against that substrate. Accordingly, absorbance is equal to enzyme activity for purposes of the present invention. The mixed protease enzyme system of the present invention is employed in compositions at higher-end levels of from less than about 10%, more preferably less than about 5% and even more preferably less than about 2% and at lower-end levels of from greater than about 0.0001%, more preferably greater than about 0.1% and even more preferably greater than about 0.5% by weight of the composition. As for within the system itself, the ratio of chymotrypsin-like protease enzyme to trypsin- like protease enzyme ranges from about 0.5:1 to about 10:1, and more preferably from about 2:1 to about 5:1 and most preferably from about 1:1 to about 3:1. Also preferably the protease enzyme is present in the compositions in an amount sufficient to provide a ratio of mg of active protease per 100 grams of composition to ppm theoretical Available O 2 ("AvO 2 ") from any peroxyacid in the wash liquor, referred to herein as the Enzyme to Bleach ratio (E/B ratio), ranging from about 1 : 1 to about 20: 1. Several examples of various cleaning compositions wherein the protease enzymes may be employed are discussed in further detail below. Chymotrypsin-like Enzymes The chymotrypsin-like enzymes, according to the present invention, are those which have an activity ratio, as defined above, of greater than about 15. Particularly, preferred for this class of enzyme are non-naturally-occurring carbonyl hydrolase variants having an amino acid sequence not found in nature, which is derived by replacement of a plurality of amino acid residues corresponding to position +76 in combination with one or more of the following residues +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +195, +197, +204, +206, +216, +217, +218, +222, +260, +265, and/or +274 of a precursor carbonyl hydrolase with different amino acids, where the numbered position corresponds to naturally-occurring subtilisin from Bacillus amyloliquefaciens or to equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin. The carbonyl hydrolase variants which are preferred chymotrypsin-like protease enzymes useful in the present invention compositions comprise replacement of amino acid residue in the following combinations: 76/99; 76/101; 76/103; 76/104; 76/107; 76/123; 76/99/101; 76/99/103; 76/99/104; 76/101/103; 76/101/104; 76/103/104; 76/104/107; 76/104/123; 76/107/123; 76/99/101/103; 76/99/101/104; 76/99/103/104; 76/101/103/104; 76/103/104/123; 76/104/107/123; 76/99/101/103/104; 76/99/103/104/123 and/or 76/99/101/103/104/123. Most preferably the variant enzymes useful for the present invention comprise the substitution, deletion or insertion of an amino acid residue in the following combination of residues: 76/99; 76/104; 76/99/104; 76/103/104; 76/104/107; 76/101/103/104; 76/99/101/103/104 and 76/101/104 of B. Lentus subtilisin with 76/103/104 being the most preferred. Such enzymes are fully described in U.S. Patent Application Serial Nos. 08/322,676 and 08/322,677, and in WO 95/10615 published April 20, 1995 by Genencor International, the disclosures of which are herein incorporated by reference. Other chymotrypsin-like protease enzymes suitable for use in the present invention include those 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® from Novo as well as the proteases known as BPN' and Carlsberg. Trypsin-like Enzymes The trypsin-like enzymes, according to the present invention, are those which have an activity ratio, as defined above, of less than about 10. Particularly suitable protease enzymes meeting the above requirement include microbial alkaline proteinases such as the protease enzyme obtained from Bacillus Lentus subtilisin and commercially available under the tradenames SAVINASE® from Novo and PURAFECT® from Genencor International. Other particularly preferred trypsin-like protease enzymes according to the present invention include those which are non-naturally-occurring carbonyl hydrolase variants which are derived by replacement of a plurality of amino acid residues of a precursor carbonyl hydrolase 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 subtilisin from Bacillus amyloliquefaciens or to • equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin with different amino acids. The preferred variant protease enzymes useful for the present invention comprise the substitution, deletion or insertion of amino acid residues in the following combinations: 210/156; 210/166; 210/76; 210/103; 210/104; 210/217; 210/156/166; 210/156/217; 210/166/217; 210/76/156; 210/76/166; 210/76/217; 210/76/156/166; 210/76/156/217; 210/76/166/217; 210/76/103/156; 210/76/103/166; 210/76/103/217; 210/76/104/156; 210/76/104/166; 210/76/104/217; 210/76/103/104/156; 210/76/103/104/166; 210/76/103/104/217; 210/76/103/104/156/166; 210/76/103/104/156/217; 210/76/103/104/166/217 and/or 210/76/103/104/156/166/217; 210/76/103/104/166/222; 210/67/76/103/104/166/222; 210/67/76/103/104/166/218/222. Most preferably the variant enzymes useful for the present invention comprise the substitution, deletion or insertion of an amino acid residue in the following combination of residues: 210/156; 210/166; 210/217; 210/156/166; 210/156/217; 210/166/217; 210/76/156/166; 210/76/103/156/166 and 210/76/103/104/156/166 of B. lentus subtilisin with 210/76/103/104/156/166 being the most preferred. The protease enzymes useful herein encompass the substitution of any of the nineteen naturally occurring L-amino acids at the designated amino acid residue positions. Such substitutions can be made in any precursor subtilisin (procaryotic, eucaryotic, mammalian, etc.). Throughout this application reference is made to various amino acids by way of common one- and three-letter codes. Such codes are identified in Dale, M.W. (1989), Molecular Genetics of Bacteria. John Wiley & Sons, Ltd., Appendix B. Preferably, the substitution to be made at each of the identified amino acid residue positions, include but are not limited to, substitutions at position +210 including I, V, L, and A, substitutions at positions +33, +62, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, and +218 of D or E, substitutions at position 76 including D, H, E, G, F, K, P and N; substitutions at position 103 including Q, T, D, E, Y, K, G, R and S; and substitutions at position 104 including S, Y, I, L, M, A, W, D, T, G and V; and substitutions at position 222 including S, C, A. Trypsin-like enzymes as described above are fully disclosed in U.S. Patent Application Serial No. , entitled "PROTEASE ENZYMES FOR TOUGH CLEANING AND COMPOSITIONS INCORPORATING SAME" to Rai et al (P&G Docket No ), filed June _, 1997. Accordingly, the protease enzyme system of the present invention provides • superior cleaning benefits, such as tough food cleaning, as well as superior spotting and filming benefits in automatic dishwashing. These benefits are particularly evident in compositions which also contain an oxygen bleaching system. Cleaning Adjunct Materials: The cleaning compositions of the present invention also comprise, in addition to the protease enzyme system described hereinbefore, one or more cleaning adjunct materials compatible with the protease enzyme. The term "cleaning adjunct materials", as used herein, means any liquid, solid or gaseous material selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid; granule; spray composition), which materials are also compatible with the protease enzyme system used in the composition. The specific selection of cleaning adjunct materials are readily made by considering the surface, item or fabric to be cleaned, and the desired form of the composition for the cleaning conditions during use (e.g., through the wash detergent use). The term "compatible", as used herein, means the cleaning composition materials do not reduce the proteolytic activity of the protease enzyme system to such an extent that the protease is not effective as desired during normal use situations. Specific cleaning composition materials are exemplified in detail hereinafter. An effective amount of the protease enzyme system described above is included in compositions useful for cleaning a variety of surfaces in need of proteinaceous stain removal. Such cleaning compositions include detergent compositions for cleaning hard surfaces, unlimited in form (e.g., liquid and granular); detergent compositions for cleaning fabrics, unlimited in form (e.g., granular, liquid and bar formulations); dishwashing compositions (unlimited in form and including both granular and liquid automatic dishwashing); oral cleaning compositions, unlimited in form (e.g., dentifrice, toothpaste and mouthwash formulations); and denture cleaning compositions, unlimited in form (e.g., liquid, tablet). As used herein, "effective amount of protease enzyme system" refers to the quantity of protease enzyme system described hereinbefore necessary to achieve the enzymatic activity necessary in the specific cleaning composition. Such effective amounts are readily ascertained by one of ordinary skill in the art and is based on many factors, such as the particular enzyme variant used, the cleaning application, the specific composition of the cleaning composition, and whether a liquid or dry (e.g., granular, bar) composition is required, and the like. The compositions of the present invention typically include from about 1% to about 99.9% by weight of the composition of the adjunct materials. Optional Detersive Enzymes Enzymes, in addition to the herinbefore described protease enzyme system, can be included in the present compositions for a variety of purposes, including removal of protein-based, carbohydrate-based, or triglyceride-based stains from surfaces such as textiles or dishes, for the prevention of refugee dye transfer, for example in laundering, and for fabric restoration. Suitable enzymes include additional proteases, amylases, lipases, cellulases, peroxidases, and mixtures thereof of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Preferred selections are influenced by factors such as pH-activity and/or stability optima, thermostability, and stability to active detergents, builders and the like. In this respect bacterial or fungal enzymes are preferred, such as bacterial amylases and proteases, and fungal cellulases. "Detersive enzyme", as used herein, means any enzyme having a cleaning, stain removing or otherwise beneficial effect in a laundry, hard surface cleaning or personal care detergent composition. Preferred detersive enzymes are hydrolases such as proteases, amylases and lipases. Preferred enzymes for laundry purposes include, but are not limited to, proteases, cellulases, lipases and peroxidases. Highly preferred for automatic dishwashing are amylases and/or proteases, including both current commercially available types and improved types which, though more and more bleach compatible though successive improvements, have a remaining degree of bleach deactivation susceptibility. Enzymes are normally incorporated into detergent or detergent additive compositions at levels sufficient to provide a "cleaning-effective amount". The term "cleaning effective amount" refers to any amount capable of producing a cleaning, stain removal, soil removal, whitening, deodorizing, or freshness improving effect on substrates such as fabrics, dishware and the like. In practical terms for current commercial preparations, typical amounts are up to about 5 mg by weight, more typically 0.01 mg to 3 mg, of active enzyme per gram of the detergent composition. Stated otherwise, the compositions herein will typically comprise from 0.001% to 10%), preferably 0.01 %-5% by weight of a commercial enzyme preparation. Protease enzymes are usually present in such commercial preparations at levels sufficient to provide from 0.005 to 0.1 Anson units (AU) of activity per gram of composition. For certain detergents, such as in automatic dishwashing, it may be desirable to increase the active enzyme content of the commercial preparation in order to minimize the total amount of non-catalytically active materials and thereby improve spotting/filming or other end-results. Higher active levels may also be desirable in highly concentrated detergent formulations. Amylases suitable herein, especially for, but not limited to automatic dishwashing purposes, include, for example, α-amylases described in GB 1,296,839 to Novo; RAPIDASE®, International Bio-Synthetics, Inc. and TERMAMYL®, Novo. FUNGAMYL® from Novo is especially useful. Engineering of enzymes for improved stability, e.g., oxidative stability, is known. See, for example J. Biological Chem., Vol. 260, No. 11, June 1985, pp 6518-6521. Certain preferred embodiments of the present compositions can make use of amylases having improved stability in detergents such as automatic dishwashing types, especially improved oxidative stability as measured against a reference-point of TERMAMYL® in commercial use in 1993. These preferred amylases herein share the characteristic of being "stability- enhanced" amylases, characterized, at a minimum, by a measurable improvement in one or more of: oxidative stability, e.g., to hydrogen peroxide / tetraacetylethylenediamine in buffered solution at pH 9-10; thermal stability, e.g., at common wash temperatures such as about 60°C; or alkaline stability, e.g., at a pH from about 8 to about 11.5, measured versus the above-identified reference-point amylase. Stability can be measured using any of the art-disclosed technical tests. See, for example, references disclosed in WO 9402597. Stability-enhanced amylases can be obtained from Novo or from Genencor International. One class of highly preferred amylases herein have the commonality of being derived using site-directed mutagenesis from one or more of the Baccillus amylases, especially the Bacillus a- amylases, regardless of whether one, two or multiple amylase strains are the immediate precursors. Oxidative stability-enhanced amylases vs. the above- identified reference amylase are preferred for use, especially in bleaching, more preferably oxygen bleaching, as distinct from chlorine bleaching, detergent compositions herein. Such preferred amylases include (a) an amylase according to the hereinbefore incoφorated WO 9402597, Novo, Feb. 3, 1994, as further illustrated by a mutant in which substitution is made, using alanine or threonine, preferably threonine, of the methionine residue located in position 197 of the B.licheniformis alpha-amylase, known as TERMAMYL®, or the homologous position variation of a similar parent amylase, such as B. amyloliquefaciens, B. subtil is, or B.stearothermophilus; (b) stability-enhanced amylases as described by Genencor International in a paper entitled "Oxidatively Resistant alpha- Amylases" presented at the 207th American Chemical Society National Meeting, March 13-17 1994, by C. Mitchinson. Therein it was noted that bleaches in automatic dishwashing detergents inactivate alpha-amylases but that improved oxidative stability amylases have been made by Genencor from B.licheniformis NCIB8061. Methionine (Met) was identified as the most likely residue to be modified. Met was substituted, one at a time, in positions 8, 15, 197, 256, 304, 366 and 438 leading to specific mutants, particularly important being M197L and M197T with the M197T variant being the most stable expressed variant. Stability was measured in CASCADE® and SUNLIGHT®; (c) particularly preferred amylases herein include amylase variants having additional modification in the immediate parent as described in WO 9510603 A and are available from the assignee, Novo, as DURAMYL®. Other particularly preferred oxidative stability enhanced amylase include those described in WO 9418314 to Genencor International and WO 9402597 to Novo. Any other oxidative stability-enhanced amylase can be used, for example as derived by site-directed mutagenesis from known chimeric, hybrid or simple mutant parent forms of available amylases. Other preferred enzyme modifications are accessible. See WO 9509909 A to Novo. Cellulases usable herein include both bacterial and fungal types, preferably having a pH optimum between 5 and 9.5. U.S. 4,435,307, Barbesgoard et al, March 6, 1984, discloses suitable fungal cellulases from Humicola insolens or Humicola strain DSM1800 or a cellulase 212-producing fungus belonging to the genus Aeromonas, and cellulase extracted from the hepatopancreas of a marine mollusk, Dolabella Auricula Solander. Suitable cellulases are also disclosed in GB-A- 2.075.028; GB-A-2.095.275 and DE-OS-2.247.832. CAREZYME® (Novo) is especially useful. See also WO 9117243 to Novo. Suitable lipase enzymes for detergent usage include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in GB 1,372,034. See also lipases in Japanese Patent Application 53,20487, laid open Feb. 24, 1978. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano," or "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 Coφ., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. LIPOLASE® enzyme derived from Humicola lanuginosa and commercially available from Novo, see also EP 341,947, is a preferred lipase for use herein. Lipase and amylase variants stabilized against peroxidase enzymes are described in WO 9414951 A to Novo. See also WO 9205249 and RD 94359044. Cutinase enzymes suitable for use herein are described in WO 8809367 A to Genencor. Peroxidase enzymes may be used in combination with oxygen sources, e.g., percarbonate, perborate, hydrogen peroxide, etc., for "solution bleaching" or prevention of transfer of dyes or pigments removed from substrates during the wash to other substrates present in the wash solution. Known peroxidases include horseradish peroxidase, ligninase, and haloperoxidases such as chloro- or bromo- peroxidase. Peroxidase-containing detergent compositions are disclosed in WO 89099813 A, October 19, 1989 to Novo and WO 8909813 A to Novo. A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A to Genencor International, WO 8908694 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 stabilized by various techniques. Enzyme stabilization 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 stabilization systems are also described, for example, in U.S. 3,519,570. A useful Bacillus, sp. AC 13 giving proteases, xylanases and cellulases, is described in WO 9401532 A to Novo. Enzyme Stabilizing System Enzyme-containing, including but not limited to, liquid compositions, herein may comprise from about 0.001% to about 10%, preferably from about 0.005%) to about 8%, most preferably from about 0.01%) to about 6%, by weight of an enzyme stabilizing system. The enzyme stabilizing system can be any stabilizing system which is compatible with the detersive enzyme. Such a system may be inherently provided by other formulation actives, or be added separately, e.g., by the formulator or by a manufacturer of detergent-ready enzymes. Such stabilizing systems can, for example, comprise calcium ion, boric acid, propylene glycol, short chain carboxylic acids, boronic acids, and mixtures thereof, and are designed to address different stabilization problems depending on the type and physical form of the detergent composition. One stabilizing approach is the use of water-soluble sources of calcium and/or magnesium ions in the finished compositions which provide such ions to the enzymes. Calcium ions are generally more effective than magnesium ions and are preferred herein if only one type of cation is being used. Typical detergent compositions, especially liquids, will comprise from about 1 to about 30, preferably from about 2 to about 20, more preferably from about 8 to about 12 millimoles of calcium ion per liter of finished detergent composition, though variation is possible depending on factors including the multiplicity, type and levels of enzymes incorporated. Preferably water-soluble calcium or magnesium salts are employed, including for example calcium chloride, calcium hydroxide, calcium formate, calcium malate, calcium maleate, calcium hydroxide and calcium acetate; more generally, calcium sulfate or magnesium salts corresponding to the exemplified calcium salts may be used. Further increased levels of Calcium and/or Magnesium may of course be useful, for example for promoting the grease-cutting action of certain types of surfactant. Another stabilizing approach is by use of borate species. See Severson, U.S. 4,537,706. Borate stabilizers, when used, may be at levels of up to 10% or more of the composition though more typically, levels of up to about 3% by weight of boric acid or other borate compounds such as borax or orthoborate are suitable for liquid detergent use. Substituted boric acids such as phenylboronic acid, butaneboronic acid, p-bromophenylboronic acid or the like can be used in place of boric acid and reduced levels of total boron in detergent compositions may be possible though the use of such substituted boron derivatives. Stabilizing systems of certain cleaning compositions, for example automatic dishwashing compositions, may further comprise from 0 to about 10%, preferably from about 0.01% to about 6% by weight, of chlorine bleach scavengers, added to prevent chlorine bleach species present in many water supplies from attacking and inactivating the enzymes, especially under alkaline conditions. While chlorine levels in water may be small, typically in the range from about 0.5 ppm to about 1.75 ppm, the available chlorine in the total volume of water that comes in contact with the enzyme, for example during dish- or fabric-washing, can be relatively large; accordingly, enzyme stability to chlorine in-use is sometimes problematic. Since perborate or percarbonate, which have the ability to react with chlorine bleach, may be present in certain of the instant compositions in amounts accounted for separately from the stabilizing system, the use of additional stabilizers against chlorine, may, most generally, not be essential, though improved results may be obtainable from their use. Suitable chlorine scavenger anions are widely known and readily available, and, if used, can be salts containing ammonium cations with sulfite, bisulfite, thiosulfite, thiosulfate, iodide, etc. Antioxidants such as carbamate, ascorbate, etc., organic amines such as ethylenediaminetetracetic acid (EDTA) or alkali metal salt thereof, monoethanolamine (MEA), and mixtures thereof can likewise be used. Likewise, special enzyme inhibition systems can be incoφorated such that different enzymes have maximum compatibility. Other conventional scavengers such as bisulfate, nitrate, chloride, sources of hydrogen peroxide such as sodium perborate tetrahydrate, sodium perborate monohydrate and sodium percarbonate, as well as phosphate, condensed phosphate, acetate, benzoate, citrate, formate, lactate, malate, tartrate, salicylate, etc., and mixtures thereof can be used if desired. In general, since the chlorine scavenger function can be performed by ingredients separately listed under better recognized functions, (e.g., hydrogen peroxide sources), there is no absolute requirement to add a separate chlorine scavenger unless a compound performing that function to the desired extent is absent from an enzyme-containing embodiment of the invention; even then, the scavenger is added only for optimum results. Moreover, the formulator will exercise a chemist's normal skill in avoiding the use of any enzyme scavenger or stabilizer which is majorly incompatible, as formulated, with other reactive ingredients, if used. In relation to the use of ammonium salts, such salts can be simply admixed with the detergent composition but are prone to adsorb water and/or liberate ammonia during storage. Accordingly, such materials, if present, are desirably protected in a particle such as that described in US 4,652,392, Baginski et al. Detergent Salts The present invention may include a suitable builder or detergency salt. The level of detergent salt/builder can vary widely depending upon the end use of the composition and its desired physical form. When present, the compositions will typically comprise at least about 1% builder and more typically from about 10% to about 80%, even more typically from about 15% to about 50%) by weight, of the builder. Lower or higher levels, however, are not meant to be excluded. Inorganic or P-containing detergent salts include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates (exemplified by the tripolyphosphates, pyrophosphates, and glassy polymeric meta- phosphates), phosphonates, phytic acid, silicates, carbonates (including bicarbonates and sesquicarbonates), sulphates, and aluminosilicates. However, non-phosphate salts are required in some locales. Importantly, the compositions herein function even in the presence of the so-called "weak" builders (as compared with phosphates) such as citrate, or in the so-called "underbuilt" situation that may occur with zeolite or layered silicate builders. Examples of silicate builders are the alkali metal silicates, particularly those having a SiO 2 :Na 2 O ratio in the range 1.6:1 to 3.2:1 and layered silicates, such as the layered sodium silicates described in U.S. Patent 4,664,839, issued May 12, 1987 to H. P. Rieck. NaSKS-6 is the trademark for a crystalline layered silicate marketed by Hoechst (commonly abbreviated herein as "SKS-6"). Unlike zeolite builders, the Na SKS-6 silicate builder does not contain aluminum. NaSKS-6 has the delta-Na 2 Siθ5 moφhology form of layered silicate. It can be prepared by methods such as those described in German DE-A-3 ,417,649 and DE-A-3,742,043. SKS-6 is a highly preferred layered silicate for use herein, but other such layered silicates, such as those having the general formula NaMSi x O x +ι-yH 2 O wherein M is sodium or hydrogen, x is a number from 1.9 to 4, preferably 2, and y is a number from 0 to 20, preferably 0 can be used herein. Various other layered silicates from Hoechst include NaSKS-5, NaSKS-7 and NaSKS-11, as the alpha, beta and gamma forms. As noted above, the delta-Na 2 Siθ5 (NaSKS-6 form) is most preferred for use herein. Other silicates may also be useful such as for example magnesium silicate, which can serve as a crispening agent in granular formulations, as a stabilizing agent for oxygen bleaches, and as a component of suds control systems. Examples of carbonate salts as builders are the alkaline earth and alkali metal carbonates as disclosed in German Patent Application No. 2,321,001 published on November 15, 1973. Aluminosilicate builders may also be added to the present invention as a detergent salt. Aluminosilicate builders are of great importance in most currently marketed heavy duty granular detergent compositions. Aluminosilicate builders include those having the empirical formula: M z (zAlO 2 ) y ]-xH 2 O wherein z and y are integers of at least 6, the molar ratio of z to y is in the range from 1.0 to about 0.5, and x is an integer from about 15 to about 264. Useful aluminosilicate ion exchange materials are commercially available. These aluminosilicates can be crystalline or amoφhous in structure and can be naturally-occurring aluminosilicates or synthetically derived. A method for producing aluminosilicate ion exchange materials is disclosed in U.S. Patent 3,985,669, Krummel, et al, issued October 12, 1976. Preferred synthetic crystalline aluminosilicate ion exchange materials useful herein are available under the designations Zeolite A, Zeolite P (B), Zeolite MAP and Zeolite X. In an especially preferred embodiment, the crystalline aluminosilicate ion exchange material has the formula: Na 12 [(AlO 2 )ι 2 (SiO 2 ) 12 ]-xH 2 O wherein x is from about 20 to about 30, especially about 27. This material is known as Zeolite A. Dehydrated zeolites (x = 0 - 10) may also be used herein. Preferably, the aluminosilicate has a particle size of about 0.1-10 microns in diameter. Organic detergent builders suitable for the piuposes of the present invention include, but are not restricted to, a wide variety of polycarboxylate compounds. As used herein, "polycarboxylate" refers to compounds having a plurality of carboxylate groups, preferably at least 3 carboxylates. Polycarboxylate builder can generally be added to the composition in acid form, but can also be added in the form of a neutralized salt. When utilized in salt form, alkali metals, such as sodium, potassium, and lithium, or alkanolammonium salts are preferred. Included among the polycarboxylate builders are a variety of categories of useful materials. One important category of polycarboxylate builders encompasses the ether polycarboxylates, including oxydisuccinate, as disclosed in Berg, U.S. Patent 3,128,287, issued April 7, 1964, and Lamberti et al, U.S. Patent 3,635,830, issued January 18, 1972. See also "TMS/TDS" builders of U.S. Patent 4,663,071, issued to Bush et al, on May 5, 1987. Suitable ether polycarboxylates also include cyclic compounds, particularly alicyclic compounds, such as those described in U.S. Patents 3,923,679; 3,835,163; 4,158,635; 4,120,874 and 4,102,903. Other useful detergency builders include the ether hydroxypolycarboxylates, copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1, 3, 5- trihydroxy benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts thereof. Citrate builders, e.g., citric acid and soluble salts thereof (particularly sodium salt), are polycarboxylate builders of particular importance. Oxydisuccinates are also especially useful in such compositions and combinations. Also suitable in the detergent compositions of the present invention are the 3,3-dicarboxy-4-oxa-l,6-hexanedioates and the related compounds disclosed in U.S. Patent 4,566,984, Bush, issued January 28, 1986. Useful succinic acid builders include the C5-C 2 Q alkyl and alkenyl succinic acids and salts thereof. A particularly preferred compound of this type is dodecenylsuccinic acid. Specific examples of succinate builders include: laurylsuccinate, myristylsuccinate, palmitylsuccinate, 2- dodecenylsuccinate (preferred), 2-pentadecenylsuccinate, and the like. Laurylsuccinates are the preferred builders of this group, and are described in European Patent Application 86200690.5/0,200,263, published November 5, 1986. Other suitable polycarboxylates are disclosed in U.S. Patent 4,144,226, Crutchfield et al, issued March 13, 1979 and in U.S. Patent 3,308,067, Diehl, issued March 7, 1967. See also Diehl U.S. Patent 3,723,322. Fatty acids, e.g., C^-Cjg monocarboxylic acids, can also be incoφorated into the compositions alone, or in combination with the aforesaid builders, especially citrate and/or the succinate builders, to provide additional builder activity. Such use of fatty acids will generally result in a diminution of sudsing, which should be taken into account by the formulator. Surfactants Detersive surfactants included in the fully-formulated detergent compositions afforded by the present invention comprises at least 0.01%, preferably from about 0.5% to about 50%), by weight of detergent composition depending upon the particular surfactants used and the desired effects. In a highly preferred embodiment, the detersive surfactant comprises from about 0.5% to about 20% by weight of the composition. The detersive surfactant can be nonionic, anionic, ampholytic, zwitterionic, or cationic. Mixtures of these surfactants can also be used. Preferred detergent compositions comprise anionic detersive surfactants or mixtures of anionic surfactants with other surfactants, especially nonionic surfactants. Nonlimiting examples of surfactants useful herein include the conventional Cn-Cjg alkyl benzene sulfonates and primary, secondary and random alkyl sulfates, the C10-C18 alkyl alkoxy sulfates, the CJO-C I S alkyl polyglycosides and their corresponding sulfated polyglycosides, Cj -Ci8 alpha-sulfonated fatty acid esters, Cι 2 -Cιg alkyl and alkyl phenol alkoxylates (especially ethoxylates and mixed ethoxy/propoxy), Cj -Ci8 betaines and sulfobetaines ("sultaines"), Cio-Cjg amine oxides, and the like. Other conventional useful surfactants are listed in standard texts. Particularly preferred surfactants in the preferred automatic dishwashing compositions (ADD) of the present invention are low foaming nonionic surfactants (LFNI). LFNI may be present in amounts from 0.01 % to about 10% by weight, preferably from about 0.1% to about 10%, and most preferably from about 0.25% to about 4%. LFNIs are most typically used in ADDs on account of the improved water-sheeting action (especially from glass) which they confer to the ADD product. They also encompass non-silicone, nonphosphate polymeric materials further illustrated hereinafter which are known to defoam food soils encountered in automatic dishwashing. Preferred LFNIs include nonionic alkoxylated surfactants, especially ethoxylates derived from primary alcohols, and blends thereof with more sophisticated surfactants, such as the polyoxypropylene/polyoxyethylene/polyoxypropylene (PO/EO/PO) reverse block polymers. The PO/EO/PO polymer-type surfactants are well-known to have foam suppressing or defoaming action, especially in relation to common food soil ingredients such as egg. The invention encompasses preferred embodiments wherein LFNI is present, and wherein this component is solid at about 95°F (35°C), more preferably solid at about 77°F (25°C). For ease of manufacture, a preferred LFNI has a melting point between about 77°F (25°C) and about 140°F (60°C), more preferably between about 80°F (26.6°C) and 110°F (43.3°C). In a preferred embodiment, the LFNI is an ethoxylated surfactant derived from the reaction of a monohydroxy alcohol or alkylphenol containing from about 8 to about 20 carbon atoms, with from about 6 to about 15 moles of ethylene oxide per mole of alcohol or alkyl phenol on an average basis. A particularly preferred LFNI is derived from a straight chain fatty alcohol containing from about 16 to about 20 carbon atoms (Ci 6-C 2 o alcohol), preferably a Ci g alcohol, condensed with an average of from about 6 to about 15 moles, preferably from about 7 to about 12 moles, and most preferably from about 7 to about 9 moles of ethylene oxide per mole of alcohol. Preferably the ethoxylated nonionic surfactant so derived has a narrow ethoxylate distribution relative to the average. The LFNI can optionally contain propylene oxide in an amount up to about 15% by weight. Other preferred LFNI surfactants can be prepared by the processes described in U.S. Patent 4,223,163, issued September 16, 1980, Builloty, incoφorated herein by reference. Highly preferred ADDs herein wherein the LFNI is present make use of ethoxylated monohydroxy alcohol or alkyl phenol and additionally comprise a polyoxyethylene, polyoxypropylene block polymeric compound; the ethoxylated monohydroxy alcohol or alkyl phenol fraction of the LFNI comprising from about 20%) to about 100%, preferably from about 30% to about 70%, of the total LFNI. Suitable block polyoxyethylene-polyoxypropylene polymeric compounds that meet the requirements described hereinbefore include those based on ethylene glycol, propylene glycol, glycerol, trimethylolpropane and ethylenediamine as initiator reactive hydrogen compound. Polymeric compounds made from a sequential ethoxylation and propoxylation of initiator compounds with a single reactive hydrogen atom, such as C^.jg aliphatic alcohols, do not generally provide satisfactory suds control in the instant ADDs. Certain of the block polymer surfactant compounds designated PLURONIC® and TETRONIC® by the BASE- Wyandotte Coφ., Wyandotte, Michigan, are suitable in ADD compositions of the invention. A particularly preferred LFNI contains from about 40% to about 70% of a polyoxypropylene/polyoxyethylene/polyoxypropylene block polymer blend comprising about 75%, by weight of the blend, of a reverse block co-polymer of polyoxyethylene and polyoxypropylene containing 17 moles of ethylene oxide and 44 moles of propylene oxide; and about 25%, by weight of the blend, of a block co- polymer of polyoxyethylene and polyoxypropylene initiated with trimethylolpropane and containing 99 moles of propylene oxide and 24 moles of ethylene oxide per mole of trimethylolpropane. Suitable for use as LFNI in the ADD compositions are those LFNI having relatively low cloud points and high hydrophilic-lipophilic balance (HLB). Cloud points of 1% solutions in water are typically below about 32°C and preferably lower, e.g., 0°C, for optimum control of sudsing throughout a full range of water temperatures. LFNIs which may also be used include those POLY-TERGENT® SLF-18 nonionic surfactants from Olin Coφ., and any biodegradable LFNI having the melting point properties discussed hereinabove. These and other nonionic surfactants are well known in the art, being described in more detail in Kirk Othmer's Encyclopedia of Chemical Technology, 3rd Ed., Vol. 22, pp. 360-379, "Surfactants and Detersive Systems", incoφorated by reference herein. Preferred are ADD compositions comprising mixed surfactants wherein the sudsing (absent any silicone suds controlling agent) is less than 2 inches, preferably less than 1 inch, as determined by the disclosure below. The equipment useful for these measurements are: a Whirlpool Dishwasher (model 900) equipped with clear plexiglass door, IBM computer data collection with Labview and Excel Software, proximity sensor (Newark Coφ. - model 95F5203) using SCXI interface, and a plastic ruler. The data is collected as follows. The proximity sensor is affixed to the bottom dishwasher rack on a metal bracket. The sensor faces downward toward the rotating dishwasher arm on the bottom of the machine (distance approximately 2 cm. from the rotating arm). Each pass of the rotating arm is measured by the proximity sensor and recorded. The pulses recorded by the computer are converted to rotations per minute (RPM) of the bottom arm by counting pulses over a 30 second interval. The rate of the arm rotation is directly proportional to the amount of suds in the machine and in the dishwasher pump (i.e., the more suds produced, the slower the arm rotation). The plastic ruler is clipped to the bottom rack of the dishwasher and extends to the floor of the machine. At the end of the wash cycle, the height of the suds is measured using the plastic ruler (viewed through the clear door) and recorded as suds height. The following procedure is followed for evaluating ADD compositions for suds production as well as for evaluating nonionic surfactants for utility. (For separate evaluation of nonionic surfactant, a base ADD formula, such as Cascade powder, is used along with the nonionic surfactants which are added separately in glass vials to the dishwashing machine.) First, the machine is filled with water (adjust water for appropriate temperature and hardness) and proceed through a rinse cycle. The RPM is monitored throughout the cycle (approximately 2 min.) without any ADD product (or surfactants) being added (a quality control check to ensure the machine is functioning properly). As the machine begins to fill for the wash cycle, the water is again adjusted for temperature and hardness, and then the ADD product is added to the bottom of the machine (in the case of separately evaluated surfactants, the ADD base formula is first added to the bottom of the machine then the surfactants are added by placing the surfactant-containing glass vials inverted on the top rack of the machine). The RPM is then monitored throughout the wash cycle. At the end of the wash cycle, the suds height is recorded using the plastic ruler. The machine is again filled with water (adjust water for appropriate temperature and hardness) and runs through another rinse cycle. The RPM is monitored throughout this cycle. An average RPM is calculated for the 1st rinse, main wash, and final rinse. The %RPM efficiency is then calculated by dividing the average RPM for the test surfactants into the average RPM for the control system (base ADD formulation without the nonionic surfactant). The RPM efficiency and suds height measurements are used to dimension the overall suds profile of the surfactant. Bleaching Agents Hydrogen peroxide sources are described in detail in the herein incoφorated Kirk Othmer's Encyclopedia of Chemical Technology, 4th Ed (1992, John Wiley & Sons), Vol. 4, pp. 271-300 "Bleaching Agents (Survey)", and include the various forms of sodium perborate and sodium percarbonate, including various coated and modified forms. An "effective amount" of a source of hydrogen peroxide is any amount capable of measurably improving stain removal (especially of tea stains) from soiled dishware compared to a hydrogen peroxide source-free composition when the soiled dishware is washed by the consumer in a domestic automatic dishwasher in the presence of alkali. More generally a source of hydrogen peroxide herein is any convenient compound or mixture which under consumer use conditions provides an effective amount of hydrogen peroxide. Levels may vary widely and are usually in the range from about 0.1% to about 70%, more typically from about 0.5% to about 30%, by weight of the ADD compositions herein. The preferred source of hydrogen peroxide used herein can be any convenient source, including hydrogen peroxide itself. For example, perborate, e.g., sodium perborate (any hydrate but preferably the mono- or tetra-hydrate), sodium carbonate peroxyhydrate or equivalent percarbonate salts, sodium pyrophosphate peroxyhydrate, urea peroxyhydrate, or sodium peroxide can be used herein. Also useful are sources of available oxygen such as persulfate bleach (e.g., OXONE, manufactured by DuPont). Sodium perborate monohydrate and sodium percarbonate are particularly preferred. Mixtures of any convenient hydrogen peroxide sources can also be used. A preferred percarbonate bleach comprises dry particles having an average particle size in the range from about 500 micrometers to about 1,000 micrometers, not more than about 10% by weight of said particles being smaller than about 200 micrometers and not more than about 10% by weight of said particles being larger than about 1,250 micrometers. Optionally, the percarbonate can be coated with a silicate, borate or water-soluble surfactants. Percarbonate is available from various commercial sources such as FMC, Solvay and Tokai Denka. While not preferred for ADD compositions of the present invention which comprise detersive enzymes, the present invention compositions may also comprise as the bleaching agent a chlorine-type bleaching material. Such agents are well known in the art, and include for example sodium dichloroisocyanurate ("NaDCC"). While effective ADD compositions herein may comprise only the nonionic surfactant and builder, fully-formulated ADD compositions typically will also comprise other automatic dishwashing detergent adjunct materials to improve or modify performance. These materials are selected as appropriate for the properties required of an automatic dishwashing composition. For example, low spotting and filming is desired — preferred compositions have spotting and filming grades of 3 or less, preferably less than 2, and most preferably less than 1, as measured by the standard test of The American Society for Testing and Materials ("ASTM") D3556- 85 (Reapproved 1989) "Standard Test Method for Deposition on Glassware During Mechanical Dishwashing". (a) Bleach Activators Preferably, the peroxygen bleach component in the composition is formulated with an activator (peracid precursor). The activator is present at levels of from about 0.01% to about 15%, preferably from about 0.5%) to about 10%, more preferably from about 1% to about 8%, by weight of the composition. Preferred activators are selected from the group consisting of tetraacetyl ethylene diamine (TAED), benzoylcaprolactam (BzCL), 4-nitrobenzoylcaprolactam, 3-chlorobenzoyl- caprolactam, benzoyloxybenzenesulphonate (BOBS), nonanoyloxybenzene- sulphonate (NOBS), phenyl benzoate (PhBz), decanoyloxybenzenesulphonate (CJO- OBS), benzoylvalerolactam (BZVL), octanoyloxybenzenesulphonate (Cg-OBS), perhydrolyzable esters and mixtures thereof, most preferably benzoylcaprolactam and benzoylvalerolactam. Particularly preferred bleach activators in the pH range from about 8 to about 9.5 are those selected having an OBS or VL leaving group. Preferred bleach activators are those described in U.S. Patent 5,130,045, Mitchell et al, and 4,412,934, Chung et al, and copending patent applications U. S. Serial Nos. 08/064,624, 08/064,623, 08/064,621, 08/064,562, 08/064,564, 08/082,270 and copending application to M. Burns, A. D. Willey, R. T. Hartshorn, C. K. Ghosh, entitled "Bleaching Compounds Comprising Peroxyacid Activators Used With Enzymes" and having U.S. Serial No. 08/133,691 (P&G Case 4890R), all of which are incoφorated herein by reference. The mole ratio of peroxygen bleaching compound (as AvO) to bleach activator in the present invention generally ranges from at least 1 :1, preferably from about 20:1 to about 1 :1, more preferably from about 10:1 to about 3:1. Quaternary substituted bleach activators may also be included. The present detergent compositions preferably comprise a quaternary substituted bleach activator (QSBA) or a quaternary substituted peracid (QSP); more preferably, the former. Preferred QSBA structures are further described in copending U.S. Serial No. 08/298,903, 08/298,650, 08/298,906 and 08/298,904 filed August 31, 1994. incoφorated herein by reference. (b Organic Peroxides, especially Diacyl Peroxides These are extensively illustrated in Kirk Othmer, Encyclopedia of Chemical Technology, Vol. 17, John Wiley and Sons, 1982 at pages 27-90 and especially at pages 63-72, all incoφorated herein by reference. If a diacyl peroxide is used, it will preferably be one which exerts minimal adverse impact on spotting/filming. (c , Metal-containing Bleach Catalysts The present invention compositions and methods utilize metal-containing bleach catalysts that are effective for use in ADD compositions. Preferred are manganese and cobalt-containing bleach catalysts. One type of metal-containing bleach catalyst is a catalyst system comprising a transition metal cation of defined bleach catalytic activity, such as copper, iron, titanium, ruthenium tungsten, molybdenum, or manganese cations, an auxiliary metal cation having little or no bleach catalytic activity, such as zinc or aluminum cations, and a sequestrate having defined stability constants for the catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid, ethylenediaminetetra (methylenephosphonic acid) and water-soluble salts thereof. Such catalysts are disclosed in U.S. Pat. 4,430,243. Other types of bleach catalysts include the manganese-based complexes disclosed in U.S. Pat. 5,246,621 and U.S. Pat. 5,244,594. Preferred examples of theses catalysts include Mn^ 2 (u-O)3(l,4,7-trimethyl-l,4,7-triazacyclononane) 2 - (PF 6 ) 2 ("MnTACN"), Mn ιπ 2 (u-O) γ (u-O Ac) ( 1 ,4,7-trimethyl- 1 ,4,7-triazacyclono- nane) -(C104) 2 , Mn IV 4(u-O)6(l ,4,7-triazacyclononane)4-(ClO4) 2 , Mn m Mn IV 4(u- O) \ (u-O Ac) 2 ( 1 ,4,7-trimethyl- 1 ,4,7-triazacyclononane) 2 -(ClO4)3 , and mixtures thereof. See also European patent application publication no. 549,272. Other ligands suitable for use herein include l,5,9-trimethyl-l,5,9-triazacyclododecane, 2- methyl-l,4,7-triazacyclononane, 2-methyl-l,4,7-triazacyclononane, and mixtures thereof. The bleach catalysts useful in automatic dishwashing compositions and concentrated powder detergent compositions may also be selected as appropriate for the present invention. For examples of suitable bleach catalysts see U.S. Pat. 4,246,612 and U.S. Pat. 5,227,084. Other bleach catalysts are described, for example, in European patent application, publication no. 408,131 (cobalt complex catalysts), European patent applications, publication nos. 384,503, and 306,089 (metallo-poφhyrin catalysts), U.S. 4,728,455 (manganese/multidentate ligand catalyst), U.S. 4,711,748 and European patent application, publication no. 224,952, (absorbed manganese on aluminosilicate catalyst), U.S. 4,601,845 (aluminosilicate support with manganese and zinc or magnesium salt), U.S. 4,626,373 (manganese/ligand catalyst), U.S. 4,1 19,557 (ferric complex catalyst), German Pat. specification 2,054,019 (cobalt chelant catalyst) Canadian 866,191 (transition metal-containing salts), U.S. 4,430.243 (chelants with manganese cations and non-catalytic metal cations), and U.S. 4,728,455 (manganese gluconate catalysts). Preferred are cobalt catalysts which have the formula: [Co(NH 3 ) n (M') m ] Y y wherein n is an integer from 3 to 5 (preferably 4 or 5; most preferably 5); M' is a labile coordinating moiety, preferably selected from the group consisting of chlorine, bromine, hydroxide, water, and (when m is greater than 1) combinations thereof; m is an integer from 1 to 3 (preferably 1 or 2; most preferably 1); m+n = 6; and Y is an appropriately selected counteranion present in a number y, which is an integer from 1 to 3 (preferably 2 to 3; most preferably 2 when Y is a -1 charged anion), to obtain a charge-balanced salt. The preferred cobalt catalyst of this type useful herein are cobalt pentaamine chloride salts having the formula [Co(NH3)5Cl] Y v , and especially [Co(NH 3 ) 5 Cl]Cl 2 . More preferred are the present invention compositions which utilize cobalt (III) bleach catalysts having the formula: [Co(NH 3 ) n (M) m (B) b ] T y wherein cobalt is in the +3 oxidation state; n is 4 or 5 (preferably 5); M is one or more ligands coordinated to the cobalt by one site; m is 0, 1 or 2 (preferably 1); B is a ligand coordinated to the cobalt by two sites; b is 0 or 1 (preferably 0), and when b=0, then m+n = 6, and when b=l, then m=0 and n=4; and T is one or more appropriately selected counteranions present in a number y, where y is an integer to obtain a charge-balanced salt (preferably y is 1 to 3; most preferably 2 when T is a -1 o charged anion); and wherein further said catalyst has a base hydrolysis rate constant of less than 0.23 M" 1 s" 1 (25°C). Preferred T are selected from the group consisting of chloride, iodide, I 3 ", formate, nitrate, nitrite, sulfate, sulfite, citrate, acetate, carbonate, bromide, PFg", BF4", B(Ph)4", phosphate, phosphite, silicate, tosylate, methanesulfonate, and combinations thereof. Optionally, T can be protonated if more than one anionic group exists in T, e.g., HPO42-, HCO 3 ", H 2 PO4~, etc. Further, T may be selected from the group consisting of non-traditional inorganic anions such as anionic surfactants (e.g., linear alkylbenzene sulfonates (LAS), alkyl sulfates (AS), alkylethoxysulfonates (AES), etc.) and or anionic polymers (e.g., polyacrylates, polymethacrylates, etc.). The M moieties include, but are not limited to, for example, F", SO4"2, NCS" , SCN", S 2 O 3 ~ 2, NH3, PO43-, and carboxylates (which preferably are mono- carboxylates, but more than one carboxylate may be present in the moiety as long as the binding to the cobalt is by only one carboxylate per moiety, in which case the other carboxylate in the M moiety may be protonated or in its salt form). Optionally, M can be protonated if more than one anionic group exists in M (e.g., HPO4 2 -, HCO 3 -, H2PO4-, HOC(O)CH 2 C(O)O-, etc.) Preferred M moieties are substituted and unsubstituted C1-C30 carboxylic acids having the formulas: RC(O)O- wherein R is preferably selected from the group consisting of hydrogen and Cl"C 3 o (preferably Cj-Cig) unsubstituted and substituted alkyl, Cg-C 3 Q (preferably Cβ-Cjg) unsubstituted and substituted aryl, and C 3 -C 3 Q (preferably C5- Cjg) unsubstituted and substituted heteroaryl, wherein substituents are selected from the group consisting of -NR' 3 , -NR'4+, -C(O)OR', -OR', -C(O)NR' 2 , wherein R' is selected from the group consisting of hydrogen and C1 -C6 moieties. Such substituted R therefore include the moieties -(CH 2 ) n OH and -(CH ) n NR'4 + , wherein n is an integer from 1 to about 16, preferably from about 2 to about 10, and most preferably from about 2 to about 5. Most preferred M are carboxylic acids having the formula above wherein R is selected from the group consisting of hydrogen, methyl, ethyl, propyl, straight or branched C4-Cι 2 alkyl, and benzyl. Most preferred R is methyl. Preferred carboxylic acid M moieties include formic, benzoic, octanoic, nonanoic, decanoic, dodecanoic, malonic, maleic, succinic, adipic, phthalic, 2-ethylhexanoic, naphthenoic, oleic, palmitic, triflate, tartrate, stearic, butyric, citric, acrylic, aspartic, fumaric, lauric, linoleic, lactic, malic, and especially acetic acid. The B moieties include carbonate, di- and higher carboxylates (e.g., oxalate, malonate, malic, succinate, maleate), picolinic acid, and alpha and beta amino acids (e.g., glycine, alanine, beta-alanine, phenylalanine). Cobalt bleach catalysts useful herein are known, being described for example along with their base hydrolysis rates, in M. L. Tobe, "Base Hydrolysis of Transition-Metal Complexes", Adv. Inorg. Bioinorg. Mech.. (1983), 2, pages 1-94. For example, Table 1 at page 17, provides the base hydrolysis rates (designated therein as koπ) f° r cobalt pentaamine catalysts complexed with oxalate (køH = 2.5 x 10 "4 M " 1 s- 1 (25°C)), NCS- (k 0 H= 5.0 x 10" 4 M ' 1 s " 1 (25°C)), formate (køH = 5.8 x lO "4 M "1 s '1 (25°C)), and acetate (k 0 H= 9 - 6 x 10~4 M_1 s_ 1 (25°C)). The most preferred cobalt catalyst useful herein are cobalt pentaamine acetate salts having the formula [Co(NH 3 )5OAc] T v , wherein OAc represents an acetate moiety, and especially cobalt pentaamine acetate chloride, [Co(NH 3 )5OAc]Cl ; as well as [Co(NH 3 ) 5 OAc](OAc) 2 ; [Co(NH 3 ) 5 OAc](PF 6 ) 2 ; [Co(NH 3 ) 5 OAc](SO 4 ); [Co. (NH 3 ) 5 OAc](BF 4 ) 2 ; and [Co(NH 3 ) 5 OAc](NO 3 ) 2 . These cobalt catalysts are readily prepared by known procedures, such as taught for example in the Tobe article hereinbefore and the references cited therein, in U.S. Patent 4,810,410, to Diakun et al, issued March 7,1989, J. Chem. Ed. (1989), 66 (12), 1043-45; The Synthesis and Characterization of Inorganic Compounds, W.L. Jolly (Prentice-Hall; 1970), pp. 461-3; Inorg. Chem.. 18, 1497-1502 (1979); Inorg. Chem.. 21, 2881-2885 (1982); Inorg. Chem.. 18, 2023-2025 (1979); Inorg. Synthesis, 173-176 (1960); and Journal of Physical Chemistry. 56, 22-25 (1952). These catalysts may be coprocessed with adjunct materials so as to reduce the color impact if desired for the aesthetics of the product, or to be included in enzyme-containing particles as exemplified hereinafter, or the compositions may be manufactured to contain catalyst "speckles". As a practical matter, and not by way of limitation, the cleaning compositions and cleaning processes herein can be adjusted to provide on the order of at least one part per hundred million of the active bleach catalyst species in the aqueous washing medium, and will preferably provide from about 0.01 ppm to about 25 ppm, more preferably from about 0.05 ppm to about 10 ppm, and most preferably from about 0.1 ppm to about 5 ppm, of the bleach catalyst species in the wash liquor. In order to obtain such levels in the wash liquor of an automatic dishwashing process, typical automatic dishwashing compositions herein will comprise from about 0.0005% to about 0.2%, more preferably from about 0.004% to about 0.08%, of bleach catalyst by weight of the cleaning compositions. pH and Buffering Variation Many detergent compositions herein will be buffered, i.e., they are relatively resistant to pH drop in the presence of acidic soils. However, other compositions herein may have exceptionally low buffering capacity, or may be substantially unbuffered. Techniques for controlling or varying pH at recommended usage levels more generally include the use of not only buffers, but also additional alkalis, acids, pH-jump systems, dual compartment containers, etc., and are well known to those skilled in the art. The preferred ADD compositions herein comprise a pH-adjusting component selected from water-soluble alkaline inorganic salts and water-soluble organic or inorganic builders. The pH-adjusting components are selected so that when the ADD is dissolved in water at a concentration of l 000 - 10,000 ppm, the pH remains in the range of above about 8, preferably from about 9.5 to about 1 1. The preferred nonphosphate pH-adjusting component of the invention is selected from the group consisting of: (i) sodium carbonate or sesquicarbonate; (ii) sodium silicate, preferably hydrous sodium silicate having SiO 2 :Na 2 O ratio of from about 1 :1 to about 2:1, and mixtures thereof with limited quantities of sodium metasilicate; (iii) sodium citrate; (iv) citric acid; (v) sodium bicarbonate; (vi) sodium borate, preferably borax; (vii) sodium hydroxide; and (viii) mixtures of (i)-(vii). Preferred embodiments contain low levels of silicate (i.e. from about 3% to about 10% SiO 2 ). Illustrative of highly preferred pH-adjusting component systems are binary mixtures of granular sodium citrate with anhydrous sodium carbonate, and three- component mixtures of granular sodium citrate trihydrate, citric acid monohydrate and anhydrous sodium carbonate. The amount of the pH adjusting component in the instant ADD compositions is preferably from about 1% to about 50%), by weight of the composition. In a preferred embodiment, the pH-adjusting component is present in the ADD composition in an amount from about 5%> to about 40%, preferably from about 10% to about 30%), by weight. For compositions herein having a pH between about 9.5 and about 11 of the initial wash solution, particularly preferred ADD embodiments comprise, by weight of ADD, from about 5% to about 40%, preferably from about 10% to about 30%, most preferably from about 15% to about 20%, of sodium citrate with from about 5% to about 30%, preferably from about 7% to 25%, most preferably from about 8% to about 20% sodium carbonate. Water-Soluble Silicates The present automatic dishwashing detergent compositions may further comprise water-soluble silicates. Water-soluble silicates herein are any silicates which are soluble to the extent that they do not adversely affect spotting/filming characteristics of the ADD composition. Examples of silicates are sodium metasilicate and, more generally, the alkali metal silicates, particularly those having a SiO 2 :Na 2 O ratio in the range 1.6:1 to 3.2:1; and layered silicates, such as the layered sodium silicates described in U.S. Patent 4,664,839, issued May 12, 1987 to H. P. Rieck. NaSKS-6® is a crystalline layered silicate marketed by Hoechst (commonly abbreviated herein as "SKS-6"). Unlike zeolite builders, Na SKS-6 and other water-soluble silicates useful herein do not contain aluminum. NaSKS-6 is the δ-Na 2 Siθ5 form of layered silicate and can be prepared by methods such as those described in German DE-A-3 ,417,649 and DE-A-3 ,742,043. SKS-6 is a preferred layered silicate for use herein, but other such layered silicates, such as those having the general formula NaMSi x O 2x -ι-i yH 2 O wherein M is sodium or hydrogen, x is a number from 1.9 to 4, preferably 2, and y is a number from 0 to 20, preferably 0 can be used. Various other layered silicates from Hoechst include NaSKS-5, NaSKS-7 and NaSKS-11, as the α-, β- and γ- forms. Other silicates may also be useful, such as for example magnesium silicate, which can serve as a crispening agent in granular formulations, as a stabilizing agent for oxygen bleaches, and as a component of suds control systems. Silicates particularly useful in automatic dishwashing (ADD) applications include granular hydrous 2-ratio silicates such as BRITESIL® H20 from PQ Coφ., and the commonly sourced BRITESIL® H24 though liquid grades of various silicates can be used when the ADD composition has liquid form. Within safe limits, sodium metasilicate or sodium hydroxide alone or in combination with other silicates may be used in an ADD context to boost wash pH to a desired level. Material Care Agents The preferred ADD compositions may contain one or more material care agents which are effective as corrosion inhibitors and/or anti-tarnish aids. Such materials are preferred components of machine dishwashing compositions especially in certain European countries where the use of electroplated nickel silver and sterling silver is still comparatively common in domestic flatware, or when aluminum protection is a concern and the composition is low in silicate. Generally, such material care agents include metasilicate, silicate, bismuth salts, manganese salts, paraffin, triazoles, pyrazoles, thiols, mercaptans, aluminum fatty acid salts, and mixtures thereof. When present, such protecting materials are preferably incoφorated at low levels, e.g., from about 0.01%) to about 5% of the ADD composition. Suitable corrosion inhibitors include paraffin oil, typically a predominantly branched aliphatic hydrocarbon having a number of carbon atoms in the range of from about 20 to about 50; preferred paraffin oil is selected from predominantly branched C 2 5- 45 species with a ratio of cyclic to noncyclic hydrocarbons of about 32:68. A paraffin oil meeting those characteristics is sold by Wintershall, Salzbergen, Germany, under the trade name WINOG 70. Additionally, the addition of low levels of bismuth nitrate (i.e., Bi(NO 3 ) 3 ) is also preferred. Other corrosion inhibitor compounds include benzotriazole and comparable compounds; mercaptans or thiols including thionaphtol and thioanthranol; and finely divided Aluminum fatty acid salts, such as aluminum tristearate. The formulator will recognize that such materials will generally be used judiciously and in limited quantities so as to avoid any tendency to produce spots or films on glassware or to compromise the bleaching action of the compositions. For this reason, mercaptan anti-tarnishes which are quite strongly bleach-reactive and common fatty carboxylic acids which precipitate with calcium in particular are preferably avoided. Adjunct Materials Detersive ingredients or adjuncts optionally included in the instant compositions can include one or more materials for assisting or enhancing cleaning performance, treatment of the substrate to be cleaned, or designed to improve the aesthetics of the compositions. Adjuncts which can also be included in compositions of the present invention, at their conventional art-established levels for use (generally, adjunct materials comprise, in total, from about 30% to about 99.9%, preferably from about 10% to about 95%, by weight of the compositions), include other active ingredients such as non-phosphate builders, chelants, enzymes, suds suppressors, dispersant polymers (e.g., from BASF Coφ. or Rohm & Haas), color speckles, silvercare, anti-tarnish and/or anti-corrosion agents, dyes, fillers, germicides, alkalinity sources, hydrotropes, anti-oxidants, enzyme stabilizing agents, perfumes, solubilizing agents, carriers, processing aids, pigments, and pH control agents. Depending on whether a greater or lesser degree of compactness is required, filler materials can also be present in the instant ADDs. These include sucrose, sucrose esters, sodium sulfate, potassium sulfate, etc., in amounts up to about 70%), preferably from 0% to about 40% of the ADD composition. Preferred filler is sodium sulfate, especially in good grades having at most low levels of trace impurities. Sodium sulfate used herein preferably has a purity sufficient to ensure it is non-reactive with bleach; it may also be treated with low levels of sequestrants, such as phosphonates or EDDS in magnesium-salt form. Note that preferences, in terms of purity sufficient to avoid decomposing bleach, applies also to pH-adjusting component ingredients, specifically including any silicates used herein. Hydrotrope materials such as sodium benzene sulfonate, sodium toluene sulfonate, sodium cumene sulfonate, etc., can be present, e.g., for better dispersing surfactant. Bleach-stable perfumes (stable as to odor); and bleach-stable dyes such as those disclosed in U.S. Patent 4,714,562, Roselle et al, issued December 22, 1987 can also be added to the present compositions in appropriate amounts. Since ADD compositions herein can contain water-sensitive ingredients or ingredients which can co-react when brought together in an aqueous environment, it is desirable to keep the free moisture content of the ADDs at a minimum, e.g., 7% or less, preferably 5% or less of the ADD; and to provide packaging which is substantially impermeable to water and carbon dioxide. Coating measures have been described herein to illustrate a way to protect the ingredients from each other and from air and moisture. Plastic bottles, including refillable or recyclable types, as well as conventional barrier cartons or boxes are another helpful means of assuring maximum shelf-storage stability. As noted, when ingredients are not highly compatible, it may further be desirable to coat at least one such ingredient with a low-foaming nonionic surfactant for protection. There are numerous waxy materials which can readily be used to form suitable coated particles of any such otherwise incompatible components; however, the formulator prefers those materials which do not have a marked tendency to deposit or form films on dishes including those of plastic construction. The following nonlimiting examples further illustrate the ADD compositions of the present invention. EXAMPLE 1 Ingredients: Weight% A B Sodium Tripolyphosphate (STPP) 28.0 30 Sodium carbonate 30.0 28.0 Hydrated 2. Or silicate 5 2 nonionic surfactants 1.0 2.0 Chymotrypsin-like Protease 1 (4% active) 0.43 0.75 Trypsin-like Protease^ (3% active) 0.22 0.5 Amylase 0.46 0.46 Perborate monohydrate (15.5% Active AvO)^ 14.5 14.5 Water, sodium sulfate and misc. Balance Balance 1 A carbonyl hydrolase variant of B. lentus subtilisin with the amino acid substitutions 76D/103A/104I. 2 Savinase® or a carbonyl hydrolase variant of B. lentus subtilisin with the amino acid substitutions 2101/ 76D/103A/104I/156E/166D. 3 The AvO level of the above formula is 2.2%. The ADD's of the above dishwashing detergent composition examples are used to wash milk-soiled glasses, by loading the soiled dishes in a domestic automatic dishwashing appliance and washing using either cold fill, 60°C peak, or uniformly 45- 50°C wash cycles with a product concentration of the exemplary compositions of from about 1,000 to about 8,000 ppm, with excellent cleaning and spotting and filming results.

Claims: WHAT IS CLAIMED IS: 1. A cleaning composition comprising: a) from about 0.0001% to about 10% by weight of the composition of a protease enzyme cleaning system comprising the combination of at least one chymotrypsin-like protease enzyme and at least one trypsin-like protease enzyme, said at least one chymotrypsin-like protease having an enzyme activity ratio of sAAPF activity/bVGR activity of at least about 15 and said trypsin-like protease enzyme having an enzyme activity ratio of sAAPF bVGR of less than about 10.0; and (b) from about 0.1% to about 99% by weight of the composition of cleaning adjunct materials. 2. An automatic dishwashing composition having improved spotting/filming benefits comprising: a) from about 0.0001% to about 10% by weight of the composition of a protease enzyme cleaning system comprising the combination of at least one chymotrypsin-like protease enzyme and at least one trypsin-like protease enzyme, said at least one chymotrypsin-like protease having an enzyme activity ratio of sAAPF activity/bVGR activity of at least about 15 and said trypsin-like protease enzyme having an enzyme activity ratio of sAAPF/bVGR of less than about 10.0; and (b) from about 0.1% to about 99% by weight of the composition of cleaning adjunct materials. 3. An automatic dishwashing composition having improved spotting/filming benefits comprising: (a) from about 0.0001% to about 10% by weight of the composition of a protease enzyme cleaning system comprising the combination of at least one chymotrypsin-like protease enzyme and at least one trypsin-like protease enzyme, said at least one chymotrypsin-like protease having an enzyme activity ratio of sAAPF activity/bVGR activity of at least about 15 and said trypsin-like protease enzyme having an enzyme activity ratio of sAAPF/bVGR of less than about 10.0; and (b) from about 0.1% to about 20% by weight of the composition of a low foaming nonionic surfactant; (c) from about 10% to about 50% by weight of the composition of a detergency builder; (d) from about 0.0001 ) to about 30% by weight of the composition of a source of bleach agent. 4. A composition as claimed in any of Claims 1-3 wherein said at least one chymotrypsin-like protease enzyme has an enzyme activity ratio of sAAPF activity/bVGR activity of at least about 17.5 and said trypsin-like protease enzyme has an enzyme activity ratio of sAAPF/bVGR of about 8.0 or less. 5. A composition as claimed in any of Claims 1-4 wherein said chymotrypsin-like enzyme is a carbonyl hydrolase variant having an amino acid sequence not found in nature, said carbonyl hydrolase being 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, and at least one position being selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +195, +197, +204, +206, +216, +217, +218, +222, +260, +265, +274 and mixtures thereof according to the numbering of Bacillus amyloliquefaciens subtilisin. 6. A composition as claimed in any of Claims 1-5 wherein said chymotrypsin-like enzyme 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, +103 and +104 according to the numbering of Bacillus amyloliquefaciens subtilisin. 7. A composition as claimed in any of Claims 1-6 wherein said trypsin-like protease enzyme is the protease enzyme obtained from Bacillus Lentus subtilisin. 8. A composition as claimed in any of Claims 1-7 wherein the weight ratio of said chymotrypsin-like protease enzyme to said trypsin-like protease enzyme is from about 0.5:1 to about 10:1. 9. A composition as claimed in any of Claims 1-8 wherein the weight ratio of said chymotrypsin-like protease enzyme to said trypsin-like protease enzyme is from about 1:1 to about 5:1 10. A composition as claimed in any of Claims 1-9 wherein said composition further comprises an amylase enzyme. 11. A composition as claimed in any of Claim 1-2 wherein said cleaning adjunct ingredients are selected from the group consisting of builders, silicates, low foaming nonionic surfactants, peroxide bleach sources, bleach activators, bleach catalysts and mixtures thereof. 12. A method for cleaning dishes while preventing spotting or filming on the dishes comprising providing soiled dishes having milk-based food soils and treating said dishes with a composition according to any of Claims 1-11.

Inventors: FOLEY PETER ROBERT, GILBERT LAWRENCE ALLEN, RAI SAROJ, SHOWELL MICHAEL STANFORD, ZHU YONG, FOLEY, PETER, ROBERT, GILBERT, LAWRENCE, ALLEN, RAI, SAROJ, SHOWELL, MICHAEL, STANFORD, ZHU, YONG
Applicants: FOLEY PETER ROBERT, GILBERT LAWRENCE ALLEN, PROCTER & GAMBLE, RAI SAROJ, SHOWELL MICHAEL STANFORD, ZHU YONG, FOLEY, PETER, ROBERT, GILBERT, LAWRENCE, ALLEN, RAI, SAROJ, SHOWELL, MICHAEL, STANFORD, THE PROCTER & GAMBLE COMPANY, ZHU, YONG
Application year: 1998
Main classification: C11D7
IPC codes: C11D3