CLEANING AND/OR TREATMENT COMPOSITIONS

This invention relates to compositions comprising certain amylase variants and processes for making and using such compositions including the use of such compositions to clean and/or treat a situs.

Skip to: Description  ·  Claims  · Patent History  ·  Patent History
Description
CROSS-REFERENCES TO RELATED APPLICATIONS

This application claims priority under 35 U.S.C. § 120 to U.S. application Ser. No. 11/811,129 filed Jun. 8, 2007, which in turn claims priority under 35 U.S.C. § 119(e) to U.S. Provisional Application Ser. No. 60/814,442 filed Jun. 16, 2006.

FIELD OF INVENTION

Compositions comprising enzymes and processes for making and using such compositions.

BACKGROUND OF THE INVENTION

The appearance of enzymes suitable for cleaning and/or treatment applications gave the formulator a new approach to clean and/or treat hard surfaces and fabrics. Unfortunately, even when enzymes are employed, performance issues remain. For example, in certain matrices and/or use conditions, enzymes do not deposit as efficiently as required to provide the desired performance. Thus, the use of this technology continues to be limited.

Surprisingly, when cleaning compositions that comprise certain α-amylases are formulated in accordance with the teachings of the present invention, such compositions can provide improved cleaning.

SUMMARY OF THE INVENTION

This invention relates to compositions comprising certain α-amylase enzymes and processes for making and using such products.

DETAILED DESCRIPTION OF THE INVENTION Definitions

As used herein, the term “cleaning composition” includes, unless otherwise indicated, granular or powder-form all-purpose or “heavy-duty” washing agents, especially laundry detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy-duty liquid types; liquid fine-fabric detergents; hand dishwashing agents or light duty dishwashing agents, especially those of the high-foaming type; machine dishwashing agents, including the various tablet, granular, liquid and rinse-aid types for household and institutional use; liquid cleaning and disinfecting agents, including antibacterial hand-wash types, laundry bars, mouthwashes, denture cleaners, car or carpet shampoos, bathroom cleaners; hair shampoos and hair-rinses; shower gels and foam baths and metal cleaners; as well as cleaning auxiliaries such as bleach additives and “stain-stick” or pre-treat types.

As used herein, the phrase “is independently selected from the group consisting of . . . ” means that moieties or elements that are selected from the referenced Markush group can be the same, can be different or any mixture of elements.

As used herein, articles, for example, “a” and “an” when used in a claim, are understood to mean one or more of what is claimed or described.

As used herein, the terms “include”, “includes” and “including” are meant to be non-limiting.

The test methods disclosed in the Test Methods Section of the present application must be used to determine the respective values of the parameters of Applicants' inventions.

Unless otherwise noted, all component or composition levels are in reference to the active level of that component or composition, and are exclusive of impurities, for example, residual solvents or by-products, which may be present in commercially available sources.

Unless otherwise noted, the enzymes of the present invention are expressed in terms of active protein level and are exclusive of impurities, for example, residual solvents or by-products, which may be present in commercially available sources.

All percentages and ratios are calculated by weight unless otherwise indicated. All percentages and ratios are calculated based on the total composition unless otherwise indicated.

It should be understood that every maximum numerical limitation given throughout this specification includes every lower numerical limitation, as if such lower numerical limitations were expressly written herein. Every minimum numerical limitation given throughout this specification will include every higher numerical limitation, as if such higher numerical limitations were expressly written herein. Every numerical range given throughout this specification will include every narrower numerical range that falls within such broader numerical range, as if such narrower numerical ranges were all expressly written herein.

Compositions

In one aspect, a composition comprising an amylase and:

    • a.) a sufficient amount of calcium to provide a wash liquor comprising said composition with a free calcium concentration as determined by Test Method 1 of from about 0.1 ppm to about 500 ppm, from about 0.2 ppm to about 200 ppm, from about 1 ppm to about 150 ppm, or from about 2 ppm to about 100 ppm, or even from about 3 ppm to about 50 ppm;
    • b.) based on total product weight, less than 15%, less than 10%, less than 8% or even from about 0.01% to about 7% builder; and/or
    • c.) having an enzyme deposition index as defined in Test Method 2 of at least 2.5, at least 2.6, or even from about 2.7 to about 50 is disclosed.
      Such composition may comprise, based on total composition weight, from about 0.0001% to about 2%, from about 0.0005% to about 1%, from about 0.001% to about 0.5% or even from about 0.002% to about 0.25% of said enzyme. Such compositions may be cleaning and/or treatment compositions. Thus it is understood that they may be solids or fluids.

In one aspect, said amylase includes α-amylases derived from Bacillus licheniformis having Sequence I.D. 5 or 6, or an enzyme that is at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or even 99% identical to said Sequence I.D. 5 or 6. Such α-amylases having at least one of the following mutations at positions corresponding to the positions corresponding to Sequence I.D. 5 or 6: 15, 23, 133, 188, 209, 475 or combinations of said positions.

In another aspect, said amylase enzymes include α-amylases derived from Bacillus licheniformis having Sequence I.D. 5 (SEQ ID No. 5 herein being equivalent to SEQ ID No 34 in U.S. Pat. No. 5,958,739) or an enzyme having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or even 99% identity to said Sequence I.D. 5. Such α-amylases having one or more of the following mutations: M15T, H133Y, N188S or T, A209V or G475R.

In another aspect, said amylase enzymes include α-amylases derived from Bacillus licheniformis having Sequence 6 (SEQ ID No. 6 herein being equivalent to SEQ ID NO. 2 in U.S. Pat. No. 6,436,888 B1) or an enzyme having at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or even 99% identity to said Sequence I.D. 6. Such α-amylases having one or more of the following mutations: M15T, H133Y, N188S or T, A209V or G475R; and optionally R23K.

In another aspect, said amylase enzymes include an amylase selected from the group consisting of:

    • a.) an amylase having Seq. I.D. 5, said amylase having one of the following groups of mutations:
      • (i) M15T+H133Y+N188S+A209V;
      • (ii) M15T+H133Y+N188T+A209V;
      • (iii) H133Y+N188S+G475R; or
      • (iv) H133Y+N188S;
    • b.) an amylase having Seq. I.D. 6, said amylase having one of the following groups of mutations:
      • (i) M15T+R23K+H133Y+N188S+A209V;
      • (ii) M15T+R23K+H133Y+N188T+A209V;
      • (iii) R23K+H133Y+N188S+G475R;
      • (iv) R23K+H133Y+N188S;
      • (v) M15T+H133Y+N188S+A209V
      • (vi) M15T+H133Y+N188T+A209V;
      • (vii) H133Y+N188S+G475R; or
      • (viii) H133Y+N188S
        and combinations thereof.

In one aspect, a composition comprising an amylase belonging to EC 3.2.1.1 such as an enzyme having Seq. I.D. 1 and:

    • a.) a sufficient amount of calcium to provide a wash liquor comprising said composition with a free calcium concentration as determined by Test Method 1 of from about 0.1 ppm to about 500 ppm, from about 0.2 ppm to about 200 ppm, from about 1 ppm to about 150 ppm, or from about 2 ppm to about 100 ppm, or even from about 3 ppm to about 50 ppm;
    • b.) based on total product weight, less than 15%, less than 10%, less than 8% or even from about 0.01% to about 7% builder; and/or
    • c.) having an enzyme deposition index as defined in Test Method 2 of at least 2.5, at least 2.6, or even from about 2.7 to about 50 is disclosed.
      Such composition may comprise, based on total composition weight, from about 0.0001% to about 2%, from about 0.0005% to about 1%, from about 0.001% to about 0.5% or even from about 0.002% to about 0.25% of said enzyme. Such compositions may be cleaning and/or treatment compositions. Thus it is understood that they may be solids or fluids.

Any of the aspects of said compositions described in the present specification may comprise a material selected from the group consisting of surfactants, builders, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleaching agents, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids, solvents, pigments, hueing agents, structurants, and mixtures thereof.

Any of the aspects of said compositions described in the present specification may comprise an additional enzyme selected from the group consisting of hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, amylases, or mixtures thereof.

In one aspect, such additional enzyme may be selected from the group consisting of: lipases, including “first cycle lipases” described in U.S. Pat. No. 6,939,702 B1 (SEQ ID No. 2 in the present specification being equivalent to SEQ ID NO:1 in U.S. Pat. No. 6,939,702 B1), a variant of SEQ ID No. 2, a variant of SEQ ID No. 2 having at least 90% identity to SEQ ID No. 2 comprising a substitution of an electrically neutral or negatively charged amino acid with R or K at any of positions 3, 224, 229, 231 and 233, or even a variant comprising T231R and N233R mutations, such variant being sold under the tradename Lipex®; alpha-amylases, including a variant of SEQ ID No. 3 (SEQ ID No. 3 corresponding to SEQ ID No. 2 in U.S. Pat. No. 5,856,164), a variant of SEQ ID No. 3 having at least 90% identity to SEQ ID No. 3 (such variant disclosed in U.S. Pat. No. 6,187,576) comprising two deletions at positions 183 and 184 and sold under the tradename Natalase®; serine proteases, including neutral or alkaline microbial serine proteases, such as subtilisins (EC 3.4.21.62), including those derived from Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens described in U.S. Pat. No. 6,312,936 B1, U.S. Pat. No. 5,679,630, U.S. Pat. No. 4,760,025; microbial-derived endoglucanases exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4), including a bacterial polypeptide endogenous to a member of the genus Bacillus which has a sequence of at least 90%, 94%, 97% and even 99% identity to the amino acid sequence of SEQ ID No. 4 (SEQ ID No. 4 herein being equivalent to SEQ ID NO:2 in US 2005/0112749 A1)—such an enzyme being commercially available under the tradename Celluclean™ by Novozymes A/S, and mixtures thereof.

Any of the aspects of the compositions described in the present specification may comprise a surfactant, including a surfactant selected from the group of anionic surfactants including anionic surfactants selected from the group consisting of linear alkylbenzene-sulfonate (LAS), alcohol ethoxysulfate (AES), mid-branched alkyl sulfates (HSAS) and mixtures thereof; non-ionic surfactants including alcohol ethoxylates, for example alcohol ethoxylates having a chain length of from 1 to 14 carbons, or 12 to 14 carbons; amine oxides and mixtures thereof.

Any of the aspects of the compositions described in the present specification may comprise a polymer, including polymers selected from the group consisting of polyacrylates, maleic/acrylic acid copolymers, cellulose-derived polymers, including carboxymethylcellulose and methyl hydroxyethylcellulose, polyethyleneimine polymers and mixtures thereof.

Any of the aspects of said compositions described in the present specification may comprise a builder selected from the group consisting of citric acid, C12-C18 fatty acid, aluminosilicates, including zeolites A, X and/or Y, sodium tripolyphosphate and mixtures thereof.

Any of the aspects of the compositions described in the present specification may comprise a material selected from the group consisting of a photobleach, a fabric hueing agent and mixtures thereof.

Any of the aspects of the compositions described in the present specification may comprise a photobleach being selected from the group consisting of xanthene dyes and mixtures thereof; sulfonated zinc phthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y, Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures thereof; water soluble phthalocyanine; and/or a fabric hueing agent selected from the group consisting of dyes, including small molecule dyes such as small molecule dyes selected from the group consisting of Colour Index (Society of Dyers and Colourists, Bradford, UK) numbers Direct Violet 9, Direct Violet 35, Direct Violet 48, Direct Violet 51, Direct Violet 66, Direct Blue 1, Direct Blue 71, Direct Blue 80, Direct Blue 279, Acid Red 17, Acid Red 73, Acid Red 88, Acid Red 150, Acid Violet 15, Acid Violet 17, Acid Violet 24, Acid Violet 43, Acid Violet 49, Acid Blue 15, Acid Blue 17, Acid Blue 25, Acid Blue 29, Acid Blue 40, Acid Blue 45, Acid Blue 75, Acid Blue 80, Acid Blue 83, Acid Blue 90 and Acid Blue 113, Acid Black 1, Basic Violet 1, Basic Violet 3, Basic Violet 4, Basic Violet 10, Basic Violet 35, Basic Blue 3, Basic Blue 16, Basic Blue 22, Basic Blue 47, Basic Blue 66, Basic Blue 75, Basic Blue 159 and mixtures thereof, polymeric dyes and mixtures thereof, dye-clay conjugates comprising at least one cationic/basic dye and a smectite clay and mixtures thereof.

Any of the aspects of the compositions described in the present specification may comprise, based on total product weight, from about 0% to about 3%, from about 0.0001% to about 0.5%, or even from about 0.0005% to about 0.3% photobleach and/or from about 0.00003% to about 0.3%, from about 0.00008% to about 0.05%, or even from about 0.0001% to about 0.04% hueing agent.

Enzymes suitable for use in the present compositions can be obtained from Genencor International, Palo Alto, Calif., U.S.A; Novozymes A/S, Bagsvaerd, Denmark; Amersham Pharmacia Biotech., Piscataway, N.J., U.S.A; Sigma-Aldrich Company Ltd, Dorset, UK.

An enzyme having Seq. ID 1 is sold under the tradename Optisize® HT Plus by Genencor International, Palo Alto, Calif., U.S.A. An enzyme having at least 90% identity to Seq. ID 2 is sold under the tradename Lipex® by Novozymes A/S, Bagsvaerd, Denmark. An enzyme having at least 90% identity with Seq. ID 3 is sold under the tradename Natalase® by Novozymes A/S, Bagsvaerd, Denmark. An enzyme having at least 90% identity to Seq. ID 4 is sold under the tradename Celluclean™ by Novozymes A/S, Bagsvaerd, Denmark. An enzyme having Seq. ID 5 is sold under the tradename of Purastar® by Genencor International, Palo Alto, Calif., U.S.A. An enzyme having Seq. ID 6 is sold under the tradename of Termamyl® by Novozymes A/S, Bagsvaerd, Denmark.

Surfactants suitable for use in the present compositions can be obtained from Stepan, Northfield, Ill., USA; Huntsman, Salt Lake City, Utah, USA; Procter & Gamble Chemicals, Cincinnati, Ohio, USA.

Builders suitable for use in the present compositions can be obtained from Rhodia, Paris, France; Industrial Zeolite (UK) Ltd, Grays, Essex, UK; Koma, Nestemica, Czech Republic.

Polymers suitable for use in the present compositions can be obtained from BASF, Ludwigshafen, Germany, CP Kelco, Arnhem, Netherlands.

Photobleaches suitable for use in the present compositions can be obtained from Aldrich, Milwaukee, Wis., USA; Frontier Scientific, Logan, Utah, USA; Ciba Specialty Chemicals, Basel, Switzerland; BASF, Ludwigshafen, Germany; Lamberti S.p.A, Gallarate, Italy; Dayglo Color Corporation, Mumbai, India; Organic Dyestuffs Corp., East Providence, R.I., USA.

Hueing agents suitable for use in the present compositions can be obtained from Aldrich, Milwaukee, Wis., USA; Ciba Specialty Chemicals, Basel, Switzerland; BASF, Ludwigshafen, Germany; Dayglo Color Corporation, Mumbai, India; Organic Dyestuffs Corp., East Providence, R.I., USA; Dystar, Frankfurt, Germany; Lanxess, Leverkusen, Germany; Megazyme, Wicklow, Ireland; Clariant, Muttenz, Switzerland.

Adjunct Materials

While not essential for the purposes of the present invention, the non-limiting list of adjuncts illustrated hereinafter are suitable for use in the instant compositions and may be desirably incorporated in certain embodiments of the invention, for example to assist or enhance cleaning performance, for treatment of the substrate to be cleaned, or to modify the aesthetics of the cleaning composition as is the case with perfumes, colorants, dyes or the like. The precise nature of these additional components, 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. Suitable adjunct materials include, but are not limited to, additional surfactants, additional builders, additional polymers, additional hueing agents, additional photobleaches, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids, solvents, additional hueing agents, structurants and/or pigments. In addition to the disclosure below, suitable examples of such other adjuncts and levels of use are found in U.S. Pat. Nos. 5,576,282, 6,306,812 B1 and 6,326,348 B1 that are incorporated by reference.

As stated, the adjunct ingredients are not essential to Applicants' compositions. Thus, certain embodiments of Applicants' compositions do not contain one or more of the following adjuncts materials: additional surfactants, additional builders, additional polymers, additional photobleaches, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids, solvents, additional hueing agents, structurants and/or pigments. However, when one or more adjuncts are present, such one or more adjuncts may be present as detailed below:

Bleaching Agents—The cleaning compositions of the present invention may comprise one or more bleaching agents. Suitable bleaching agents other than bleaching catalysts include photobleaches, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, pre-formed peracids and mixtures thereof. In general, when a bleaching agent is used, the compositions of the present invention may comprise from about 0.1% to about 50% or even from about 0.1% to about 25% bleaching agent by weight of the subject cleaning composition. Examples of suitable bleaching agents include:

(1) photobleaches

(2) preformed peracids: Suitable preformed peracids include, but are not limited to, compounds selected from the group consisting of percarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, for example, Oxone®, and mixtures thereof. Suitable percarboxylic acids include hydrophobic and hydrophilic peracids having the formula R—(C═O)O—O-M wherein R is an alkyl group, optionally branched, having, when the peracid is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the peracid is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and M is a counter ion, for example, sodium, potassium or hydrogen;

(3) sources of hydrogen peroxide, for example, inorganic perhydrate salts, including alkali metal salts such as sodium salts of perborate (usually mono- or tetra-hydrate), percarbonate, persulphate, perphosphate, persilicate salts and mixtures thereof. In one aspect of the invention the inorganic perhydrate salts are selected from the group consisting of sodium salts of perborate, percarbonate and mixtures thereof. When employed, inorganic perhydrate salts are typically present in amounts of from 0.05 to 40 wt %, or 1 to 30 wt % of the overall composition and are typically incorporated into such compositions as a crystalline solid that may be coated. Suitable coatings include, inorganic salts such as alkali metal silicate, carbonate or borate salts or mixtures thereof, or organic materials such as water-soluble or dispersible polymers, waxes, oils or fatty soaps; and

(4) bleach activators having R—(C═O)-L wherein R is an alkyl group, optionally branched, having, when the bleach activator is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the bleach activator is hydrophilic, less than 6 carbon atoms or even less than 4 carbon atoms; and L is leaving group. Examples of suitable leaving groups are benzoic acid and derivatives thereof—especially benzene sulphonate. Suitable bleach activators include dodecanoyl oxybenzene sulphonate, decanoyl oxybenzene sulphonate, decanoyl oxybenzoic acid or salts thereof, 3,5,5-trimethyl hexanoyloxybenzene sulphonate, tetraacetyl ethylene diamine (TAED) and nonanoyloxybenzene sulphonate (NOBS). Suitable bleach activators are also disclosed in WO 98/17767. While any suitable bleach activator may be employed, in one aspect of the invention the subject cleaning composition may comprise NOBS, TAED or mixtures thereof.

When present, the peracid and/or bleach activator is generally present in the composition in an amount of from about 0.1 to about 60 wt %, from about 0.5 to about 40 wt % or even from about 0.6 to about 10 wt % based on the composition. One or more hydrophobic peracids or precursors thereof may be used in combination with one or more hydrophilic peracid or precursor thereof.

The amounts of hydrogen peroxide source and peracid or bleach activator may be selected such that the molar ratio of available oxygen (from the peroxide source) to peracid is from 1:1 to 35:1, or even 2:1 to 10:1.

Surfactants—The cleaning compositions according to the present invention may comprise a surfactant or surfactant system wherein the surfactant can be selected from nonionic surfactants, anionic surfactants, cationic surfactants, ampholytic surfactants, zwitterionic surfactants, semi-polar nonionic surfactants and mixtures thereof. When present, surfactant is typically present at a level of from about 0.1% to about 60%, from about 1% to about 50% or even from about 5% to about 40% by weight of the subject composition.

Builders—The cleaning compositions of the present invention may comprise one or more detergent builders or builder systems. Builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates, alkali metal silicates, alkaline earth and alkali metal carbonates, aluminosilicate builders and polycarboxylate compounds, 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, citric acid, oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts thereof.

Chelating Agents—The cleaning compositions herein may contain a chelating agent. Suitable chelating agents include copper, iron and/or manganese chelating agents and mixtures thereof. When a chelating agent is used, the subject composition may comprise from about 0.005% to about 15% or even from about 3.0% to about 10% chelating agent by weight of the subject composition.

Dye Transfer Inhibiting Agents—The cleaning compositions of the present invention may also include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in a subject composition, the dye transfer inhibiting agents may be present at levels from about 0.0001% to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition.

Brighteners—The cleaning compositions of the present invention can also contain additional components that may tint articles being cleaned, such as fluorescent brighteners. Suitable fluorescent brightener levels include lower levels of from about 0.01, from about 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt %.

Dispersants—The compositions of the present invention can also contain dispersants. Suitable water-soluble organic materials include 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.

Enzymes—The cleaning compositions can comprise one or more enzymes which provide cleaning performance and/or fabric care benefits. Examples of suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, amylases, or mixtures thereof. A typical combination is an enzyme cocktail that may comprise, for example, a protease and lipase in conjunction with amylase. When present in a cleaning composition, the aforementioned additional enzymes may be present at levels from about 0.00001% to about 2%, from about 0.0001% to about 1% or even from about 0.001% to about 0.5% enzyme protein by weight of the composition.

Enzyme Stabilizers—Enzymes for use in detergents can be stabilized by various techniques. The enzymes employed herein can be stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions that provide such ions to the enzymes. In case of aqueous compositions comprising protease, a reversible protease inhibitor, such as a boron compound, can be added to further improve stability.

Catalytic Metal Complexes—Applicants' cleaning compositions may include catalytic metal complexes. 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. No. 4,430,243.

If desired, the compositions herein can be catalyzed by means of a manganese compound. Such compounds and levels of use are well known in the art and include, for example, the manganese-based catalysts disclosed in U.S. Pat. No. 5,576,282.

Cobalt bleach catalysts useful herein are known, and are described, for example, in U.S. Pat. No. 5,597,936; U.S. Pat. No. 5,595,967. Such cobalt catalysts are readily prepared by known procedures, such as taught for example in U.S. Pat. No. 5,597,936, and U.S. Pat. No. 5,595,967.

Compositions herein may also suitably include a transition metal complex of ligands such as bispidones (WO 05/042532 A1) and/or macropolycyclic rigid ligands—abbreviated as “MRLs”. As a practical matter, and not by way of limitation, the compositions and processes herein can be adjusted to provide on the order of at least one part per hundred million of the active MRL species in the aqueous washing medium, and will typically provide from about 0.005 ppm to about 25 ppm, from about 0.05 ppm to about 10 ppm, or even from about 0.1 ppm to about 5 ppm, of the MRL in the wash liquor.

Suitable transition-metals in the instant transition-metal bleach catalyst include, for example, manganese, iron and chromium. Suitable MRLs include 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.

Suitable transition metal MRLs are readily prepared by known procedures, such as taught for example in WO 00/32601, and U.S. Pat. No. 6,225,464.

Solvents—Suitable solvents include water and other solvents such as lipophilic fluids. Examples of suitable lipophilic fluids include siloxanes, other silicones, hydrocarbons, glycol ethers, glycerine derivatives such as glycerine ethers, perfluorinated amines, perfluorinated and hydrofluoroether solvents, low-volatility nonfluorinated organic solvents, diol solvents, other environmentally-friendly solvents and mixtures thereof.

Processes of Making Compositions

The compositions of the present invention can be formulated into any suitable form and prepared by any process chosen by the formulator, non-limiting examples of which are described in Applicants' examples and in U.S. Pat. No. 4,990,280; U.S. 20030087791A1; U.S. 20030087790A1; U.S. 20050003983A1; U.S. 20040048764A1; U.S. Pat. No. 4,762,636; U.S. Pat. No. 6,291,412; U.S. 20050227891A1; EP 1070115A2; U.S. Pat. No. 5,879,584; U.S. Pat. No. 5,691,297; U.S. Pat. No. 5,574,005; U.S. Pat. No. 5,569,645; U.S. Pat. No. 5,565,422; U.S. Pat. No. 5,516,448; U.S. Pat. No. 5,489,392; U.S. Pat. No. 5,486,303.

Method of Use

The present invention includes a method for cleaning and/or treating a situs inter alia a surface or fabric. Such method includes the steps of optionally washing and/or rinsing said surface or fabric, contacting said surface or fabric with a composition of the present invention in neat or diluted form such as in a wash liquor and then optionally washing and/or rinsing said surface or fabric. For purposes of the present invention, washing includes but is not limited to, scrubbing, and mechanical agitation. As will be appreciated by one skilled in the art, the cleaning compositions of the present invention are ideally suited for use in laundry applications. Accordingly, the present invention includes a method for laundering a fabric. The method may comprise the steps of contacting a fabric to be laundered with a said cleaning laundry solution comprising at least one embodiment of Applicants' cleaning composition, cleaning additive or mixture thereof. The fabric may comprise most any fabric capable of being laundered in normal consumer use conditions. The solution may have in one aspect a pH of from about 7.5 to about

10.5 or even a pH of from about 8 to about 10.5. The compositions may be employed at

concentrations of from about 500 ppm to about 15,000 ppm in solution. The water temperatures typically range from about 5° C. to about 90° C. The water to fabric ratio is typically from about 1:1 to about 30:1.

Test Methods Test Method 1 Procedure for Determining the Concentration of Free CALCIUM (Ca++) Basis of Method

Free calcium is assayed by using an ion specific electrode that is specific for calcium. This measurement technique is well known and is exemplified in many literature references, such as Analytical Chemistry, Vol 46, No 1, 1974, p. 12-15, and manuals exemplifying the use of such electrodes are broadly known and available (e.g. from Metrohm of Buckinghamshire, UK and from HACH LANGE LTD, Manchester, UK). The description below shows how such a technique may be applied to measurements of free calcium for detergents.

Calibration:

Before use, the electrodes must be calibrated. This may be done by measuring a series of known standard solutions, made by serial dilution of the 1000 ppm Calcium standard solution. For a full calibration, prepare 100 ml of solutions containing 1000, 100, 10, 1, and 0.1 ppm Ca2+.

Add 2 ml of Ionic Strength Adjustment Buffer (ISAB) solution to each standard and mix. Prepare a calibration graph.

Sample Preparation

    • a. To 6 separate IL volumetric flasks add, 0, 20, 30, 40, 50, 100 and 200 ml of 1000 ppm calcium standard solution and add deionised water to make the volume to 1 liter to make solutions containing 0, 20, 30, 40, 50, 100 & 200 ppm of calcium. Transfer each 1 liter calcium solution to a 1 liter tergotometer pot and stir for 10 mins on a standard tergotometer.
    • b. To 50 ml of each solution from Step a. above, add 1 ml of ISAB buffer and measure calcium. This serves to check that the initial solution contains the level of calcium expected.
    • c. To each tergotometer pot from Step a. above add sufficient detergent to give a detergent solution having the same concentration as would be realized by adding the detergent manufacturer's recommended dose of detergent to the standard volume within a washing machine or median hand-wash practices. (For example formulations 1-6, typical detergent concentration would be 1.5-3 g/liter; for example formulations 7-12, typical detergent concentration would be 8-9 g/liter; for example formulations 13-16, typical detergent concentration would be 1.5 g/liter; and for examples 17 & 18, typical detergent concentrations would be 8-9 g/liter). Stir for 10 mins.
    • d. To 50 ml of each solution from Step c., add 1 ml of ISAB buffer, immerse the electrode and take the calcium reading, once equilibrated (typically takes several seconds). This is the free calcium reading for the detergent composition.

Apparatus Used:

Ion-Selective Calcium Electrode: Ion-selective calcium electrodes are broadly available. The one used for this test is sourced from VWR International Ltd., Leicestershire, UK and comprises the following parts: Ion-Selective Electrode for calcium ion (such as ELIT 8041 PVC membrane); Reference electrode: single junction silver chloride (such as ELIT 001); Dual electrode head (such as ELIT 201); ELIT Computer Interface/Ion Analyzer attached to a Dell PC.

Standard solutions: The 1000 ppm calcium chloride solution can be made by dissolving calcium chloride (sourced from Sigma Aldrich of Milwaukee, US) in deionized water, and the buffer solution (ISAB) comprising 4 Molar KCl can be sourced from VWR International Ltd., Leicestershire, UK.

Standard Tergotometer: (e.g. models available from Copley Scientific, Nottingham, UK such as that sold under catalogue number Dissolution Tester DIS 8000).

Test Method 2 Procedure for Determining Enzyme Deposition Index Basis of Method:

This method compares the residual enzyme concentration of various amylases detectable by standard Double Antibody Sandwich ELISA (DAS-ELISA) methods, well known to those skilled in the art, by reaction with the appropriate antibodies (DAS-ELISA technique is exemplified in various patents, e.g. U.S. Pat. No. 5,188,937 & U.S. Pat. No. 6,818,804, and in various literature articles, e.g. L. S. Miller, “A robotic immunoassay system for detergent enzymes.” Laboratory Information Management, 1994, Vol 26, pgs 79-87; Butler, J. E. “The immunochemistry of sandwich ELISA's: principles and applications for the quantitative determination of immunoglobulins.” In “ELISA and Other Solid Phase Immunoassays. Theoretical and Practical Aspects” Eds Kemeny, D. M. and Challacombe, S. J. John Wiley and Sons, NY. 1988, pgs. 155-180 and references incorporated therein.) Standard calibration methods are used.

The enzyme deposition index (EDI) is the ratio of the (mass of test alpha-amylase protein extracted/g fabric) and the (mass of Termamyl® protein extracted/g fabric). Thus, the equation for cotton fabric is Equation 1. This method may be used, for example, to determine the suitability of an enzyme for use as a detergent ingredient and/or predict the performance of an enzyme in, for example, a detergent application.


EDI=(Mass of test alpha-amylase protein extracted per g cotton)/(Mass of Termamyl® extracted per g cotton)  Equation 1

Sample Preparation

    • 1. To separate tergotometer pots add 980 ml of water containing 145±10 ppm calcium and 2.0 g of sodium carbonate (sourced from SigmaAldrich of Milwaukee, USA). Stir for 10 minutes to dissolve. Allow to equilibrate to 40° C.
    • 2. Add 0.69 g of LAS (Linear alkylbenzenesulfonate having an average aliphatic carbon chain length C11-C12) and 0.38 g of AE3S(C12-15 alkyl ethoxy (3) sulfate), both supplied by Stepan, Northfield, Ill., USA. Stir to dissolve.
    • 3. Add liquid samples of the various enzymes to be studied to the different tergotometer pots to ensure 0.2 mg of amylase are present in each pot. One pot should contain 0.2 mg Termamyl® (available from Novozymes of Denmark) to act as the reference versus which the other enzymes are to be indexed.
    • 4. Adjust the water volume in each pot to 1 liter, if needed, using water containing 145±10 ppm calcium. The resultant solution should contain 690 ppm of LAS, 380 ppm AE3S, 2000 ppm of sodium carbonate and 0.2 ppm of the enzyme.
    • 5. To each tergotometer pot, add three standard cotton swatches (sourced ex. Center for Test Materials (CFT) B.V. of Holland) with fabric code CN03, each weighing 3.5±0.3 g. The total weight of cotton should be 10.5±0.5 g per tergotometer pot.
    • 6. Start the tergotometer run (conditions are 40±2° C., 150 rpm and run time is 20 minutes).
    • 7. After 20 minutes the fabrics are removed, hand squeezed until not excess liquid is visible and then rinsed for 5 minutes in a tergotometer in 1 liter of water containing 145±10 ppm calcium (conditions are 150 rpm agitation, with a water temperature of 25±2° C.).
    • 8. The swatches are removed and hand squeezed to remove excess liquor and then allowed to air dry at room temperature for 3-5 hours.
    • 9. An extraction buffer is prepared comprising of:
      • a. 0.93 g/L 2-Amino-2-(hydroxymethyl)-1,3-propanediol (otherwise known as Trizma base);
      • b. 4.96 g/L Sodium Thiosulphate pentahydrate;
      • c. 0.147 g/L Calcium Chloride dehydrate;
      • d. 29.22 g/L sodium Chloride;
      • e. 1.0 g Sodium Azide; and
      • f. 1.0 g/L Polyethylene glycol sorbitan monolaurate (otherwise known as Tween 20 with CAS #9005-64-5)
      • The pH of the buffer is adjusted to pH=8 using 0.1N hydrochloric acid prior to use.
      • All reagents are available from Sigma Aldrich Company Ltd. Dorset, UK.
    • 10. Each swatch of known weight is placed in a separate 50 ml extraction tube and 25 ml of extraction buffer is added. The tube is hand shaken vigorously for 1 minute (+/−10 s) then left to stand for 15 minutes (+/−1 minute) then shaken vigorously again for 1 minute (+/−10 s). The tube is allowed to stand for a further 15 minutes (+/−1 minute) before given a final vigorous shaking for 1 minute (+/−10 s).
    • 11. The resultant solution is assayed via standard ELISA methods using a Rosys Plato 7381 analyzer (Supplier Rosys Anthos GmbH Feldbachstr CH-8634 Hombrechtikon Switzerland or equivalent ELISA equipment such as those supplied by Dynex Technologies of Virginia, USA or Biotech of Vermont, USA).
    • 12. From this assay by comparing to the standard calibration curve, the mass of amylase protein detected can be determined and the mass of enzyme extracted/g of fabric can be calculated.
    • 13. The whole process (Steps 1-12) is repeated 3 more times to generate further sets of data.
    • 14. The enzyme deposition index is then calculated by taking the average of 12 readings expressed in ng amylase protein/g fabric (these twelve readings come from the three pieces of cloth per pot from each of the four runs) for each enzyme and indexing such value to that observed for Termamyl® protein as shown in Equation 1.

Equipment Used

Standard Tergotometer (e.g. models available from Copley Scientific, Nottingham, UK such as that sold under catalogue number Dissolution Tester DIS 8000).

EXAMPLES

Unless otherwise indicated, materials can be obtained from Aldrich, P.O. Box 2060, Milwaukee, Wis. 53201, USA.

Examples 1-6

Granular laundry detergent compositions designed for hand washing or top-loading washing machines.

1 2 3 4 5 6 (wt %) (wt %) (wt %) (wt %) (wt %) (wt %) Linear alkylbenzenesulfonate 20 22 20 15 20 20 C12-14 Dimethylhydroxyethyl 0.7 0.2 1 0.6 0.0 0 ammonium chloride AE3S 0.9 1 0.9 0.0 0.5 0.9 AE7 0.0 0.0 0.0 1 0.0 3 Sodium tripolyphosphate 5 0.0 4 9 2 0.0 Zeolite A 0.0 1 0.0 1 4 1 1.6R Silicate (SiO2:Na2O at 7 5 2 3 3 5 ratio 1.6:1) Sodium Carbonate 25 20 25 17 18 19 Polyacrylate MW 4500 1 0.6 1 1 1.5 1 Carboxy Methyl Cellulose 1 0.3 1 1 1 1 Amylase* (20 mg active/g) 0.1 0.2 0.1 0.2 0.1 0.1 Savinase ® (32.89 mg active/g) 0.1 0.1 0.1 0.1 0.1 0.1 Natalase ® (8.65 mg active/g) 0.1 0.0 0.1 0.0 0.1 0.1 Lipex ® (18 mg active/g) 0.03 0.07 0.3 0.1 0.07 0.4 Fluorescent Brightener 1 0.06 0.0 0.06 0.18 0.06 0.06 Fluorescent Brightener 2 0.1 0.06 0.1 0.0 0.1 0.1 DTPA 0.6 0.8 0.6 0.25 0.6 0.6 MgSO4 1 1 1 0.5 1 1 Sodium Percarbonate 0.0 5.2 0.1 0.0 0.0 0.0 Sodium Perborate 4.4 0.0 3.85 2.09 0.78 3.63 Monohydrate NOBS 1.9 0.0 1.66 0.0 0.33 0.75 TAED 0.58 1.2 0.51 0.0 0.015 0.28 Sulphonated zinc 0.0030 0.0 0.0012 0.0030 0.0021 0.0 phthalocyanine S-ACMC 0.1 0.0 0.0 0.0 0.06 0.0 Direct Violet 9 0.0 0.0 0.0003 0.0005 0.0003 0.0 Acid Blue 29 0.0 0.0 0.0 0.0 0.0 0.0003 Sulfate/Moisture* *Balance to 100% for Examples 1-6

Examples 7-12

Granular laundry detergent compositions designed for front-loading automatic washing machines.

7 8 9 10 11 12 (wt %) (wt %) (wt %) (wt %) (wt %) (wt %) Linear alkylbenzenesulfonate 8 7.1 7 6.5 7.5 7.5 AE3S 0 4.8 0 5.2 4 4 Alkylsulfate 1 0 1 0 0 0 AE7 2.2 0 3.2 0 0 0 C10-12 Dimethyl 0.75 0.94 0.98 0.98 0 0 hydroxyethylammonium chloride Crystalline layered silicate (δ- 4.1 0 4.8 0 0 0 Na2Si2O5) Zeolite A 5 0 5 0 2 2 Citric Acid 3 5 3 4 2.5 3 Sodium Carbonate 15 20 14 20 23 23 Silicate 2R (SiO2:Na2O at ratio 0.08 0 0.11 0 0 0 2:1) Soil release agent 0.75 0.72 0.71 0.72 0 0 Acrylic Acid/Maleic Acid 1.1 3.7 1.0 3.7 2.6 3.8 Copolymer Carboxymethylcellulose 0.15 1.4 0.2 1.4 1 0.5 Protease (84 mg active/g) 0.2 0.2 0.3 0.15 0.12 0.13 Amylase* (20 mg active/g) 0.2 0.15 0.2 0.3 0.15 0.15 Lipex ® (18.00 mg active/g) 0.05 0.15 0.1 0 0 0 Natalase ® (8.65 mg active/g) 0.1 0.2 0 0 0.15 0.15 Celluclean ™ (15.6 mg active/g) 0 0 0 0 0.1 0.1 TAED 3.6 4.0 3.6 4.0 2.2 1.4 Percarbonate 13 13.2 13 13.2 16 14 Na salt of Ethylenediamine-N,N′- 0.2 0.2 0.2 0.2 0.2 0.2 disuccinic acid, (S,S) isomer (EDDS) Hydroxyethane di phosphonate 0.2 0.2 0.2 0.2 0.2 0.2 (HEDP) MgSO4 0.42 0.42 0.42 0.42 0.4 0.4 Perfume 0.5 0.6 0.5 0.6 0.6 0.6 Suds suppressor agglomerate 0.05 0.1 0.05 0.1 0.06 0.05 Soap 0.45 0.45 0.45 0.45 0 0 Sulphonated zinc phthalocyanine 0.0007 0.0012 0.0007 0 0 0 (active) S-ACMC 0.01 0.01 0 0.01 0 0 Direct Violet 9 (active) 0 0 0.0001 0.0001 0 0 Sulfate/Water & Miscellaneous* *Balance to 100% for Examples 7-12

Any of the above compositions is used to launder fabrics at a concentration of 7000 to 10000 ppm in water, 20-90° C., and a 5:1 water:cloth ratio. The typical pH is about 10.

Examples 13-18 Heavy Duty Liquid Laundry Detergent Compositions Raw Materials and Notes For Composition Examples 1-18

13 14 15 16 17 18 (wt %) (wt %) (wt %) (wt %) (wt %) (wt %) AES C12-15 alkyl 11 10 4 6.32 0 0 ethoxy (1.8) sulfate AE3S 0 0 0 0 2.4 0 Linear alkyl 1.4 4 8 3.3 5 8 benzene sulfonate HSAS 3 5.1 3 0 0 0 Sodium formate 1.6 0.09 1.2 0.04 1.6 1.2 Sodium hydroxide 2.3 3.8 1.7 1.9 1.7 2.5 Monoethanolamine 1.4 1.49 1.0 0.7 0 0 Diethylene glycol 5.5 0.0 4.1 0.0 0 0 Nonionic 23.9 0.4 0.6 0.3 0.3 0 0 Nonionic 24.7 0 0 0 0 2.4 6 Chelant 0.15 0.15 0.11 0.07 0.5 0.11 Citric Acid 2.5 3.96 1.88 1.98 0.9 2.5 C12-14 dimethyl 0.3 0.73 0.23 0.37 0 0 Amine Oxide C12-18 Fatty Acid 0.8 1.9 0.6 0.99 3.5 2.5 Borax 1.43 1.5 1.1 0.75 1 1.07 Ethanol 1.54 1.77 1.15 0.89 0 3 Ethoxylated (EO15) 0.3 0.33 0.23 0.17 0.0 0.0 tetraethylene pentaimine1 Ethoxylated 0.8 0.81 0.6 0.4 1 1 hexamethylene diamine2 1,2-Propanediol 0.0 6.6 0.0 3.3 0.5 2 Protease (40.6 mg active/g) 0.8 0.6 0.7 0.9 0.7 0.6 Mannaway ® (25 mg active/g) 0.07 0.05 0.045 0.06 0.04 0.045 Amylase* (15 mg active/g) 0.3 0.2 0.3 0.1 0.2 0.4 Natalase ® (29 mg 0 0.2 0.1 0.15 0.07 0 active/g) Lipex ® (18 mg active/g) 0.4 0.2 0.3 0.1 0.2 0 Liquitint ® Violet 0.006 0.002 0 0 0 0.002 CT (active) S-ACMC — — 0.01 0.05 0.01 0.02 Water, perfume, dyes & Balance Balance Balance Balance Balance Balance other components

Raw Materials and Notes For Composition Examples 1-18

Linear alkylbenzenesulfonate having an average aliphatic carbon chain length C11-C12 supplied by Stepan, Northfield, Ill., USA

C12-14 Dimethylhydroxyethyl ammonium chloride, supplied by Clariant GmbH, Sulzbach, Germany

    • AE3S is C12-15 alkyl ethoxy (3) sulfate supplied by Stepan, Northfield, Ill., USA

AE7 is C12-15 alcohol ethoxylate, with an average degree of ethoxylation of 7, supplied by Huntsman, Salt Lake City, Utah, USA

Sodium tripolyphosphate is supplied by Rhodia, Paris, France

Zeolite A is supplied by Industrial Zeolite (UK) Ltd, Grays, Essex, UK

1.6R Silicate is supplied by Koma, Nestemica, Czech Republic

Sodium Carbonate is supplied by Solvay, Houston, Tex., USA

Polyacrylate MW 4500 is supplied by BASF, Ludwigshafen, Germany

Carboxy Methyl Cellulose is Finnfix® BDA supplied by CP Kelco, Arnhem, Netherlands

Suitable chelants are, for example, diethylenetetraamine pentaacetic acid (DTPA) supplied by Dow Chemical, Midland, Mich., USA or Hydroxyethane di phosphonate (HEDP) supplied by Solutia, St Louis, Mo., USA Bagsvaerd, Denmark

Protease (examples 7-12) described in U.S. Pat. No. 6,312,936 B1 supplied by Genencor International, Palo Alto, Calif., USA

Protease (examples 13-18) described in U.S. Pat. No. 4,760,025 is supplied by Genencor International, Palo Alto, Calif., USA

    • A suitable amylase is, for example, Optisize® HT Plus supplied by Genencor International, Palo Alto, Calif., USA, or any of the other amylases specifically described in the present specification.

Fluorescent Brightener 1 is Tinopal® AMS, Fluorescent Brightener 2 is Tinopal® CBS-X, Sulphonated zinc phthalocyanine and Direct Violet 9 is Pergasol® Violet BN-Z all supplied by Ciba Specialty Chemicals, Basel, Switzerland

Sodium percarbonate supplied by Solvay, Houston, Tex., USA

Sodium perborate is supplied by Degussa, Hanau, Germany

NOBS is sodium nonanoyloxybenzenesulfonate, supplied by Eastman, Batesville, Ark., USA

TAED is tetraacetylethylenediamine, supplied under the Peractive® brand name by Clariant GmbH, Sulzbach, Germany

S-ACMC is carboxymethylcellulose conjugated with C.I. Reactive Blue 19, sold by Megazyme, Wicklow, Ireland under the product name AZO-CM-CELLULOSE, product code S-ACMC.

Soil release agent is Repel-o-tex® PF, supplied by Rhodia, Paris, France

Acrylic Acid/Maleic Acid Copolymer is molecular weight 70,000 and acrylate:maleate ratio 70:30, supplied by BASF, Ludwigshafen, Germany

Na salt of Ethylenediamine-N,N′-disuccinic acid, (S,S) isomer (EDDS) is supplied by Octel, Ellesmere Port, UK

Hydroxyethane di phosphonate (HEDP) is supplied by Dow Chemical, Midland, Mich., USA

Suds suppressor agglomerate is supplied by Dow Corning, Midland, Mich., USA

HSAS is mid-branched alkyl sulfate as disclosed in U.S. Pat. No. 6,020,303 and U.S. Pat. No. 6,060,443

C12-14 dimethyl Amine Oxide is supplied by Procter & Gamble Chemicals, Cincinnati, Ohio, USA

Liquitint(Violet CT is supplied by Milliken, Spartanburg, S.C., USA)

1 as described in U.S. Pat. No. 4,597,898.

2 available under the tradename LUTENSIT® from BASF and such as those described in WO 01/05874

The dimensions and values disclosed herein are not to be understood as being strictly limited to the exact numerical values recited. Instead, unless otherwise specified, each such dimension is intended to mean both the recited value and a functionally equivalent range surrounding that value. For example, a dimension disclosed as “40 mm” is intended to mean “about 40 mm”.

All documents cited in the Detailed Description of the Invention are, in relevant part, incorporated herein by reference; the citation of any document is not to be construed as an admission that it is prior art with respect to the present invention. To the extent that any meaning or definition of a term in this document conflicts with any meaning or definition of the same term in a document incorporated by reference, the meaning or definition assigned to that term in this document shall govern.

While particular embodiments of the present invention have been illustrated and described, it would be obvious to those skilled in the art that various other changes and modifications can be made without departing from the spirit and scope of the invention. It is therefore intended to cover in the appended claims all such changes and modifications that are within the scope of this invention.

Claims

1. A composition comprising an amylase having Seq. I.D. 1 and based on total product weight, less than 15% builder.

2. The composition of claim 1, said composition comprising a material selected from the group consisting of surfactants, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleaching agents, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids, solvents, pigments, hueing agents, photobleaches, structurants, and mixtures thereof.

3. The composition of claim 2, said composition comprising an additional enzyme.

4. The composition of claim 3, wherein said additional enzyme is selected from the group consisting of hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, amylases, and mixtures thereof.

5. The composition of claim 4, wherein said additional enzyme is selected from the group consisting of:

a.) lipases;
b.) alpha-amylases;
c.) serine proteases;
d.) microbial-derived endoglucanases; and
e.) mixtures thereof.

6. The composition of claim 2, said composition comprising a surfactant, selected from the group of:

a.) anionic surfactants selected from the group consisting of linear alkylbenzene-sulfonate (LAS), alcohol ethoxysulfate (AES), mid-branched alkyl sulfates (HSAS) and mixtures thereof;
b.) non ionic alcohol ethoxylates, said alcohol ethoxylates;
c.) amine oxides; and
d.) mixtures thereof.

7. The composition of claim 2, said composition comprising a polymer, selected from the group consisting of

a.) polyacrylates;
b.) maleic/acrylic acid copolymers;
c.) cellulose-derived polymers;
d.) polyethyleneimine polymer; and
e.) mixtures thereof.

8. The composition of claim 2, said composition comprising a material selected from the group consisting of a photobleach, a fabric hueing agent and mixtures thereof, said photobleach being selected from the group consisting of

a.) xanthene dyes;
b.) sulfonated zinc phthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y, Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures thereof;
c.) water soluble phthalocyanine; and
d.) mixtures thereof
and said fabric hueing agent being selected from the group consisting of
a.) dyes;
b.) dye-clay conjugates comprising at least one cationic/basic dye and a smectite clay; and
c.) mixtures thereof.

9. The composition of claim 8, said composition comprising, based on total product weight, from about 0% to about 3% photobleach and/or from about 0.00003% to about 0.3% hueing agent.

10. A composition comprising an amylase enzyme having E.C. 3.2.1.1, and a material selected from the group consisting of surfactants, chelating agents, dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleaching agents, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids, solvents, pigments, hueing agents, photobleaches, structurants, and mixtures thereof, said composition having an enzyme deposition index of at least 2.5.

11. The composition of claim 10, said composition comprising an additional enzyme.

12. The composition of claim 11, wherein said additional enzyme is selected from the group consisting of hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, amylases, or mixtures thereof.

13. The composition of claim 12, wherein said additional enzyme is selected from the group consisting of:

a.) lipases;
b.) alpha-amylases;
c.) serine proteases;
d.) microbial-derived endoglucanases; and
e.) mixtures thereof.

14. The composition of claim 10, said composition comprising a surfactant, selected from the group of:

a.) anionic surfactants selected from the group consisting of linear alkylbenzene-sulfonate (LAS), alcohol ethoxysulfate (AES), mid-branched alkyl sulfates (HSAS) and mixtures thereof;
b.) non ionic alcohol ethoxylates;
c.) amine oxides; and
d.) mixtures thereof.

15. The composition of claim 10, said composition comprising a polymer selected from the group consisting of:

a.) polyacrylates;
b.) maleic/acrylic acid copolymers;
c.) cellulose-derived polymers;
d.) polyethyleneimine polymer; and
e.) mixtures thereof.

16. The composition of claim 10, said composition comprising a builder selected from the group consisting of

a.) citric acid;
b.) C12-C18 fatty acid;
c.) aluminosilicates;
d.) sodium tripolyphosphate; and
e.) mixtures thereof.

17. The composition of claim 16, said composition comprising, based on total product weight, less than 15% builder.

18. The composition of claim 10, said composition comprising a material selected from the group consisting of a photobleach, a hueing agent and mixtures thereof, said photobleach being selected from the group consisting of

a.) xanthene dyes;
b.) sulfonated zinc phthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y, Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures thereof;
c.) water soluble phthalocyanine; and
d.) mixtures thereof
and said fabric hueing agent being selected from the group consisting of
a.) dyes;
b.) dye-clay conjugates comprising at least one cationic/basic dye and a smectite clay; and
c.) mixtures thereof.

19. The composition of claim 18, said composition comprising, based on total product weight, from about 0% to about 3% photobleach and/or from about 0.00003% to about 0.3% hueing agent.

20. A composition comprising an amylase having Seq. I.D. 1 and a sufficient amount of calcium to provide a wash liquor comprising said composition with a free calcium concentration of from about 0.1 ppm to about 500 ppm.

21. A method of determining the deposition index of an enzyme, said method comprising determining the enzyme deposition index of an enzyme according to Test Method 2.

Patent History
Publication number: 20090325852
Type: Application
Filed: Aug 28, 2009
Publication Date: Dec 31, 2009
Inventors: Eva Maria Perez-Prat Vinuesa (Newcastle), Colin Ure (Newcastle), Andre Cesar Baeck (Bonheiden), Philip Frank Souter (Morpeth)
Application Number: 12/549,525
Classifications
Current U.S. Class: Enzyme Component Of Specific Activity Or Source (e.g., Protease, Of Bacterial Origin, Etc.) (510/392); Sandwich Assay (435/7.94)
International Classification: C11D 3/386 (20060101); G01N 33/573 (20060101);