GB2353280A - Methods for activating enzymes - Google Patents

Methods for activating enzymes Download PDF

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GB2353280A
GB2353280A GB0013365A GB0013365A GB2353280A GB 2353280 A GB2353280 A GB 2353280A GB 0013365 A GB0013365 A GB 0013365A GB 0013365 A GB0013365 A GB 0013365A GB 2353280 A GB2353280 A GB 2353280A
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enzyme
enzymes
protease
detergent
cleaning
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GB0013365D0 (en
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Ashoke Kumar Mitra
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Procter and Gamble Co
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Procter and Gamble Co
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2414—Alpha-amylase (3.2.1.1.)
    • C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N13/00—Treatment of microorganisms or enzymes with electrical or wave energy, e.g. magnetism, sonic waves
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
    • C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/40—Specific cleaning or washing processes
    • C11D2111/46—Specific cleaning or washing processes applying energy, e.g. irradiation

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • Biomedical Technology (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Detergent Compositions (AREA)

Abstract

The present invention relates to methods for activating enzymes, preferably detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, and compositions, preferably detergent compositions comprising such activated enzymes. More particularly, the present invention relates to methods for activating enzymes, preferably detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, comprising subjecting the enzymes to a source of microwave irradiation sufficient to activate said enzymes such that said irradiated enzymes exhibit an activity greater than said non-irradiated enzymes.

Description

)95/3D 2353280 METHOD FOR ACTIVATING ENZYMES AND CLEANING COMPOSITIONS
COMPRISING SUCH ACTIVATED ENZYMES
Technical Field of the Invention
The present invention relates to methods for activating enzymes, preferably detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, and compositions, preferably detergent compositions comprising such activated enzymes. More particularly, the present invention relates to methods for activating enzymes, preferably detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, comprising subjecting the enzymes to a source of microwave irradiation sufficient to activate said enzymes such that said irradiated enzymes exhibit an activity greater than said non-irradiated enzymes.
Background of the Invention
Cleaning and detergent compositions containing enzymes are well known in the art. However, there is a continuing need for more effective cleaning by the enzymes within such cleaning and detergent compositions.
Enzymes, however, are known to have compatibility problems with various components of cleaning and detergent compositions and various conditions under which cleaning and detergent compositions are used.
Microwaving of biological enzymes is known in the art as described in WO 93/21344; Byus et al., Cancer Res. (1988) 48:4222-4226; Ward et al., J. Microwave Power (1975) 10:315320; Meltz et a]., Radiat. Res. (1987) 110:255-66; Dutta, S.K. and Verma, M., Cuff. Sci. (1989) 58:58-63;; and Dutta, S.K. and Verma, M., Curr. Sci. (1988) 57:779-786. However, microwaving of enzymes for enhancing the cleaning (soil and/or stain removal) properties of the enzymes is not disclosed in such references.
Accordingly, a need exists for enzymes with enhanced activities for use in cleaning and/or detergent compositions.
2 Summary of the Invention
The method of the present invention for activating an enzyme, preferably a detergent enzyme, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, comprising subjecting said enzyme to a source of microwave irradiation sufficient to activate said enzyme such that said irradiated enzyme exhibits an activity greater than said non- irradiated enzyme fulfills the need discussed above. Also, the detergent compositions comprising the activated enzymes fulfill the needs discussed above.
In one aspect of the present invention a method for activating an enzyme, preferably detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, comprising subjecting said enzyme to a source of microwave irradiation sufficient to activate said enzyme such that said irradiated enzyme exhibits an activity greater than said non-irradiated enzyme is provided.
In another aspect of the present invention a detergent composition comprising an activated enzyme, preferably detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases, wherein said activated enzyme is activated by subjecting said enzyme to a source of microwave irradiation sufficient to activate said enzyme such that said irradiated enzyme exhibits an activity greater than said non-irradiated enzyme; and one or more cleaning adjunct materials.
Accordingly, the present invention provides a method for activating an enzyme; and a detergent composition comprising an activated enzyme activated by the method of the present invention.
Detailed Description of the Invention
Method for Activation The method for activating an enzyme of the present invention comprises subjecting said enzyme to microwave irradiation sufficient to activate said enzyme such that said irradiated enzyme exhibits an activity greater than said non-irradiated enzyme.
EnZymes - Suitable enzymes for use with the method of the present invention are described hereinafter. Preferably, the enzymes are detergent enzymes, more preferably lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof, most preferably proteases and/or amylases.
Source of Microwave Irradiation - Any means known to the art for providing microwave irradiation can be used for the method of the present invention. For example, a microwave oven that is part of standard equipment in most biological laboratories and a domestic microwave 3 oven. Preferably, the source of microwave irradiation is a domestic microwave oven. A commercially available domestic microwave ovens are the Panasonic Golden Premier microwave oven, the Whirlpool Model MH7135XEQ (900 watts) microwave oven and the Amana Model R 311 (700 watts) microwave oven.
It is desirable that the source of microwave irradiation provide maximum power levels of from about 500 to about 2000 watts, more preferably from about 750 to about 1500 watts, most preferably from about 900 to about I 100 watts.
Conditions:.
i. Power - Any power provided by the source of microwave irradiation that results in an enzyme exhibiting greater activity than the same enzyme without being subjected to microwave irradiation can be used. The method of the present invention is preferably carried out at a power of from about 50 to 1200 watts, more preferably from about 50 to about 880 watts, still even more preferably from about 75 to about 560 watts, most preferably from about 90 to about 370 watts.
ii. Frequena - Any frequency provided by the source of microwave irradiation that results in an enzyme exhibiting greater activity than the same enzyme without being subjected to microwave irradiation can be used. The method of the present invention is preferably carried out at a frequency of from about I to about 1000 gigahertz (GRz), more preferably, from about 2 to about 100 GHz; most preferably, from about 2 to about 12 GHz.
iii. Timing - The enzyme to be activated can be subjected to microwave irradiation for any period of time so long as the enzyme does not become deactivated or begin to lose enzymatic activity. Preferably, the enzyme to be activated is subjected to microwave irradiation from about I second to about 10 minutes, more preferably from about 10 seconds to about 5 minutes, most preferably from about 15 seconds to about I minute.
iv. Buffer - Preferably, the enzyme to be activated is present in a buffer solution, preferably a standard biological buffer system, more preferably a buffer system selected from the group consisting of. Tris, phosphate, acetate as well as detergent matrices with pH's from about 6 to about I I and ionic strengths from about 0. 1 mM to about I M.
Effect of Activation By subjecting the enzymes of the present invention to microwave irradiation, the irradiated enzymes exhibit a greater activity than the non-irradiated enzyme. These activation effects are enzyme and matrix specific. Microwave irradiation adsorption onto the enzymes depends on both the dipole moment of the enzyme and the dielectric constant of the surrounding medium. Accordingly, not all enzymes are activated by irradiation the same way under the same conditions.
4 Preferably, the irradiated enzymes exhibit from at least 10% more activity than the nonirradiated enzymes. More preferably, the irradiated enzymes exhibit from about 10% to about 200% more activity than the nonirradiated enzymes. Still even more preferably, the irradiated enzymes exhibit from about 20% to about 100% more activity than the nonirradiated enzymes. Most preferably, the irradiated enzymes exhibit from about 30% to about 80% more activity than the non-irradiated enzymes. All of these activity measurements are measured by the pNA and casein activities and/or p-nitrophenol method (SIGMA kit 577).
The irradiated enzymes also retain their enhanced activities or a portion of their enhanced activities for over I hour, preferably, the irradiated enzymes retain their enhanced activities or a portion of their enhanced activities from about I hour to about 14 days, more preferably from about 5 hours to about 7 days, most preferably from about 12 hours to about 3 days.
The activated enzymes of the present invention preferably provide improved soil and/or stain removal of enzyme-specific soils and/or stains as compared to the non-activated enzymes. Examples of soils and/or stains include, but are not limited to, grass, blood, BMI, chili, mushroom soup, spaghetti sauce, baby food, barbeque sauce, EnZymes Examples of suitable enzymes useful in the present invention include, but are not limited to, hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, B-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, and known amylases, or mixtures thereof. A preferred combination is a cleaning and/or detergent composition having a cocktail of conventional applicable enzymes like protease, lipase, cutinase and/or cellulase in conjunction with an amylase of the present invention. Particularly useful in the methods and compositions of the present invention are detergent enzymes.
Examples of such suitable detergent enzymes are disclosed in U.S. Patent Nos. 5,576,282, 5,728,671 and 5,707,950.
Preferred detergent enzymes for use in the present invention are selected from the group consisting of lipases, mannanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof. More preferably the detergent enzymes for use in the present invention are selected from the group consisting of amylases, proteases and mixtures thereof.
Eroteases - Suitable proteases are the subtilisins which are obtained from particular strains of B. subtilis and B. licheniformis (subtilisin BPN and BPN'). One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASES 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 ALCALASE8, DURAZYM%) and SAVINASEO from Novo and MAXATASES, MAXACALO, PROPERASES and MAXAPEM& (protein engineered Maxacal) from Gist-Brocades. Proteolytic enzymes also encompass modified bacteria] serine proteases, such as those described in European Patent Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called "Protease A" herein. More preferred is what is called herein "Protease C", which is a variant of an alkaline serine protease from Bacillus in which lysine replaced arginine at position 27, tyrosine replaced valine at position 104, serine replaced asparagine at position 123, and alanine replaced threonine at position 274. Protease C is described in EP 90915958:4, corresponding to WO 91/06637, Published May 16, 1991. Genetically modified variants, particularly of Protease C, are also included herein. See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO 93/18140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO 92/03529 A to Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter & Gamble. A recombinant trypsin-like protease for detergents suitable herein is described in WO 94/25583 to Novo.
In more detail, the protease referred to as "Protease D" is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a position in said carbonyl hydrolase equivalent to position +76, preferably also in combination with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +101, +103, +104, +107, + 123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, + 206, +210, +216, +217, +218, +222, +260, +265, and/or +274 according to the numbering of Bacillus amyloliquefaciens subtilisin, as described in WO 95/10615 published April 20, 1995 by Genencor International. Also suitable for the present invention are proteases described in patent applications EP 251 446 and W091/06637 and protease BLAPS described in W091/02792. The proteolytic enzymes are incorporated in the cleaning and/or detergent compositions of the present invention a level of from 0. 0001% to 2%, preferably from 0.00 1% to 0.2%, more preferably from 0.005% to 0. 1% pure enzyme by weight of the composition.
Useful proteases are also described in PCT publications: WO 95/30010 published November 9,1995 by The Procter & Gamble Company; WO 95/30011 published November 9, 6 1995 by The Procter & Gamble Company; WO 95/29979 published November 9, 1995 by The Procter & Gamble Company.
Other particularly useful proteases are multiply-substituted protease variants comprising a substitution of an amino acid residue with another naturally occurring amino acid residue at an amino acid residue position corresponding to position 103 of Bacillus amyloliquefaciens subtilisin in combination with a substitution of an amino acid residue with another naturally occurring amino acid residue at one or more amino acid residue positions corresponding to positions 1, 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21, 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 101, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128, 130, 131, 133, 134, 137, 140, 141, 142, 146, 147, 158, 159, 160, 166, 167, 170, 173, 174, 177, 181, 182, 183, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 265, 268, 269, 270, 271, 272, 274 and 275 of Bacillus amyloliquefaciens subtilisin; wherein when said protease variant includes a substitution of amino acid residues at positions corresponding to positions 103 and 76, there is also a substitution of an amino acid residue at one or more amino acid residue positions other than amino acid residue positions corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens subtilisin and/or multiply-substituted protease variants comprising a substitution of an amino acid residue with another naturally occurring amino acid residue at one or more amino acid residue positions corresponding to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtilisin as described in PCT Publication Nos. WO 99/20727, WO 99/20726, WO 99/20770 and WO 99/20769 to The Procter & Gamble Company and Genencor International, Inc., and PCT Publication No. WO 99/20723 to The Procter & Gamble Company. More preferably the protease variant includes a substitution set selected from the group consisting of 12n6/103/104/130/222/245/26 1; 62/103/104/159/232/236/245/248/252; 62/103/104/159/213/232/236/245/248/252; 62/101/103/104/159/212/213/232/236/245/248/252; 68/103/104/159/232/236/245; 68/103/104/159/230/232/236/245; 68/103/104/159/209/232/236/245; 68/103/104/159/232/236/245/257; 68/76/103/104/159/213/232/236/245/260; 68/103/104/159/213/232/236/245/248/252; 7 68/103/104/159/183/232/236/245/248/252; 68/103/104/159/185/232/236/245/248/252; 68/1031104/159/185/210/232/236/245/248/252; 68/103/1041159/210/232/236/245/248/252; 68/1031104/15912131232/2361245; 98/103/104/159/232/236/245/248/252; 9811021103/104/159/212/232/236/245/248/252; 10 1/103/10411591232/236/245/248/252; 102/103/104/159/232/236/245/248/252; 1031104/159/230/236/245; 103/1041159/232/236/245/248/252; 103/104/159/21712321236/245/248/252; 103/104/1301159/232/236/245/248/252; 103/104/131/159/232/2361245/2481252; 103/104/1591213/232/236/245/248/252; and 10311041159/232/236/245. Still even more preferably the protease variant includes a substitution set selected from the group consisting of.
12R/76D/103A/104T/130T/222S/245R/261D; 62D/103A/1041/159D/232V/236H]245R/248D/252K; 62D/103A/1041/159D/213R/232V/236H/245R/248D/252K; 68A/103A/10411159D/209W/232V/236H/245R; 68A/76D/103A/1041/159D/213R/232V/236I-F245R/260A; 68A/103A/1041/159D/213E/232V/236H/245R/248D/252K; 68A/103A/1041/159D/183D/232V/236H/245R/248D/252K; 68A/103A/10411159D/232V/236H/245R; 68A/103A/10411159D/23OV/232V/236H/245R; 68A/103A/10411159D/232V/236H/245R/257V; 68A/103A/1041/159D/213G/232V/236W245R/248D/252K; 68A/103A/10411159D/185D/232V/236H/245R/248D/252K; 68A/103A/10411159D/185D/21OL/232V/236H/245R/248D/252K; 68A/103A/10411159D/210L/232V/236H/245R/248D/252K; 68A/ 103 All 0411159D/213 G/23 2V/23 6H/24511; 98L/103A/1041/159D/232V/236H]245R/248D/252K; 98L/102A/103A/104I/159D/212G/232V/236H/245R/248D/252K; IOIG/103A/1041/159D/232V/236I-11245R/248D/252K; 8 102A/I 03A/l 041/159D/232V/236H/245R/248D/252K; 103A/l 041/159D/23OV/236H/245R; 103A/l 041/1 59D/232V/236H]245R/248D/252K; 103A/I 041/159D/217E/232V/236H/245R/248D/252K; 103A/I 041/13OG/I 59D/232V/23614/245R/248D/252K; 103A/l 041/13 IV/I 59D/232V/236H/245R/248D/252K; 103A/1041/159D/213R/232V/236IU245R/248D/252K; and 103A/l 041/159D/232V/236fU245R.
Most preferably the protease variant includes the substitution set 101/103/104/159/232/236/245/248/252, preferably 10IG/103A/1041/159D/232V/ 236H/245R/248D/252K.
Also suitable for the present invention are proteases described in patent applications EP 251 446 and WO 91/06637, protease BLAPS described in W091/02792 and their variants described in WO 95/23221.
See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO 93/18140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO 92/03529 A to Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter & Gamble. A recombinant trypsin-like protease for detergents suitable herein is described in WO 94/25583 to Novo. Other suitable proteases are described in EP 516 200 by Unilever.
Commercially available proteases useful in the present invention are known as ESPERASEO, ALCALASEO, DURAZYMO, SAVINASE8, EVERLASE8 and KANNASE8 all from Novo Nordisk A/S of Denmark, and as MAXATASEO, MAXACALO, PROPERASE9 and MAXAPEMO all from Genencor International (formerly Gist- Brocades of The Netherlands).
Also in relation to enzymes herein, enzymes and their directly linked inhibitors, e.g., protease and its inhibitor linked by a peptide chain as described in WO 98/13483 A, are useful in conjunction with the present hybrid builders. Enzymes and their non-linked inhibitors used in selected combinations herein include protease with protease inhibitors selected from proteins, peptides and peptide derivatives as described in WO 98/13461 A, WO 98/13460 A, WO 98/13458 A, WO 98/13387 A.
Highly preferred proteases for use in the present invention are SAVINASEO commercially available from Novo Nordisk A/S of Denmark and "Protease D", especially where the protease includes mutations at positions equivalent to 76/103/104 according to the 9 numbering of Bacillus amyloliquefaciens subtilisin, as described in WO 95/10615 published April 20, 1995 by Genencor International.
Arnylases - Suitable amylases include both a- and f-amylases. Nonlimiting examples of suitable amylases are described in WO 94/02597, Novo Nordisk A/S published February 03, 1994, W094/18314, Genencor, published August 18, 1994 and W095/10603, Novo Nordisk A/S, published April 20, 1995. Other suitable amylases are a-amylases, which include, but are not limited to, those disclosed in US Pat. 5,003,257; EP 252,666; WO 91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British Patent Specification No. 1,296,839 (Novo). Other suitable amylases are stability- enhanced amylases including PURAFACT OX AM@ described in WO 94/18314, published August 18, 1994 and W096/05295, Genencor, published February 22, 1996.
Examples of commercial oc-amylases products are TERMAMYLO, BAN@, FUNGAMYL(D and DURAMYLO, all available from Novo Nordisk A/S Denmark. W095/26397 describes other suitable amylases: a-amylases characterized by having a specific activity at least 25% higher than the specific activity of TERMAMYLO at a temperature range of 251C to 55'C and at a pH value in the range of 8 to 10, measured by the Phadebas(g) (xamylase activity assay. Other amylolytic enzymes with improved properties with respect to the activity level and the combination of thermostability and a higher activity level are described in W095/35382.
Highly preferred amylases for use in the present invention include DURAMYLO.
Bleach/amylase/protease combinations (EP 755,999 A; EP 756,001 A; EP 756, 000 A) are also useful.
Mannanases - Suitable mannanases are selected from the group consisting of. three mannans-degrading enzymes: EC 3.2.1.25: fmannosidase, EC 3.2.1. 78: Endo-1,4-f3mannosidase, referred therein after as "mannanase" and EC 3.2.1.100: 1,4-P-mannobiosidase and mixtures thereof (JUPAC Classification- Enzyme nomenclature, 1992 ISBN 0-12-2271653 Academic Press).
More preferably, the compositions of the present invention, when a mannanase is present, comprise a 0-1,4-Mannosidase (E.C. 3.2.1.78) referred to as Mannanase. The term "mannanase" or "galactomannanase" denotes a mannanase enzyme defined according to the art as officially being named mannan endo-1,4-beta-mannosidase and having the alternative names beta-mannanase and endo-1,4-mannanase and catalyzing the reaction: random hydrolysis of 1,4beta-D- mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomarmans.
In particular, Mannanases (EC 3.2.1.78) constitute a group of polysaccharases which degrade mannans and denote enzymes which are capable of cleaving polyose chains containing mannose units, i.e. are capable of cleaving glycosidic bonds in mannans, glucomannans, galactomannans and galactogluco-mannans. Mannans are polysaccharides having a backbone composed of f-1,4- linked mannose; glucomannans are polysaccharides having a backbone or more or less regularly alternating P-1,4 linked mannose and glucose; galactomannans and galactoglucomannans are mannans and glucomannans with oc-1,6 linked galactose side branches. These compounds may be acetylated.
The degradation of galactomannans and galactoglucomannans is facilitated by full or partial removal of the galactose side branches. Further the degradation of the acetylated mannans, glucomannans, galactomannans, and galactogluco-mannans is facilitated by full or partial deacetylation. Acetyl groups can be removed by alkali or by mannan acetylesterases. The oligomers which are released from the mannanases or by a combination of mannanases and ocgalactosidase and/or mannan acetyl esterases can be further degraded to release free maltose by f-mannosidase and/or fglucosidase.
Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, No. 11, pp. 3505-3510 (1990) describes a betamannanase derived from Bacillus stearothermophilus in dimer form having molecular weight of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from Bacillus subtilis having a molecular weight of 38 kDa, an optimum activity at pH 5.0 and 55C and a pI of 4.8. JP03047076 discloses a beta- mannanase derived from Bacillus sp., having a molecular weight of 373 kDa measured by gel filtration, an optimum pH of 8-10 and a pI of 5.3-5.4. JP- 63056289 describes the production of an alkaline, thermostable beta- mannanase which hydrolyses beta1,4-D-mannopyranoside bonds of e.g. mannans and produces manno-oligosaccharides. JP63036774 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and betamannosidase at an alkaline pH. JP-08051975 discloses alkaline betamannanases from alkalophilic Bacillus sp. AM-001. A purified mannanase from Bacillus amyloliquefaciens useful in the bleaching of pulp and paper and a method of preparation thereof is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active at an extreme pH and temperature. WO 94/25576 discloses an enzyme from Aspergillus aculeatus, CBS 101.43, exhibiting mannanase activity which may be useful for degradation or modification of plant or algae cell wall material. WO 93/24622 discloses a mannanase isolated from Trichoderma reseei useful for bleaching lignocellulosic pulps. An hemicellulase capable of degrading mannan-containing hemicellulose is described in W091/18974 and a purified mannanase from Bacillus amyloliquefaciens is described in W097/11164.
Preferably, the mannanase enzyme will be an alkaline mannanase as defined below, more preferably, a mannanase originating from a bacterial source. Especially, the laundry detergent composition of the present invention will comprise an alkaline marmanase selected from the mannanase from the strain Bacillus agaradhaerens NICMB 40482; the mannanase from Bacillus suhtilis strain 168, gene yght; the mannanase from Bacillus sp. 1633 and/or the mannanase from Bacillus sp. AA112. Most preferred mannanase for the inclusion in the detergent compositions of the present invention is the marmanase enzyme originating from Bacillus sp. 1633 as described in the co-pending Danish patent application No. PA 1998 01340.
The terms "alkaline marmanase enzyme" is meant to encompass an enzyme having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of its maximum activity at a given pH ranging from 7 to 12, preferably 7.5 to 10.5.
The alkaline mannanase from Bacillus agaradhaerens NICMB 40482 is described in the co-pending U.S. patent application serial No. 09/111,256. More specifically, this mannanase is:
i) a polypeptide produced by Bacillus agaradhaerens, NCIMB 40482; or ii) a polypeptide comprising an amino acid sequence as shown in positions 32-343 of SEQ ID NO:2 as shown in U.S. patent application serial No. 09/111,256; or iii) an analogue of the polypeptide defined in i) or ii) which is at least 70% homologous with said polypeptide, or is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal antibody raised against said polypeptide in purified for-in.
Also encompassed is the corresponding isolated polypeptide having marmanase activity selected from the group consisting of- (a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: I from nucleotide 97 to nucleotide 1029 as shown in U.S. patent application serial No. 09/111,256; (b) species homologs of (a); (c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 70% identical to the amino acid sequence of SEQ ID NO:
2 from amino acid residue 32 to amino acid residue 343 as shown in U.S. patent application serial No. 09/111,256; (d) molecules complementary to (a), (b) or (c); and (e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pSJ1678 comprising the polynucleotide molecule (the DNA sequence) encoding said mannanase has been transformed into a strain of the Escherichia coli which was deposited by the inventors according to theBudapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Saminlung 12 von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Gennany, on 18 May 1998 under the deposition number DSM 12180.
A second more preferred mannanase enzyme is the mannanase from the Bacillus subtilis strain 168, which is described in the co-pending U.S. patent application serial No. 09/095,163. More specifically, this marmanase is:
i) is encoded by the coding part of the DNA sequence shown in SED ID No. 5 shown in the U.S. patent application serial No. 09/095,163 or an analogue of said sequence; and/or ii) a polypeptide comprising an amino acid sequence as shown SEQ ID NO:6 shown in the U.S. patent application serial No. 09/095,163; or iii) an analogue of the polypeptide defined in ii) which is at least 70% homologous with said polypeptide, or is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal antibody raised against said polypeptide in purified form.
Also encompassed in the corresponding isolated polypeptide having mannanase activity selected from the group consisting of- (a) polynucleotide molecules encoding a polypeptide having marmanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO:5 as shown in the U.S. patent application serial No. 09/095,163 (b) species hornologs of (a); (c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 70% identical to the amino acid sequence of SEQ ID NO: 6 as shown in the U.S. patent application serial No. 09/095,163; (d) molecules complementary to (a), (b) or (c); and (e) degenerate nucleotide sequences of (a), (b), (c) or (d).
A third more preferred mannanase is described in the co-pending Danish patent application No. PA 1998 01340. More specifically, this mannanase is:
i) a polypeptide produced by Bacillus sp. 1633; ii) a polypeptide comprising an amino acid sequence as shown in positions 33-340 of SEQ ID NO:2 as shown in the Danish application No. PA 1998 01340; or iii) an analogue of the polypeptide defined in i) or ii) which is at least 65% homologous with said polypeptide, is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal antibody raised against said polypeptide in purified form.
Also encompassed is the corresponding isolated polynucleotide molecule selected from the group consisting of- (a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from nucleotide 317 to nucleotide 1243 the Danish application No. PA 1998 01340; (b) species homologs of (a); (c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 33 to amino acid residue 340 the Danish application No. PA 1998 01340; (d) molecules complementary to (a), (b) or (c); and (e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pBXM3 comprising the polynucleotide molecule (the DNA sequence) encoding a mannanase of the present invention has been transformed into a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zelikulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 29 May 1998 under the deposition number DSM 12197.
A fourth more preferred mannanase is described in the Danish co-pending patent application No. PA 1998 01341. More specifically, this mannanase is:
i) a polypeptide produced by Bacillus sp. AAl 12; ii) a polypeptide comprising an amino acid sequence as shown in positions 25-362 of SEQ ID NO:2as shown in the Danish application No. PA 1998 0134 1; or iii) an analogue of the polypeptide defined in i) or ii) which is at least 65% homologous with said polypeptide, is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal antibody raised against said polypeptide in purified form.
Also encompassed is the corresponding isolated polynucleotide molecule selected from the group consisting of (a) polymicleotide molecules encoding a polypeptide having marmanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: I from nucleotide 225 to nucleotide 1236 as shown in the Danish application No. PA 1998 01341; (b) species homologs of (a); 14 (c) polynucleotide molecules that encode a polypeptide having marmanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 25 to amino acid residue 362 as shown in the Danish application No. PA 1998 01341; (d) molecules complementary to (a), (b) or (c); and (e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pBXMI comprising the polynucleotide molecule (the DNA sequence) encoding a marmanase of the present invention has been transformed into a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Samnilung von Mikroorganismen und Zellkulturen GrnbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 7 October 1998 under the deposition number DSM 12433.
The marmanase, when present, is incorporated into the treating compositions of the present invention preferably at a level of from 0. 0001% to 2%, more preferably from 0.0005% to 0. 1 %, most preferred from 0.00 1 % to 0.02% pure enzyme by weight of the composition.
Xyloglucanases - Suitable xyloglucanases for the purpose of the present invention are enzymes exhibiting endoglucanase activity specific for xyloglucan, preferably at a level of from about 0.00 1 % to about I %, more preferably from about 0.0 1 % to about 0.5%, by weight of the composition. As used herein, the term "endoglucanase activity" means the capability of the enzyme to hydrolyze 1,4-fD-glycosidic linkages present in any cellulosic material, such as cellulose, cellulose derivatives, lichenin, f-D-glucan, or xyloglucan. The endoglucanase activity may be determined in accordance with methods known in the art, examples of which are described in WO 94/14953 and hereinafter. One unit of endoglucanase activity (e.g. CMCU, AVIU, XGU or BGU) is defined as the production of I gmol reducing sugar/min from a glucan substrate, the glucan substrate being, e.g., CMC (CMCU), acid swollen Avicell (AVIU), xyloglucan (XGU) or cereal f-glucan (BGU). The reducing sugars are determined as described in WO 94/14953 and hereinafter. The specific activity of an endoglucanase towards a substrate is defined as units/mg of protein.
Suitable are enzymes exhibiting as its highest activity XGU endoglucanase activity (hereinafter "specific for xyloglucan"), which enzyme:
i) is encoded by a DNA sequence comprising or included in at least one of the following partial sequences (a) ATTCATTTGT GGACAGTGGA C (SEQ ID No: 1) (b) GTTGATCGCA CATTGAACCA (SEQ ID NO: 2) (c) ACCCCAGCCG ACCGATTGTC (SEQ ID NO: 3) (d) CTWMACC TCACCATCAT (SEQ ID NO: 4) (c) TTAACAMT TWACCATGA (SEQ ID NO: 5) (f) AWMCCCT WMCCCTT (SEQ ID NO: 6) (g) GWACWTGG MCCWTGC CAGMCC (SEQ ID NO: 7) (h) GACAGTAWA ATCCAGCATT (SEQ ID NO: 8) (i) AWATCAGCC G=GTACA (SEQ ID NO: 9) 0) CCATGAAM CACCGTAM (SEQ ID NO: 10) (k) WACTGMC TCTCCCAGGT (SEQ ID NO: 11) (1) GTGGGCGGCC CCTCAGWAA (SEQ ID NO: 12) (m) ACWTCCTCC AATMCWT (SEQ ID NO: 13) (n) GGCTGGTAG TAATGAGM (SEQ ID NO: 14) (o) GGWCAGAW TTGWCAGGC (SEQ ID NO: 15) (p) CAMATCCW GGMTWTGG G (SEQ ID NO: 16) (q) AAAGATWAT TTGWGACAG TGGACGTTGA TWCACATTG AAWAMCCC AGWGAWGA TTGWMCC TTACCTCACC ATCAMAM ATCMTCAC CATGAAGM TWMCWT CWTTGWAC MGGMCC GCTGWAGCC TCCAGCGCCG CACAMCM CWTCAGTGG GATACCGWA WGCCWTGA CTWACCCW TACAACGACC MGGGWGA GACWWGGC ACCGGCTCW AGMCACTGG AGWGACTCC TACAWGGW ACACCATCW TTGWACACC AWAGGTCCT GGWGGAGTA GCAGCAGCGT CAAGAWTAT GCCAACG (SEQ ID NO: 17) or (r) CAWATCTCC ATTGAGTAAT CACGTTGGTG TTCWTGWC CGCCGTGTTG WTGWGGAG GCTGWWGA GACGGGTGGG GATGGTGGTG GGAGAGAAW TAGGGCGCW WMCAGTC CCTAGWAGG ATACCGGAAA ACWTGWGT AGGAGGMA TAGGMCCA GGAGACWM TATAGGGGAT AAATGAGATT GAATGWGGC CACACTCAAA CCAACCAGGT CCTWACATA CAAMCATAT ACCAATTATA CCTACCAAAA AAAAAAAAAA AAAAAAAAAA AAAA (SEQ ID NO: 18) 16 or a sequence homologous thereto encoding a polypeptide specific for xyloglucan with endoglucanase activity, ii) is immunologically reactive with an antibody raised against a highly purified endoglucanase encoded by the DNA sequence defined in i) and derived from Aspergillus aculeatus, CBS 101.43, and is specific for xyloglucan.
More specifically, as used herein the term "specific for xyloglucan" means that the endoglucanse enzyme exhibits its highest endoglucanase activity on a xyloglucan substrate, and preferably less than 75% activity, more preferably less than 50% activity, most preferably less than about 25% activity, on other cellulose-containing substrates such as carboxymethyl cellulose, cellulose, or other glucans.
Preferably, the specificity of an endoglucanase towards xyloglucan is further defined as a relative activity determined as the release of reducing sugars at optimal conditions obtained by incubation of the enzyme with xyloglucan and the other substrate to be tested, respectively. For instance, the specificity may be defined as the xyloglucan to 13- glucan activity (XGU/BGU), xyloglucan to carboxy methyl cellulose activity (XGU/CMCU), or xyloglucan to acid swollen Avicell activity (XGU/AVIU), which is preferably greater than about 50, such as 75, 90 or 100.
The term "derived from" as used herein refers not only to an endoglucanase produced by strain CBS 101.43, but also an endoglucanase encoded by a DNA sequence isolated from strain CBS 101.43 and produced in a host organism transformed with said DNA sequence. The term "homologue" as used herein indicates a polypeptide encoded by DNA which hybridizes to the same probe as the DNA coding for an endoglucanase enzyme specific for xyloglucan under certain specified conditions (such as presoaking in 5xSSC and prehybridizing for I h at -40'C in a solution of 5xSSC, 5xDenhardt's solution, and 50 gg of denatured sonicated calf thymus DNA, followed by hybridization in the same solution supplemented with 50 LCi 32-P-dCTP labelled probe for 18 h at -40'C and washing three times in 2xSSC, 0.2% SIDS at 40'C for 30 minutes). More specifically, the term is intended to refer to a DNA sequence which is at least 70% homologous to any of the sequences shown above encoding an endoglucanase specific for xyloglucan, including at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% with any of the sequences shown above. The term is intended to include modifications of any of the DNA sequences shown above, such as nucleotide substitutions which do not give rise to another amino acid sequence of the polypeptide encoded by the sequence, but which correspond to the codon usage of the host organism into which a DNA construct comprising any of the DNA sequences is introduced or nucleotide substitutions which do give rise to a different amino acid sequence and therefore, possibly, a different amino acid sequence and therefore, possibly, a different protein structure which might give rise to an endoglucanase mutant with different properties than the native enzyme. Other examples of possible modifications are insertion of 17 one or more nucleotides into the sequence, addition of one or more nucleotides at either end of the sequence, or deletion of one or more nucleotides at either end or within the sequence.
Endoglucanase specific for xyloglucan useful in the present invention preferably is one which has a XGU/BGU, XGU/CMU and/or XGU/AVIU ratio (as defined above) of more than 5 0, such as 75, 90 or 100.
Furthermore, the endoglucanase specific for xyloglucan is preferably substantially devoid of activity towards P-glucan and/or exhibits at the most 25% such as at the most 10% or about 5%, activity towards carboxymethyl cellulose and/or Avicell when the activity towards xyloglucan is 100%. In addition, endoglucanase specific for xyloglucan of the invention is preferably substantially devoid of transferase activity, an activity which has been observed for most endoglucanases specific for xyloglucan of plant origin.
Endoglucanase specific for xyloglucan may be obtained from the fungal species A. aculeatus, as described in WO 94/14953. Microbial endoglucanases specific for xyloglucan has also been described in WO 94/14953. Endoglucanases specific for xyloglucan from plants have been described, but these enzymes have transferase activity and therefore must be considered inferior to microbial endoglucanses specific for xyloglucan whenever extensive degradation of xyloglucan is desirable. An additional advantage of a microbial enzyme is that it, in general, may be produced in higher amounts in a microbial host, than enzymes of other origins.
The xyloglucanase, when present, is incorporated into the treating compositions of the invention preferably at a level of from 0.0001% to 2%, more preferably from 0.0005% to 0.1%, most preferred from 0.001% to 0. 02% pure enzyme by weight of the composition.
LiRases - Suitable lipase enzymes include, but are not limited to, those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034. Suitable lipases also include those which show a positive immunological crossreaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano," hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g. Chromohacter viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. Especially suitable lipases are lipases such as MI LIPASEO and LIPOMAX0 (Gist-Brocades) and LIPOLASEO and LIPOLASE ULTRA(D(Novo) which have found to be very effective when used in combination with the compositions of the present invention.
Cellulases - Cellulases usable in the present invention include both bacterial or fungal cellulase. Preferably, they will have a pH optimum of between 5 and 9.5. Suitable cellulases are 18 disclosed in U.S. Patent 4,435,307, Barbesgoard et al, which discloses fungal cellulase produced from Humicola insolens. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A2.095.275 and DE-OS-2.247.832.
Examples of such cellulases are cellulases produced by a strain of Humicola insolens (Humicola grisea var. thermoidea), particularly the Hurnicola strain DSM 1800.
Other suitable cellulases are cellulases originated from Hurnicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a -43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. WO 91/17243. Also suitable cellulases are the EGIII cellulases, from Trichoderma longibrachiaturn described in W094/21801, Genencor, published September 29, 1994. Especially suitable cellulases are the cellulases having color care benefits. Examples of such cellulases are cellulases described in European patent application No. 91202879.2, filed November 6, 1991 (Novo). CELLUZYME8 (Novo Nordisk A/S) is usefill in the present invention. W091/17243 describes other suitable cellulases.
Peroxidases - Peroxidase enzymes are known in the art, and include, for example, horseradish peroxidase, ligninase and haloperoxidase such as chloro- and bromo-peroxidase. Peroxidase-containing cleaning and/or detergent compositions are disclosed, for example, in U.S. Patent Nos. 5, 576,282, 5,728,671 and 5,707,950, PCT International Applications WO 89/099813, W089/09813 and in European Patent application EP No. 91202882. 6, filed on November 6, 1991 and EP No. 96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme.
Preferred enhancers are substituted phenthiazine and phenoxasine 10Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10phenoxazinepropionic acid (POP) and 10-methylphenoxazine (described in WO 94/12621) and substitued syringates (0-C5 substitued alkyl syringates) and phenols. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide.
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special kind of lipase, namely lipases which do not require interfacial activation. Examples of suitable cutinases are described in WO 88/09367 (Genencor).
A range of enzyme materials is also disclosed in WO 93/07263 and WO 93/07260 to Genencor International, WO 89/08694 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 are also disclosed in U.S. 4,261,868, Hora et al, April 14, 198 1.
19 The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / genetic engineering techniques in order to optimize their performance efficiency in the laundry detergent and/or fabric care compositions of the invention. For example, the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that the optimal pH, bleach or chelant stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular laundry application.
A range of enzyme materials are also disclosed in WO 9307263 and WO 9307260 to Genencor International, WO 8908694, and U.S. 3,553,139, January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S. 4, 101,457, and in U.S. 4,507,219. Enzyme materials particularly useful for liquid detergent formulations, and their incorporation into such formulations, are disclosed in U.S. 4,261,868.
Various carbohydrase enzymes which impart antimicrobial activity may also be -included in the present invention. Such enzymes include endoglycosidase, Type 11 endoglycosidase and glucosidase as disclosed in U.S. Patent Nos. 5,041,236, 5,395,541, 5,238,843 and 5,356,803 the disclosures of which are herein incorporated by reference. Of course, other enzymes having antimicrobial activity may be employed as well including peroxidases, oxidases and various other enzymes.
It is also possible to include an enzyme stabilization system into the compositions of the present invention when any enzyme is present in the composition.
The enzymes of the present invention are normally incorporated in cleaning and/or detergent compositions at levels from 0.0001% to 2% of active enzyme by weight of the compositions. The enzymes can be added as separate single ingredients (prills, granulates, stabilized liquids, etc. containing one enzyme) or as mixtures of two or more enzymes (e.g. cogranulates).
CLEANING AND/QR DETERGENT COMIPOSITIONS The cleaning and/or detergent compositions of the present invention also comprise, in addition to one or more activated (irradiated) enzymes of the present invention described herein before, one or more cleaning adjunct materials, preferably compatible with the enzyme(s). The term "cleaning adjunct materials", as used herein, means any liquid, solid or gaseous material selected for the particular type of cleaning and/or detergent composition desired and the form of the product (e.g., liquid; granule; powder; gel composition), which materials are also preferably compatible with the activated enzymes of the present invention. Granular compositions can also be in "compact" form and the liquid compositions can also be in a "concentrated" form.
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 and/or detergent conditions during use (e.g., through the wash detergent use). The term "compatible", as used herein, means the cleaning adjunct materials do not reduce the enzymatic activity of the activated enzymes to such an extent that the activated enzymes are not effective as desired during normal use situations. Examples of suitable cleaning adjunct materials include, but are not limited to, surfactants, builders, bleaches, bleach activators, bleach catalysts, non-activated enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, perservatives, anti-oxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tamish and/or anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments and pH control agents as described in U.S. Patent Nos. 5,705,464, 5,710,115, 5,698,504, 5,695,679, 5,686,014 and 5,646,101. Specific cleaning adjunct materials are exemplified in detail hereinafter.
If the cleaning adjunct materials are not compatible with the activated enzymes within the cleaning and/or detergent compositions, then suitable methods of keeping the cleaning adjunct materials and the activated enzymes separate (not in contact with each other) until combination of the two components is appropriate can be used. Suitable methods can be any method known in the art, such as gelcaps, encapulation, tablets, physical separation, etc.
Preferably an effective amount of one or more activated (irradiated) enzymes described above are included in compositions useful for laundering a variety of fabrics in need of cleaning.
As used herein, "effective amount of one or more activated (irradiated) enzymes" refers to the quantity of activated enzymes of the present invention described hereinbefore necessary to achieve the enzymatic activity necessary in the specific cleaning and/or detergent 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 activated enzyme used, the cleaning and/or detergent application, the specific composition of the cleaning and/or detergent composition, and whether a liquid or dry (e.g., granular, powder) composition is required, and the like.
The cleaning and/or detergent compositions of the present invention comprise:
(a) an activated (irradiated) enzyme in accordance with the present invention; and (b) one or more cleaning adjunct materials.
Preferably, the cleaning and/or detergent compositions comprise from about 0.0001%, preferably from about 0.001%, more preferably from about 0. 01% by weight of the cleaning 21 and/or detergent compositions of one or more activated (irradiated) enzymes of the present invention, to about 10%, preferably to about 2%, more preferably to about 1%, most preferably to about 0. 1% - Preferably, the cleaning and/or detergent compositions of the present invention comprise one or more activated (irradiated) enzymes of the present invention such that the activated (irradiated) enzymes are present in the cleaning and/or detergent compositions of the present invention at a level of from about 0.0001%, preferably from about 0.001%, more preferably from about 0.01% to about 10%, preferably to about 2%, more preferably to about 1%, most preferably to about 0.1% of pure enzyme by weight of the cleaning and/or detergent composition.
Several examples of various cleaning and/or detergent compositions wherein the activated (irradiated) enzymes of the present invention may be employed are discussed in further detail below. Also, the cleaning and/or detergent compositions may include from about 1% to about 99.9% by weight of the composition of the cleaning adjunct materials.
As used herein, "fabric cleaning and/or detergent compositions" include hand and machine cleaning and/or detergent compositions including cleaning and/or detergent additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics.
When the cleaning and/or detergent compositions of the present invention are formulated as compositions suitable for use in a cleaning and/or detergent machine washing method, the compositions of the present invention preferably contain both a surfactant and a builder compound and additionally one or more cleaning adjunct materials preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap dispersants, soil suspension and anti-redeposition agents and corrosion inhibitors. Cleaning and/or detergent compositions can also contain softening agents, as additional cleaning adjunct materials.
The compositions of the present invention can also be used as detergent additive products in solid or liquid form. Such additive products are intended to supplement or boost the performance of conventional detergent compositions and can be added at any stage of the cleaning and/or detergent process.
If needed the density of the cleaning and/or detergent compositions herein ranges from 400 to 1200 g/litre, preferably 500 to 950 g/litre of composition measured at 20C.
The "compact" form of the cleaning and/or detergent compositions herein is best reflected by density and, in terms of composition, by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 22 17-35% by weight of the total composition. In the compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, most preferably not exceeding 5% by weight of the composition. The inorganic filler salts, such as meant in the present compositions are selected from the alkali and alkaline-earth-metal salts of sulfates and chlorides. A preferred filler salt is sodium sulfate.
Liquid cleaning and/or detergent compositions according to the present invention can also be in a "concentrated form", in such case, the liquid cleaning and/or detergent compositions according the present invention will contain a lower amount of water, compared to conventional liquid detergents. Typically the water content of the concentrated liquid cleaning and/or detergent composition is preferably less than 40%, more preferably less than 30%, most preferably less than 20% by weight of the cleaning and/or detergent composition.
CLEANING ADJUNCT MATERIALS While not essential for the purposes of the present invention, several conventional cleaning adjunct materials illustrated hereinafter are suitable for use in the cleaning and/or detergent compositions containing the irradiated enzymes of the present invention, and may be desirably incorporated in preferred 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 ofthe cleaning and/or detergent 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. Unless otherwise indicated, the cleaning and/or detergent compositions of the invention may for example, be formulated as granular or powder-form allpurpose or "heavy-duty" washing agents, especially laundry detergent 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.
Surfactants - Preferably, the cleaning and/or detergent compositions according to the present invention comprise a surfactant or surfactant system wherein the surfactant can be selected from nonionic and/or anionic and/or cationic surfactants, and/or ampholytic and/or zwitterionic and/or semi-polar nonionic surfactants.
23 The surfactant is typically present at a level of from about 0.1%, preferably about 1%, more preferably about 5% by weight of the cleaning and/or detergent compositions to about 99.9%, preferably about 80%, more preferably about 35%, most preferably 30% about by weight of the cleaning and/or detergent compositions.
The surfactant can be nonionic, anionic, ampholytic, zwitterionic, or cationic. Mixtures of these surfactants can also be used. Preferred cleaning and/or detergent compositions comprise anionic surfactants or mixtures of anionic surfactants with other surfactants, especially nonionic surfactants.
The surfactant is preferably formulated to be compatible with enzyme components present in the composition. In liquid or gel compositions the surfactant is most preferably formulated such that it promotes, or at least does not degrade, the stability of any enzyme in these compositions.
Nonlimiting examples of suitable nonionic, anionic, cationic, ampbolytic, zwitterionic and semi-polar nonionic surfactants are disclosed in U.S. Patent Nos. 5,707,950 and 5,576,282. Additional examples of suitable surfactants can be found in McCutcheon's EMULSIFIERS AND DETERGENTS, North American Edition, 1997, McCutcheon Division, MC Publishing Company, in U.S. Patent Nos. 3,929,678 and 4,259,217; in the series "Surfactant Science", Marcel Dekker, Inc., New York and Basel; in "Handbook of Surfactants", M.R. Porter, Chapman and Hall, 2nd Ed., 1994; in "Surfactants in Consumer Products", Ed. J. Falbe, Springer-Verlag, 1987; and "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perry and Berch).
Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula:
R2 - C(O) - N(R) - Z, wherein RI is H, or RI is CI-4 bydrocarbyl, 2hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R2 is C5-31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof. Preferably, RI is methyl, R2 is a straight C 11- 15 alkyl or C 16-18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive arnination reaction.
Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants hereof are water soluble salts or acids of the formula RO(A)mSO3M wherein R is an unsubstituted CIO-C24 alkyl or hydroxyalkyl group having a CIO-C24 alkyl component, preferably a C12C20 alkyl or hydroxyalkyl, more preferably C12-C18 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, rn is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, and M is H or a cation which can be, for example, a metal cation 24 (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substitutedammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein.
When included therein, the cleaning and/or detergent compositions, especially laundry detergent compositions, of the present invention typically comprise from about 1%, more preferably about 3% by weight of such anionic surfactants to about 40%, more preferably about 20% by weight of such anionic surfactants.
Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition having the formula:
RIR2R3R4N+X- wherein R1 is C8-C16 alkyl, each of R2, R3 and R4 is independently CI-C4 alkyl, Cl-C4 hydroxy alkyl, benzyl, and -(C2H40)xH where x has a value from 2 to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl.
When included therein, the cleaning and/or detergent compositions of the present invention typically comprise from about 0.2%, more preferably about 1% by weight of such cationic surfactants to about 25%, more preferably about 8% by weight of such cationic surfactants.
When included therein, the cleaning and/or detergent compositions of the present invention typically comprise from about 0.2%, more preferably about 1% by weight of such ampholytic surfactants to about 15%, more preferably about 10% by weight of such ampholytic surfactants.
When included therein, the cleaning and/or detergent compositions of the present invention typically comprise from about 0.2%, more preferably about 1% by weight of such zwitterionic surfactants to about 15%, more preferably about 10% by weight of such zwitterionic surfactants.
When included therein, the cleaning and/or detergent compositions of the present invention typically comprise from about 0.2%, more preferably 1% by weight of such sernipolar nonionic surfactants to about 15%, more preferably about 10% by weight of such semipolar nonionic surfactants.
The cleaning and/or detergent compositions of the present invention can also comprise from about 0.001% to about 100% of one or more (preferably a mixture of two or more) midchain branched surfactants, preferably midchain branched alkyl alkoxy alcohols having the formula:
R R1 R I I I CH3CH2(CH2),,CH(CH2),CH((H2)yUtl(UH2),(EO/PO)mOH mid-chain branched alkyl sulfates having the formula:
1 R R' R 2 1 1 1 CH3CH2(CH2),CH(CH2),CH(CH2)y(jH((jH2)z0S03M and mid-chain branched alkyl alkoxy sulfates having the formula:
R R' R 1 1 1 CH3CH2(C;H2),LH(CH2)xCH(CH2)yCH(UH2)z(E0/P0)m0SO3M wherein the total number of carbon atoms in the branched primary alkyl moiety of these formulae (including the R, RI, and R2 branching, but not including the carbon atoms which comprise any EO/PO alkoxy moiety) is from 14 to 20, and wherein further for this surfactant mixture the average total number of carbon atoms in the branched primary alkyl moieties having the above formula is within the range of greater than 14.5 to about 17.5 (preferably from about 15 to about 17); R, RI, and R2 are each independently selected from hydrogen, Cl-C3 alkyl, and mixtures thereof, preferably methyl; provided R, Rl, and R2 are not all hydrogen and, when z is 1, at least R or RI is not hydrogen. M is a water soluble cation and may comprises more than one type of cation, for example, a mixture of sodium and potassium. The index w is an integer from 0 to 13; x is an integer from 0 to 13; y is an integer from 0 to 13; z is an integer of at least 1; provided w + x + y + z is from 8 to 14. EO and PO represent ethyleneoxy units and propyleneoxy units having the formula:
CH3 CH3 1 1 -CHCH20- or -UH2CHOrespectively, however, other alkoxy units inter alia 1, 3-propyleneoxy, butoxy, and mixtures thereof are suitable as alkoxy units appended to the mid-chain branched alkyl moieties.
The mid-chain branched surfactants are preferably mixtures which comprise a surfactant system. Therefore, when the surfactant system comprises an alkoxylated surfactant, the index m indicates the average degree of alkoxylation within the mixture of surfactants. As such, the index m is at least about 0.01, preferably within the range of from about 0.1, more preferably from about 0.5, most preferably from about 1 to about 30, preferably to about 10, more preferably to about 5. When considering a mid-chain branched surfactant system which comprises only alkoxylated surfactants, the value of the index m represents a distribution of the average degree of alkoxylation corresponding to m, or it may be a single specific chain with alkoxylation (e.g., ethoxylation andlor propoxylation) of exactly the number of units corresponding to m.
The preferred mid-chain branched surfactants of the present invention which are suitable for use in the surfactant systems of the present invention have the formula:
CH3 1 CH3(CH2),,CH(CH2)bCH2(E0/P0)m0SO3M or the formula:
26 CH3 CH3 I I CH3(CH2)dCH(CH2)eCHCH2(EO/PO).OS03M wherein a, b, d, and e are integers such that a + b is from 10 to 16 and d + e is from 8 to 14; M is selected from sodium, potassium, magnesium, ammonium and substituted ammonium, and mixtures thereof The surfactant systems of the present invention which comprise mid-chain branched surfactants are preferably formulated in two embodiments. A first preferred embodiment comprises mid-chain branched surfactants which are formed from a feedstock which comprises 25% or less of mid-chain branched alkyl units. Therefore, prior to admixture with any other conventional surfactants, the mid-chain branched surfactant component will comprise 25% or less of surfactant molecules which are non-linear surfactants.
A second preferred embodiment comprises mid-chain branched surfactants which are formed from a feedstock which comprises from about 25% to about 70% of mid-chain branched alkyl units. Therefore, prior to admixture with any other conventional surfactants, the mid-chain branched surfactant component will comprise from about 25% to about 70% surfactant molecules which are non-linear surfactants.
The surfactant systems of the cleaning and/or detergent compositions of the present invention can also comprise from about 0.001%, preferably from about 1%, more preferably from about 5%, most preferably from about 10% to about 100%, preferably to about 60%, more preferably to about 30% by weight, of the surfactant system, of one or more (preferably a mixture of two or more) mid-chain branched alkyl arylsulfonate surfactants, preferably surfactants wherein the aryl unit is a benzene ring having the formula:
RVI, R3 I P [Mqj b S03 - - a wherein L is an acyclic hydrocarbyl moiety comprising from 6 to 18 carbon atoms; R', W, and R' are each independently hydrogen orC1_C3 alkyl, provided R' and R' are not attached at the terminus of the L unit; M is a water soluble cation having charge q wherein a and b are taken together to satisfy charge neutrality.
Bleaching System - In addition to the organic catalyst of the present invention, the bleaching compositions of the present invention preferably comprise a bleaching system. Bleaching systems typically comprise a peroxygen source. Peroxygen sources are well-known in the art and the peroxygen source employed in the present invention may comprise any of these well known sources, including peroxygen compounds as well as compounds which under 27 consumer use conditions provide an effective amount of peroxygen in situ. The peroxygen source may include a hydrogen peroxide source, the in situ formation of a peracid anion through the reaction of a hydrogen peroxide source and a bleach activator, preformed peracid compounds or mixtures of suitable peroxygen sources. Of course, one of ordinary skill in the art will recognize that other sources of peroxygen may be employed without departing from the scope of the invention. Preferably, the peroxygen source is selected from the group consisting of- (i) preformed peracid compounds selected from the group consisting of percarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, and mixtures thereof, and (ii) hydrogen peroxide sources selected from the group consisting of perborate compounds, percarbonate compounds, perphosphate compounds and mixtures thereof, and a bleach activator.
When present, peroxygen sources (peracids and/or hydrogen peroxide sources) will typically be at levels of from about 1%, preferably from about 5% to about 30%, preferably to about 20% by weight of the composition. If present, the amount of bleach activator will typically be from about 0.1%, preferably from about 0.5% to about 60%, preferably to about 40% by weight, of the bleaching composition comprising the bleaching agent-plus-bleach activator.
a. Preformed Peracids - The preformed peracid compound as used herein is any convenient compound which is stable and which under consumer use conditions provides an effective amount of peracid anion. The bleach boosters of the present invention may of course be used in conjunction with a preformed peracid compound selected from the group consisting of percarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, and mixtures thereof, examples of which are described in U.S. Patent No. 5,576,282 to Miracle et al.
One class of suitable organic peroxycarboxylic acids have the general formula: 0 11 ' i -.R-U-0-0H wherein R is an alkylene or substituted alkylene group containing from I to about 22 carbon atoms or a phenylene or substituted phenylene group, and Y is hydrogen, halogen, alkyl, aryl, C(O)OH or -C(O)OOH.
Organic peroxyacids suitable for use in the present invention can contain either one or two peroxy groups and can be either aliphatic or aromatic. When the organic peroxycarboxylic acid is aliphatic, the unsubstituted peracid has the general formula:
28 0 11 Y-(CH2)n-U-U-U-t-I where Y can be, for example, H, CH3, CH2CI, C(O)OH, or C(O)OOH; and n is an integer from 0 to 20. When the organic peroxycarboxylic acid is aromatic, the unsubstituted peracid has the general formula:
0 11 Y-C61714-k--U-UH wherein Y can be, for example, hydrogen, alkyl, alkylhalogen, halogen, C(O)OH or C(O)OOH.
Typical monoperoxy acids useful herein include alkyl and aryl peroxyacids such as:
0) peroxybenzoic acid and ring-substituted peroxybenzoic acid, e.g. peroxy-anaphthoic acid, monoperoxyphthalic acid (magnesium salt hexahydrate), and ocarboxybenzamidoperoxyhexanoic acid (sodium salt); (ii) aliphatic, substituted aliphatic and arylalkyl monoperoxy acids, e.g. peroxylauric acid, peroxystearic acid, N-nonanoylaminoperoxycaproic acid (NAPCA), N,N-(3-octylsuccinoyl)aminoperoxycaproic acid (SAPA) and N, Nphthaloylarninoperoxycaproic acid (PAP); (iii) amidoperoxyacids, e.g. monononylamide of either peroxysuccinic acid (NAPSA) or of peroxyadipic acid (NAPAA).
Typical diperoxyacids useful herein include alkyl diperoxyacids and aryldiperoxyacids, such as:
(iv) 1,12-diperoxydodecanedioic acid; (v) 1,9-diperoxyazelaic acid; (vi) diperoxybrassylic acid; diperoxysebacic acid and diperoxyisophthalic acid; (vii) 2-decyldiperoxybutane-1,4-dioic acid; (viii) 4,4-sulfonylbisperoxybenzoic acid.
Such bleaching agents are disclosed in U.S. Patent 4,483,781, Hartman, issued November 20, 1984, U.S. Patent 4,634,551 to Bums et al., European Patent Application 0,133,354, Banks et al. published February 20, 1985, and U.S. Patent 4,412,934, Chung et al. issued November 1, 1983. Sources also include 6-nonylamino-6-oxoperoxycaproic acid as fully described in U. S. Patent 4,634,55 1, issued January 6, 1987 to Bums et al. Persulfate compounds such as for example OXONE, manufactured commercially by E.I. DuPont de Nemours of Wilmington, DE can also be employed as a suitable source of peroxymonosulfuric acid.
b. Hydrogen Peroxide Sources - The hydrogen peroxide source may be any suitable hydrogen peroxide source and present at such levels as fully described in U.S. Patent No.
5,576,282.For example, the hydrogen peroxide source may be selected from the group 29 consisting of perborate compounds, percarbonate compounds, perphosphate compounds and mixtures thereof Hydrogen peroxide sources are described in detail in the herein incorporated 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.
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.
Compositions of the present invention 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"). However, chlorine-type bleaches are less preferred for compositions which comprise enzymes.
b. Bleach Activators - Preferably, the peroxygen source in the composition is formulated with an activator (peracid precursor). The activator is present at levels of from about 0.01%, preferably from about 0.5%, more preferably from about 1% to about 15%, preferably to about 10%, more preferably to about 8%, by weight of the composition. A bleach activator as used herein is any compound which when used in conjunction with a hydrogen peroxide source leads to the in situ production of the peracid corresponding to the bleach activator. Various non limiting examples of activators are fully disclosed in U.S. Patent No. 5,576,282, U.S. Patent 4,915,854 and U.S. Patent 4,412,934. See also U.S. 4,634,551 for other typical bleaches and activators useful herein.
Preferred activators are selected from the group consisting of tetraacetyl ethylene diamine (TAED), benzoyleaprolactam (BzCL), 4nitrobenzoylcaprolactam, 3-chlorobenzoylcaprolactarn, benzoyloxybenzenesulphonate (BOBS), nonanoyloxybenzenesulphonate (NOBS), phenyl benzoate (PhBz), decanoyloxybenzenesulphonate (CIO-OBS), benzoylvalerolactam (BZVL), octanoyloxybenzenesulphonate (C8-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 hydrophobic bleach activators include, but are not limited to, nonanoyloxybenzenesulphonate (NOBS), 4-[N-(nonaoyl) amino hexanoyloxy]benzene sulfonate sodium salt (NACA-OBS) an example of which is described in U.S. Patent No. 5,523,434, lauroyloxybenzenesulphonate (LOBS or C12OBS), 10undecenoyloxybenzenesulfonate (UDOBS or Cl I-OBS with unsaturation. in the 10 position), and decanoyloxybenzoic acid (DOBA).
Preferred bleach activators are those described in U.S. 5,698,504 Christie et al., issued December 16, 1997; U.S. 5,695,679 Christie et al. issued December 9, 1997; U.S. 5,686,401 Willey et al., issued November 11, 1997; U.S. 5,686,014 Hartshorn et al., issued November 11, 1997; U.S. 5, 405,412 Willey et al., issued April 11, 1995; U.S. 5,405,413 Willey et al. , issued April 11, 1995; U.S. 5,130,045 Mitchel et al., issued July 14, 1992; and U.S. 4,412,934 Chung et al., issued November 1, 1983, and copending patent applications U. S. Serial Nos. 08/709,072, 08/064,564, all of which are incorporated 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, more preferably from about 10: 1 to about 1: 1, preferably to about 3: 1.
Quaternary substituted bleach activators may also be included. The present bleaching 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 U.S. 5,686,015 Willey et al., issued November 11, 1997; U.S. 5,654,421 Taylor et al., issued August 5, 1997; U.S. 5,460,747 Gosselink et al., issued October 24, 1995; U.S. 5,584,888 Miracle et al., issued December 17, 1996; and U.S. 5,578,136 Taylor et al., issued November 26, 1996; all of which are incorporated herein by reference.
Highly preferred bleach activators useful herein are amide-substituted as described in U.S. 5,698,504, U.S. 5,695,679, and U.S. 5,686,014 each of which are cited herein above. Preferred examples of such bleach activators include: (6-octanamidocaproyl) oxybenzenesulfonate, (6nonanamidocaproyl)oxybenzenesulfonate, (6-decanamido caproyl)oxybenzenesulfonate and mixtures thereof.
Other useful activators, disclosed in U.S. 5,698,504, U.S. 5,695,679, U.S. 5,686,014 each of which is cited herein above and U.S. 4,966,723Hodge et al., issued October 30, 1990, include 31 benzoxazin-type activators, such as a C,H, ring to which is fused in the 1,2-positions a moiety -C(O)OC(Rl)=N-.
Depending on the activator and precise application, good bleaching results can be obtained from bleaching systems having with in-use pH of from about 6 to about 13, preferably from about 9.0 to about 10.5. Typically, for example, activators with electron-withdrawing moieties are used for near-neutral or sub-neutral pH ranges. Alkalis and buffering agents can be used to secure such pH.
Acyl lactain activators, as described in U.S. 5,698,504, U.S. 5,695,679 and U.S. 5,686,014, each of which is cited herein above, are very useful herein, especially the acyl caprolactams (see for example WO 94-28102 A) and acyl valerolactams (see U.S. 5,503,639 Willey et al., issued April 2, 1996 incorporated herein by reference).
d. Organic Peroxides, especially Diacyl Peroxides - In addition to the bleaching agents described above, the bleaching compositions of the present invention can optionally include organic peroxides. Organic peroxidse 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 incorporated herein by reference. If a diacyl peroxide is used, it will preferably be one which exerts minimal adverse impact on spotting/filming.
e. Metal-containing Bleach Catalysts - The bleaching compositions can also optionally include metal-containing bleach catalysts, preferrably 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 watersoluble salts thereof. Such catalysts are disclosed in U.S. 4,430,243 Bragg, issued February 2, 1982.
i. Manganese Metal Complexes - 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 manganesebased catalysts disclosed in U.S. 5,576,282 Miracle et al., issued November 19, 1996; U.S. 5,246,621 Favre et al., issued September 21, 1993; U.S. 5,244,594 Favre et al., issued September 14, 1993; U.S. 5,194,416 Jureller et al., issued March 16, 1993; U.S. 5,114,606 van Vliet et al., issued May 19, 1992; and European Pat. App. Pub. Nos. 549,271 Al, 549,272 Al, 544,440 A2, and 544,490 Al; Preferred examples of these catalysts include MnlV2(u-0)3(1,4,7-trimethyl-1,4,7-triazacyclononane)2- 32 (PF6)2, MnII12(u-O)I(u-OAc)2(1,4,7-trimethyl-1,4,7- triazacyclononane)2(CIO4)2, MnlV4(u0)6(1,4,7-triazacyclononane)4(CI04)4, MnllIMnIV4(u-0) I (u-OAc)2-(1,4,7-trimethyl- 1,4, 7triazacyclononane)2(CI04)3, MnIV(1,4,7-trimethyl-1,4,7- triazacyclononane)- (OCH3)3(PF6), and mixtures thereof Other metal-based bleach catalysts include those disclosed in U.S. 4,430,243 included by reference herein above and U.S. 5,114,611 van Kralingen, issued May 19, 1992. The use of manganese with various complex ligands to enhance bleaching is also reported in the following: U.S. 4,728,455 Rerek, issued March 1, 1988; U.S. 5,284,944 Madison, issued Februaary 8, 1994; U.S. 5, 246,612 van Dijk et al., issued September 21, 1993; U.S. 5,256,779 Kerschner et al., issued October 26, 2993; U.S. 5,280,117 Kerschner et al. , issued January 18, 1994; U.S. 5,274,147 Kerschner et al., issued December 28, 1993; U.S. 5,153,161 Kerschner et al., issued October 6, 1992; and U.S. 5,227,084 Martens et al., issued July 13, 1993.
ii. Cobalt Metal Complexes - Cobalt bleach catalysts useful herein are known, and are described, for example, in U.S. 5,597,936 Perkins et al., issued January 28, 1997; U.S. 5,595,967 Miracle et al., January 21, 1997; U.S. 5,703,030 Perkins et al., issued December 30, 1997; and M. L. Tobe, "Base Hydrolysis of Transition-Metal Complexes", Ady. Inorg. Bioinorg. Mech. (1983), 2, pages 1-94. The most preferred cobalt catalyst useful herein are cobalt pentaamine acetate salts having the formula [Co(NH3)5OAc] Ty, wherein "OAc" represents an acetate moiety and "Ty" is an anion, and especially cobalt pentaamine acetate chloride, [Co(NH3)5OAc]CI2; as well as [Co(NH3)5OAc](OAc)2; [Co(NH3)5OAc](PF6)2; [Co(NH3)5OAc](SO4); [Co(NH3)5OAc](BF4)2; and [Co(NH3)5OAc](NO3)2 (herein "PAC").
These cobalt catalysts are readily prepared by known procedures, such as taught for example in U.S. 5,597,936, U.S. 5,595,967, U.S. 5,703,030, cited herein above, the Tobe article and the references cited therein, and 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 Chemi Utry, 56,22-25 (1952).
iii. Transition Metal Complexes of Macropolycyclic Rigid Ligands Compositions herein may also suitably include as bleach catalyst a transition metal complex of a macropolycyclic rigid ligand. The phrase "macropolycyclic rigid ligand" is sometimes abbreviated as "MRL" in discussion below. The amount used is a catalytically effective amount, suitably about I ppb or more, for example up to about 99.9%, more typically about 0.001 ppm or more, preferably from about 0.05 ppm. to about 500 ppm (wherein "ppb" denotes parts per billion by weight and "ppm" denotes parts per million by weight). Suitable transition metals e.g., Mn are illustrated hereinafter.
"Macropolycyclic" means a MRL is both a macrocycle and is polycyclic. "Polycyclic" means at least bicyclic. The term 33 "rigid" as used herein herein includes "having a superstructure" and "cross-bridged". "Rigid" has been defined as the constrained converse of flexibility: see D.H. Busch., Chemical Reviews., (1993), 93, 847-860, incorporated by reference. More particularly, "rigid" as used herein means that the MRL must be determinably more rigid than a macrocycle ("parent macrocycle") which is otherwise identical (having the same ring size and type and number of atoms in the main ring) but lacking a superstructure (especially linking moieties or, preferably cross-bridging moieties) found in the MRL's. In determining the comparative rigidity of macrocycles with and without superstructures, the practitioner will use the free form (not the metal-bound form) of the macrocycles. Rigidity is well-known to be useful in comparing macrocycles; suitable tools for determining, measuring or comparing rigidity include computational methods (see, for example, Zimmer, Chemical Reviews, (1995), 95(38), 2629- 2648 or Hancock et al., Inorganica Chimica Acta, (1989), 164, 73- 84.
Preferred MRL's herein are a special type of ultra-rigid ligand which is cross-bridged. A "cross-bridge" is nonlimitingly illustrated in 1. 11 hereinbelow. In 1. 11, the cross-bridge is a CH2CH2- moiety. It bridges N I and N 8 in the illustrative structure. By comparison, a "sameside" bridge, for example if one were to be introduced across N I and N 12 in 1. 11, would not be sufficient to constitute a "cross-bridge" and accordingly would not be preferred.
Suitable metals in the rigid ligand complexes include Mn(II), Mn(III), Mn(IV), Mn(V), Fe(II), Fe(III), Fe(IV), Co(I), Co(II), Co(III), Ni(I), Ni(II), Ni(III), Cu(I), Cu(II), Cu(III), Cr(II), Cr(III), Cr(IV), Cr(V), Cr(VI), V(III), V(IV), V(V), Mo(IV), Mo(V), Mo(VI), W(IV), W(V), W(VI), Pd(II), Ru(II), Ru(III), and Ru(IV). Preferred transition-metals in the instant transitionmetal bleach catalyst include manganese, iron and chromium.
More generally, the MRL's (and the corresponding transition-metal catalysts) herein suitably comprise:
(a) at least one macrocycle main ring comprising four or more heteroatoms; and (b) a covalently connected non-metal superstructure capable of increasing the rigidity of the macrocycle, preferably selected from (i) a bridging superstructure, such as a linking moiety; (ii) a cross-bridging superstructure, such as a cross-bridging linking moiety; and (iii) combinations thereof.
The term "superstructure" is used herein as defined in the literature by Busch et al., see, for example, articles by Busch in "Chemical Reviewe'.
Preferred superstructures herein not only enhance the rigidity of the parent macrocycle, but also favor folding of the macrocycle so that it coordinates to a metal in a cleft. Suitable superstructures can be remarkably simple, for example a linking moiety such as any of those illustrated in Fig. I and Fig. 2 below, can be used.
34 (CH2)n Fig. I wherein n is an integer, for example from 2 to 8, preferably less than 6, typically 2 to 4, or T (CH2)M- (CH2)n 11 z Fig. 2 wherein m and n are integers from about I to 8, more preferably from I to 3; Z is N or CH; and T is a compatible substituent, for example H, alkyl, trialkylammonium, halogen, nitro, sulfonate, or the like. The aromatic ring in LI 0 can be replaced by a saturated ring, in which the atom in Z connecting into the ring can contain N, 0, S or C.
Suitable MRL's are further nonlimitingly illustrated by the following compound:
3 2rj,' 1 14( N a N 6 b 13 121)7 1-1' I 1 9 10 Fig. 3 This is a MRL in accordance with the invention which is a highly preferred, crossbridged, methyl-substituted (all nitrogen atoms tertiary) derivative of cyclam. Formally, this ligand is named 5,12-dimethyl-1,5,8, 12-tetraazabicyclo[6.6.2]hexadecane using the extended von Baeyer system. See "A Guide to IUPAC Nomenclature of Organic Compounds: Recommendations 1993", R. Panico, W.H. Powell and J-C Richer (Eds.), Blackwell Scientific Publications, Boston, 1993; see especially section R-2.4.2. 1.
Transition-metal bleach catalysts of Macrocyclic Rigid Ligands which are suitable for use in the invention compositions can in general include known compounds where they conform with the definition herein, as well as, more preferably, any of a large number of novel compounds expressly designed for the present laundry or cleaning uses, and non-limitingly illustrated by any of the following:
Dichloro-5,12-dimethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(II) Diaquo-5,12-dimethyl-1,5,8,12-tetraazabicyclo[6.6. 2]hexadecane Manganese(II) Hexafluorophosphate Aquo-hydroxy-5,12-dimethyl-1,5,8,12-tetraazabicyclo[6. 6.2]hexadecane Manganese(III) Hexafluorophosphate Diaquo-5,12-dimethyl-1, 5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(I1) Tetrafluoroborate Dichloro-5,12-dimethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(III) Hexafluorophosphate Dichloro-5,12-di-n-butyl-1,5,8,12tetraaza bicyclo[6.6.2]hexadecane Manganese(I1) Dichloro-5,12-dibenzyl-1, 5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(I1) Dichloro-5-n-butyl12-methyl-1,5,8,12-tetraaza- bicyclo[6.6.2]hexadecane Manganese(I1) Dichloro-5-n-octy]- 12-methyl- 1,5,8,12-tetraaza- bicyclo[6.6. 2]hexadecane Manganese(II) Dichloro-5-n-butyl- 12-methy]- 1, 5,8,12tetraaza- bicyclo[6.6.2]hexadecane Manganese(II).
As a practical matter, and not by way of limitation, the 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 ppin to about 25 ppm, more preferably from about 0.05 ppm to about 10 ppin, and most preferably from about 0.1 ppm to about 5 ppin, of the bleach catalyst species in the wash liquor. In order to obtain such levels in the wash liquor of an automatic washing process, typical 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, especially manganese or cobalt catalysts, by weight of the cleaning compositions.
Preferably, the peroxygen source is selected from hydrogen peroxide sources selected from the group consisting of perborate compounds, percarbonate compounds, perphosphate compounds and mixtures thereof, and a bleach activator.
Preferably, the bleach activator is selected from the group consisting of hydrophobic bleach activators as disclosed herein.
The purpose of such a bleaching composition is to mitigate unwanted decomposition of the organic catalyst, and to allow the peracid to achieve bleaching performance on a fabric in need of cleaning, such as a stained fabric, in a wash solution prior to the availability of the organic catalyst.
ADDITIONAL DETERGENT COMPONENTS The following are non-limiting examples of additional detergent components (adjunct ingredients) useful in the cleaning and/or detergent compositions, especially laundry detergent compositions, of the present invention, said adjunct ingredients include builders, optical brighteners, soil release polymers, dye transfer agents, dispersants, enzymes, suds suppressers, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric 36 conditioners, hydrolyzable surfactants, preservatives, anti-oxidants, chelants, stabilizers, antishrinkage agents, anti-wrinkle agents, germicides, fungicides, anti corrosion agents, and mixtures thereof Builders - The cleaning and/or detergent compositions of the present invention preferably comprise one or more detergent builders or builder systems. When present, the compositions will typically comprise at least about 1% builder, preferably from about 5%, more preferably from about 10% to about 80%, preferably to about 50%, more preferably to about 30% by weight, of detergent builder.
The level of 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. Formulations typically comprise from about 5% to about 50%, more typically about 5% to about 30%, by weight, of detergent builder. Granular formulations typically comprise from about 10% to about 80%, more typically from about 15% to about 50% by weight, of the detergent builder. Lower or higher levels of builder, however, are not meant to be excluded.
Inorganic or P-containing detergent builders 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 alum inosilicates. However, non-phosphate builders are required in some locales. Importantly, the compositions herein function surprisingly well 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 Si02:Na2O ratio in the range 1.6:1 to 3.2:1 and layered silicates, such as the layered sodium silicates described in U.S. 4,664,839 Rieck, issued May 12, 1987. NaSKS-6 is the trademark for a crystalline layered silicate marketed by Hoechst (commonly abbreviated herein as "SKS6"). Unlike zeolite builders, the Na SKS-6 silicate builder does not contain aluminum. NaSKS6 has the delta- Na2SiO5 morphology 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 NaMSix02x+l- yH20 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-1 1, as the alpha, beta and gamma forms. As noted above, the delta-Na2SiO5 (NaSKS-6 form) is most preferred for use herein. Other silicates may also be useful such as for example magnesium 37 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 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 are useful in the present invention. Aluminosilicate builders are of great importance in most currently marketed heavy duty granular detergent compositions, and can also be a significant builder ingredient in liquid detergent formulations. Aluminosilicate builders include those having the empirical formula:
[Mz(zAI02)yj-xH20 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 alum inosi licates can be crystalline or amorphous in structure and can be natural ly-occurring alum inosilicates or synthetically derived. A method for producing aluminosilicate ion exchange materials is disclosed in U.S. 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 alurninosilicate ion exchange material has the formula:
Nal2[(AI02)12(SiO2)121-xH20 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 purposes 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 U.S. 3,128,287 Berg, issued April 7, 1964, U.S. 3,635,830 Lamberti et al., issued January 18, 1972, and U.S. 3,936,448 Lamberti, issued February 3, 1976. See also "TMS/TDS" builders of U.S. 4,663,071 Bush et al., issued May 5, 1987. Suitable ether polycarboxylates also include cyclic compounds, particularly alicyclic compounds, such as those described in U.S. 3,923,679 Rapko, issued December 2, 1975; U.S.
38 4,158,635 Crutchfield et al., issued June 19, 1979; U.S. 4,120,874 Crutchfield et al., issued October 17, 1978; and U.S. 4,102,903 Crutchfield et al., issued July 25, 1978.
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 for heavy duty liquid detergent formulations due to their availability from renewable resources and their biodegradability. Citrates can also be used in granular compositions, especially in combination with zeolite and/or layered silicate builders. Oxydisuccinates are also especially useful in such compositions and combinations.
Also suitable in the cleaning and/or detergent compositions of the present invention are the 3,3-dicarboxy-4-oxa-1,6-hexanedioates and the related compounds disclosed in U.S. 4,566,984, Bush, issued January 28, 1986. Useful succinic acid builders include the C5-C20 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, palm itylsuccinate, 2-dodecenylsuccinate (preferred), 2pentadecenylsuccinate, 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. 4,144,226, Crutchfield et al., issued March 13, 1979 and in U.S. 3,308,067, Diehl, issued March 7, 1967. See also Diehl U.S. Patent 3,723,322.
Fatty acids, e.g., C12-CI8 monocarboxylic acids, can also be incorporated 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.
In situations where phosphorus-based builders can be used, and especially in the formulation of bars used for hand-laundering operations, the various alkali metal phosphates such as the well-known sodium tripolyphosphates, sodium pyrophosphate and sodium orthophosphate can be used. Phosphonate builders such as ethane- I -hydroxy- 1, 1 diphosphonate and other known phosphonates (see, for example, U.S. Patents 3,159,581; 3,213,030; 3,422,021; 3,400,148 and 3,422,137) can also be used.
39 Chelating Agents - The cleaning and/or detergent compositions herein may also optionally contain one or more iron and/or manganese chelating agents. Such chelating agents can be selected from the group consisting of amino carboxylates, amino phosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures therein, all as hereinafter defined. Without intending to be bound by theory, it is believed that the benefit of these materials is due in part to their exceptional ability to remove iron and manganese ions from washing solutions by formation of soluble chelates.
Examples of suitable chelating agents and levels of use are described in U.S. Pat. Nos. 5,576,282 and 5,728,671.
A preferred biodegradable chelator for use herein is ethylenediamine disuccinate ("EDDS"), especially the [S,S] isomer as described in U.S. Patent 4,704,233, November 3, 1987, to Hartman and Perkins.
The compositions herein may also contain water-soluble methyl glycine diacetic acid (MGDA) salts (or acid form) as a chelant or co-builder useful with, for example, insoluble builders such as zeolites, layered silicates and the like.
If utilized, these chelating agents will generally comprise from about 0. 1% by weight of the cleaning and/or detergent compositions herein to about 15%, more preferably 3.0% by weight of the cleaning and/or detergent compositions herein.
Dye Transfer Inhibiting Agents - The cleaning and/or detergent compositions of the present invention may also include one or more compounds, dye transfer inhibiting agents, for inhibiting dye transfer from one fabric to another of solubilized and suspended dyes encountered during fabric laundering and conditioning operations involving colored fabrics.
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. Examples of such dye transfer inhibiting agents are disclosed in U.S. Pat. Nos. 5,707,950 and 5,707,951.
Additional suitable dye transfer inhibiting agents include, but are not limited to, crosslinked polymers. Cross-linked polymers are polymers whose backbone are interconnected to a certain degree; these links can be of chemical or physical nature, possibly with active groups on the backbone or on branches. Cross-linked polymers have been described in the Journal of Polymer Science, volume 22, pages 1035-1039.
In one embodiment, the cross-linked polymers are made in such a way that they form a three-dimensional rigid structure, which can entrap dyes in the pores formed by the threedimensional structure.
In another embodiment, the cross-linked polymers entrap dyes by swelling.
Suitable cross-linked polymers are described in the co-pending European patent application 94870213.9.
* Addition of such polymers also enhances the performance of the enzymes within the cleaning and/or detergent compositions herein.
The dye transfer inhibiting agents have the ability to complex or adsorb fugitive dyes wash out of dyed fabrics before the dyes have the opportunity to become attached to other articles in the wash.
When present in the cleaning and/or detergent compositions herein, the dye transfer inhibiting agents are present at levels from about 0.0001%, more preferably about 0.01%, most preferably about 0.05% by weight of the cleaning and/or detergent compositions to about 10%, more preferably about 2%, most preferably about 1% by weight of the cleaning and/or detergent compositions.
Dispersants - The cleaning and/or detergent compositions of the present invention can also contain dispersants. Suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts are polyaerylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 1,000 to 100, 000.
Especially, copolymer of acrylate and methylacrylate such as the 48ON having a molecular weight of 4000, at a level from 0.5-20% by weight of composition can be added in the detergent compositions of the present invention.
The compositions of the invention may contain a lime soap peptiser compound, which has a lime soap dispersing power (LSDP), as defined hereinafter of no more than 8, preferably no more than 7, most preferably no more than 6. The lime soap peptiser compound is preferably present at a level from 0% to 20% by weight.
A numerical measure of the effectiveness of a lime soap peptiser is given by the lime soap dispersant power (LSDP) which is determined using the lime soap dispersant test as described in an article by H.C. Borghetty and C.A. Bergman, J. Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime soap dispersion test method is widely used by practitioners in this art field being referred to, for example, in the following review articles; W.N. Linfield, Surfactant science Series, Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume 27, pages 159-163, (1990); and M.K. Nagarajan, W1. Masler, Cosmetics and Toiletries, volume 104, pages 71-73, (1989). The LSDP is the % weight ratio of dispersing agent to sodium oleate required to disperse the lime soap deposits formed by 0.025g of sodium oleate in 30rnI of water of 333ppm CaC03 (Ca:Mg--3:2) equivalent hardness.
41 Surfactants having good lime soap peptiser capability will include certain amine oxides, betaines, sulf6betaines, alkyl ethoxysulfates and ethoxylated alcohols.
Exemplary surfactants having a LSDP of no more than 8 for use in accord with the present invention include C16-Cl 8 dimethyl amine oxide, C12-Cl 8 alkyl ethoxysulfates with an average degree of ethoxylation of from 1-5, particularly C I 2-C 15 alkyl ethoxysulfate surfactant with a degree of ethoxylation of amount 3 (LSDP=4), and the C I 4-C 15 ethoxylated alcohols with an average degree of ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol A012 and Lutensol A030 respectively, by BASF GmbH.
Polymeric lime soap peptisers suitable for use herein are described in the article by M.K. Nagarajan, W.F. Masler, to be found in Cosmetics and Toiletries, volume 104, pages 7173,(1989).
Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyljbenzene sulfonate, 4[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl6-aminohexanoyl]benzene sulfonate and mixtures thereof; and nonanoyloxy benzene sulfonate together with hydrophilic hydrophobic bleach formulations can also be used as lime soap peptisers compounds.
Enzyme Stabilizers - 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. AC13 giving proteases, xylanases and cellulases, is described in WO 9401532 to Novo. The enzymes employed herein can be stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions which provide such ions to the enzymes. Suitable enzyme stabilizers and levels of use are described in U.S. Pat. No. 5,576, 282.
Other Detergent Ingredients - The bleaching compositions herein may also optionally contain one or more of the following: polymeric dispersing agents, clay soil removal/antiredeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids and/or pigments. Suitable examples of such other detergent ingredients and levels of use are found in U.S. Patent No. 5,576,282.
Test Protocol The following test protocols, covering enzymes, preferably detergent enzymes generally, and proteases, amylases and cellulases, specifically, have been included to aid in the determination as to what enzymes fall within the scope of the present invention. If an enzyme that is subjected to microwave irradiation exhibits greater activity than the same enzyme not subjected to microwave irradiation as determined by these test protocols, then that enzyme falls within the scope of the present invention. The following test protocols include a generic enzyme 42 protocol, a protease-specific protocol, an amylase-specific protocol and a cellu lase- specific protocol.
Generic Step 1: Determination of Non-irradiated EnZyme Activi Non-irradiated enzyme (control enzyme activity) activity is measured by heating the enzyme either diluted (1:2 in 10 mM Potassium phosphate buffer) or undiluted in a 40 'C water bath for 30 seconds, cooled to room temperature and activity measured by an enzyme suitable measurement method for the type of enzyme being tested.
Step 2: Preparation of Enzyme Assay Liquid enzyme raw material of the non-irradiated enzyme is diluted with an appropriate buffer, preferably 10 mM potassium phosphate buffer such that the enzyme solution has pH 7.5.
Step 3: Irradiating Enzyme Assqy The enzyme assay is subjected to microwave irradiation using a domestic microwave having a maximum power of 1100 watts. The irradiating power used for this protocol is 10% of the maximum power or 110 watts. The enzyme assay is irradiated under 110 watts for a time of 30 seconds.
Step 4: Measuring Irradiated Ename Activily The irradiated enzyme activity is measured after irradiating in Step 3 by further diluting, if appropriate for measurement convenience, in the same buffer to 1:100 by a measurement method suitable for the irradiated enzyme. All enzyme activities are measured by the rate of change of absorbance under enzyme suitable measurement methods.
Step 5: Dete ination of Irradiated Enzyme Activity Compared to Nonirradiated Enzyme Activiiy The results of the irradiated enzyme activity are expressed as a percent of activity of the non-irradiated (control) enzyme.
Proteases Step 1: Determination of Non-irradiated EnZyme Activity Non-irradiated enzyme (control enzyme activity) activity is measured by heating the enzyme either diluted (1:2 in 10 mM Potassium phosphate buffer) or undiluted in a 40 'C water bath for 30 seconds, cooled to room temperature and activity measured by pNA andlor casein methods.
Step 2: Preparation of Enzyme Assay Liquid enzyme raw material of the non-irradiated enzyme is diluted 1:2 with 10 mM buffer (potassium phosphate buffer) such that the enzyme solution has pH 7.5.
43 Step 3: Irradiating Enzyme Assay The enzyme assay is subjected to microwave irradiation using a domestic microwave having a maximum power of I 100 watts. The irradiating power used for this protocol is 10% of the maximum power or I 10 watts. The enzyme assay is irradiated under I 10 watts for a time of 30 seconds.
Step 4: Measuring Irradiated EnZyme Activity The irradiated enzyme activity is measured after irradiating in Step 3 by further diluting in the same buffer to 1: 100 for measurement of pNA activity. All pNA activities are measured by the rate of change of absorbance at 410 run for 3 0 seconds.
Step 5: Determination of Irradiated Enzyme Activity Compared to Nonirradiated Enzyme Activi1y The results of the irradiated enzyme activity are expressed as a percent of activity of the non-irradiated (control) enzyme.
Amylases Step 1: Determination of Non-irradiated Enzyme Activi1y Non-irradiated enzyme activities were measured by heating the enzyme either diluted (1:2 in 10 mM Potassium phosphate buffer) or undiluted in a40C water bath for 30 seconds, cooled to room temperature and activities measured by the p-nitrophenol method (SIGMA 577).
Step 2: PreRaration of EnKyme Assgy Liquid enzyme raw material of the non-irradiated enzyme is diluted 1:2 with 10 mM buffer (potassium phosphate buffer) such that the enzyme solution has pH 7.5.
Step 3: Irradiating EnZyme Ass The enzyme assay is subjected to microwave irradiation using a domestic microwave having a maximum power of I 100 watts. The irradiating power used for this protocol is 10% of the maximum power or I 10 watts. The enzyme assay is irradiated under I 10 watts for a time of 30 seconds.
Step 4: Measuring Irradiated Enzyme Activit The irradiated enzyme activity is measured after irradiating in Step 3 by cooling the enzyme assay and further diluting in the same buffer 2000- fold. Irradiated amylase activity is measured by the SIGMA diagnostic kit (procedure #577) commercially available from Sigma Chemicals of St. Louis, Missouri. The irradiated amylase enzyme is incubated with the SIGMA reagent in distilled water as per method protocols of the #577 procedure and the reaction is allowed to proceed for 5 minutes. The reaction is stopped by adding 10 LL of acetonitrile to precipitate the protein. The intensity of the yellow color of the precipitate is measured at 405 nm.
44 Step 5: Determination of Irradiated Enzyme Activity Compared to Nonirradiated Enzyme Activity The results of the irradiated enzyme activity are expressed as a percent of activity of the non-irradiated (control) enzyme.
Cellulases Step 1: Determination of Non-irradiated Enzyme Activi Non-irradiated enzyme activities were measured by heating the enzyme either diluted (1:2 in 10 mM Potassium phosphate buffer) or undiluted in a 40C water bath for 30 seconds, cooled to room temperature and activities measured by the hydrolysis rate of carboxymethycellulose.
Step 2: Preparation of Enzyme Assa Liquid enzyme raw material of the non-irradiated enzyme is diluted 1:2 with 10 mM buffer (potassium phosphate buffer) such that the enzyme solution has pH 7.5, if necessary. Preferably, cellulase stock, such as Carezyme8 stock is used as the enzyme assay, in which case no dilution is required.
Step 3: Irradiating Enzyme Ass The enzyme assay is subjected to microwave irradiation using a domestic microwave having a maximum power of I 100 watts. The irradiating power used for this protocol is 10% of the maximum power or I 10 watts. The enzyme assay is irradiated under I 10 watts for a time of 20 seconds.
Step 4: Measuring Irradiated EnZyme Activity The irradiated enzyme activity is measured after irradiating in Step 3 by cooling the enzyme assay and diluting the enzyme assay 200-fold with 10 mM of a buffer (potassium phosphate buffer) such that the enzyme assay has pH 7.5. The cellulase activity is assayed by the DNSA reducing sugar assay method using 2 mL of a 1.25% solution of sodium carboxymethy1cellulose commercially available from Sigma Chemicals of St. Louis, Missouri under the product name # C5678.
Step 5: Determination of Irradiated EnKyme Activity Compared to Nonirradiated Enzyme Activity The results of the irradiated enzyme activity are expressed as a percent of activity of the non-irradiated (control) enzyme.
Examples
Cleaning Compositions for Hard Surfaces, Dishes and Fabrics Examples I. Hard surface cleaning coml2ositions As used herein "hard surface cleaning composition" refers to liquid and granular detergent compositions for cleaning hard surfaces such as floors, walls, bathroom tile, and the like. Hard surface cleaning compositions of the present invention comprise an effective amount of one or more protease enzymes, preferably from about 0.0001% to about 10%, more preferably from about 0.001% to about 5%, more preferably still from about 0.001% to about 1% by weight of active protease enzyme of the composition. In addition to comprising one or more protease enzymes, such hard surface cleaning compositions typically comprise a surfactant and a water-soluble sequestering builder. In certain specialized products such as spray window cleaners, however, the surfactants are sometimes not used since they may produce a filmy/streaky residue on the glass surface. (See U.S. Patent No. 5,679, 630 Examples).
The surfactant component, when present, may comprise as little as 0.1% of the compositions herein, but typically the compositions will contain from about 0.25% to about 10%, more preferably from about I% to about 5% of surfactant.
Typically the compositions will contain from about 0.5% to about 50% of a detergency builder, preferably from about 1% to about 10%. Preferably the pH should be in the range of about 8 to 12. Conventional pH adjustment agents such as sodium hydroxide, sodium carbonate or hydrochloric acid can be used if adjustment is necessary.
Solvents may be included in the compositions. Useful solvents include, but are not limited to, glycol ethers such as diethyleneglycol monohexyl ether, diethyleneglycol monobutyl ether, ethyleneglycol monobutyl ether, ethyleneglycol monohexyl ether, propyleneglycol monobutyl ether, dipropyleneglycol monobutyl ether, and diols such as 2,2,4-trimethyl-1, 3pentanediol and 2-ethyl-1,3-hexanediol. When used, such solvents are typically present at levels of from about 0.5% to about 15%, preferably from about 3% to about 11%.
Additionally, highly volatile solvents such as isopropanol or ethanol can be used in the present compositions to facilitate faster evaporation of the composition from surfaces when the surface is not rinsed after "full strength" application of the composition to the surface. When used, volatile solvents are typically present at levels of from about 2% to about 12% in the compositions.
The hard surface cleaning composition embodiment of the present invention is illustrated by the following nonlimiting examples.
46 Examples 1-7
Liquid Hard Surface Cleaning Compositions Example No.
Component 1 2 3 4 5 6 7 Activated Protease 0.05 0.05 0.20 0.02 0.03 0.10 0.03 Protease - - - - - 0.20 0.1 Chelant 2.90 2.90 - - Citrate - - - 2.90 2.90 LAS - 1.95 - 1.95 - 1.95 - AS 2.00 - 2.20 - 2.20 - 2.20 AES 2.00 2.20 - 2.20 - 2.20 Amine Oxide 0.40 - 0.50 - 0.50 - 0.50 Hydrotrope - 1.30 - 1.30 - 1.30 - Solvent 6.30 6.30 6.30 6.30 6.30 6.30 Water and Minors balance to 100% Na4 ethylenediamine diacetic acid Diethyleneglycol monohexyl ether All formulas adjusted to pH 7 Examples 8-13
Spray Compositions for Cleaning Hard Surfaces and Removing Household Mildew Example No.
Component 8 9 10 11 12 13 Activated Protease 0.20 0.05 0.10 0.30 0.20 0.30 Protease - - - - 0.30 0.10 C8AS 2.00 2.00 2.00 2.00 2.00 2.00 C12AS 4.00 4.00 4.00 4.00 4.00 4.00 Base 0.80 0.80 0.80 0.80 0.80 0.80 Silicate 0.04 0.04 0.04 0.04 0.04 0.04 Perfume 0.35 0.35 0.35 0.35 0.35 0.35 Water and Minors balance to 100% Product pH is about 7.
2. Dishwashing Compositions Examples 14-19 Dishwashing Composition Example No.
47 Component 14 15 16 17 18 19 Activated Protease 0.05 0.50 0.02 0.40 0.10 0.03 Protease - - - - 0.40 0.1 TFAA 1 0.90 0.90 0.90 0.90 0.90 0.90 AES 12.00 12.00 12.00 12.00 12.00 12.00 2-methyl undecanoic acid 4.50 4.50 -4.50 4.50 - C12 alcohol ethoxylate (4) 3.00 3.00 3.00 3.00 3.00 3.00 Amine oxide 3.00 3.00 3.00 3.00 3.00 3.00 Hydrotrope, 2.00 2.00 2.00 2.00 2.00 2.00 Ethanol 4.00 4.00 4.00 4.00 4.00 4.00 Mg++ (as M902) 0.20 0.20 0.20 0.20 0.20 0.20 Ca++ (as CaC12) 0.40 0.40 0.40 0.40 0.40 0.40 Water and Minors balance to 100% Product pH is adjusted to 7.
48 Example 20
Dishwashing Compositions CoMponent A (ADW) B(ADW) C(LM) STPP 17.J5 Citrate 15.0 0 Sodium polyacrylate (MW 4500) 0.80 Acusol 4SON - 5.10 Potassium carbonate 8.30 - Sodium carbonate - 8.50 2. 1 r K Silicate 3.99 - 2.Or Na S-ificate 2.00 3.2r Na Silicate 5.18 Aluminum tristearate 0.10 Nonionic surfactant 2.50 - NaAEO.6S - 24.70 Glucose amide - 3.09 CIOE8 4.11 Betaine - 2.06 Amine oxide - 2.06 Magnesium as oxide - 0.49 Hydrotrope - - 4.47 Sodium hypochlorite as AvCl, 1.15 - - Activated Protease 0.01 0.43 0.05 Balance to 100% 49 Example 21 Liquid Dishwashing Compositions (especially suitable under Japanese conditions) Component A B C D AEIAS 24.69 24.69 24.69 24.69 N-cocoyl N-methyl glucarnine 3.09 3.09 3.09 3.09 Arnine oxide 2.06 2.06 1 2.06 2.06 Betaine 2.06 2.06 2.06 2.06 Nonionic surfactant 4.11 4.11 4.11 4.11 Hydrotrope 4.47 4.47 4.47 4.47 Magnesium 0.49 0.49 0.49 0.49 Ethanol 7.2 7.2 7.2 7.2 LernonEase 0.45 0.45 0.45 0.45 Geraniol/BHT - 0.60/0.0 - 0.60/0.02 2 Arnylase 0.03 - Protease 0.43 - - Activated Amylase - 0.005 1 0.03 0.005 1 Activated Protease 0.01 0.01 0.43 Balance to 100% Example 22 Granular Automatic Dishwashing Composition Component A B c Citric Acid 15.0 - Citrate 4.0 29.0 15.0 Acrylate/methacrylate copolymer 6.0 - 6.0 Acrylic acid maleic acid copolymer - 3.7 - Dry add carbonate 9.0 - 20.0 Alkali metal silicate 8.5 17.0 9.0 Paraffin - 0.5 - Benzotriazole - 0.3 - Termainyl 60T 1.6 1.6 1.6 Activated Protease 0.2 0.1 0.06 Percarbonate (AvO) 1.5 - Perborate monohydrate - 0.3 1.5 Perborate tetrahydrate - 0.9 - Tetraacetylethylene diamine 3.8 4.4 - Diethylene triamine penta methyl Phosphonic acid 0.13 0.13 0.13 (Mg salt) Alkyl ethoxy sulphate - 3 times ethoxylated 3.0 Alkyl ethoxy propoxy nonionic surfactant - 1.5 Suds suppressor 2.0 - Olin SLF18 nonionic surfactant - 2.0 Sulphate Balance to 100% 51 Example 23 Compact high density (0.96Kg/1) dishwashing detergent compositions A to F in accordance with the invention:
Component A B c D E F STPI? - 51.4 51.4 - - 44.3 Citrate 17.05 - - 49.6 40.2 - Carbonate 17.50 14.0 20.0 8.0 33.6 Bicarbonate - - - 26.0 - Silicate 14.81 15.0 8.0 - 25.0 3.6 Metasilicate 2.50 4.5 4.5 - - PB1 9.74 7.79 7.79 - PB4 - - - 9.6 - - Perearbonate - - - - 11.8 4.8 Nonionic 2.00 1.50 1.50 2.6 1.9 5.9 TAED 2.39 - - 3.8 - 1.4 HEDP 1.00 - - DETPMP 0.65 MnTACN - - - 0.008 PAM - 0.008 0.008 - - Paraffin 0.50 0.38 0.38 0. Activated Protease 0.1 0.06 0.05 0.03 0.07 0.01 Activated Arnylase 1.5 1.5 1.5 2.6 2.1 0.8 BTA 0.30 0.22 0.22 0.3 0.3 0.3 Polycarboxylate 6.0 - - 4.2 0.9 Perfume 0.2 0.12 0.12 0.2 0.2 0.2 Sulphate / Water 20.57 1.97 2.97 3.6 4.5 3.9 pH (1% Solution) 11.0 11.0 11.3 9.6 10.8 10.9 52 Example 24
Granular dishwashing detergent compositions examples A to F of bulk density 1.02Kg/L in accordance with the invention:
Component A B c D E F STPP 30.00 33.5 27.9 29.62 33.8 22.0 Carbonate 30.50 30.50 30.5 23.00 34.5 45.0 Silicate 7.40 7.5.0 12.6 13.3 3.2 6.2 Metasilicate - 4.5 Percarbonate - - - 4.0 P131 4.4 4.5 4.3 - - NaDCC - 2.00 - 0.9 Nonionic 1.0 0.75 1.0 1.90 0.7 0.5 TAED 1.00 - - 0.9 PAM 0.004 - Paraffin 0.25 0.25 - - Activated Protease 0.05 0.06 0.025 0.1 0.02 0.07 Activated Amylase 0.38 0.64 0.46 - 0.6 BTA 0.15 0.15 - 0.2 Perfume 0.2 0.2 0.05 0.1 0.2 Sulphate/water 1 23.45 16.87 22.26 30.08 21.7 25.4 pH (1 % solution) 10.80 11.3 11.0 10.70 1 11.5 10.9 53 Example 25
Tablet detergent composition examples A to H in accordance with the present invention are prepared by compression of a granular dishwashing detergent composition at a pressure of 13KN/cin2 using a standard 12 head rotary press:
Component A B c D E F G H STPP - 48.8 54.7 38.2 - 52.4 56.1 36.0 Citrate 20.0 - - - 35.9 - - - Carbonate 20.0 5.0 14.0 15.4 8.0 23.0 20.0 28.0 Silicate 15.0 14.8 15.0 12.6 23.4 2.9 4.3 4.2 Activated Protease 0.05 0.09 0.05 0.03 0.06 0.03 0.03 0.1 Activated Arnylase 1.5 1.5 1.5 0.85 1.9 0.4 2.1 0.3 PB1 14.3 7.8 11.7 12.2 - - 6.7 8.5 PB4 - - - - 22.8 - 3.4 Perearbonate - - - - - 10.4 - Nonionic 1.5 2.0 2.0 2.2 1.0 4.2 4.0 6.5 PAM - - 0.016 0.009 - - - - MnTACN - - - - 0.007 - - - TAED 2.7 2.4 - - - 2.1 0.7 1.6 HEDP 1.0 - - 0.93 0.4 0.2 - DETPIVIP 0.7 - - - - - - Paraffin 0.4 0.5 0.5 0.55 - 0.5 - BTA 0.2 0.3 0.3 0.33 0.3 0.3 0.3 - Polycarboxylate 4.0 - - - 4.9 0.6 0.8 - PEG - - - - 2.0 - 2.0 Glycerol - - 0.4 - 0.5 Perfume 0.05 0.20 0.2 0.2 0.2 Sulphate / water 17.4 14.7 - 15.74 11.3 weight of tablet 20g 25g 20g 30g 18g 20g 25g 24.0 pH (1% solution) 10.7 10.6 10.7 10.7 10.9 11.2 11.0 10.8 54 Example 26 Dimple Tablet Automatic Dishwashing Composition Component A (% R.M.) 11 (g R.M.) C (g R.M.) Tablet Body
Sodium Carbonate 15.348 3.500 5.25 STPP(12% H20) 46.482 10.600 9.93 Gran HEDP 0.789 0.180 0.28 SKS 6 6.578 1.500 2.25 2 ratio Silicate 7.016 1.600 1.65 PB1 10.743 2.450 3.68 Termamyl 2x PCA 0.491 0.112.17 Activated Savinase 0.526 0.120 0.18 Plurafac 3.508 0.800 0.9 BTA 0.263 0.060 0.09 PEG 1.140 0.260 - PEG 4000 - - 0.39 Winog 0.439 0.100 0.15 Perfume 0.101 0.023 0.01 Dimple Filling Citric Acid 0.987 0.225 0.23 Bicarbonate 2.600 0.593 0.59 Sandolan EBRL Dye 0.007 0.0017 0.0017 PEG 400/4000 0.395 0.090 PEG 400 - 0.02 PEG 4000 - - 0.08 Arnylase 1.412 0.322 0.32 Protease 0.05 0.268 0.27 3. Fabric cleaning compositions Granular Fabric Cleaning Composition The granular fabric cleaning compositions of the present invention contain an effective amount of one or more protease enzymes, preferably from about 0.001% to about 10%, more preferably, from about 0.005% to about 5%, more preferably from 0.0 1% to about I% by weight of active protease enzyme of the composition. (See U.S. Patent No. 5,679,630 Examples).
Example 27 Granular Fabric Cleaning Compo ition Example No.
Component A B C D Activated Protease 0.10 0.20 0.03 0.05 Protease - - 0.2 0.15 C 13 linear alkyl benzene sulfonate 22.00 22.00 22.00 22.00 Phosphate (as sodium 23.00 23.00 23.00 23.00 tripolyphosphates) Sodium carbonate 23.00 23.00 23.00 23.00 Sodium silicate 14.00 14.00 14.00 14.00 Zeolite 8.20 8.20 8.20 8.20 Chelant (diethylaenetriamine- 0.40 0.40 0.40 0.40 pentaacetic acid) Sodium sulfate 5.50 5.50 5.50 5.50 Water balance to 100% Example 28 Granular Fabric Cleaning Composition Example No.
Component A B C D Activated Protease 0.10 0.20 0.03 0.05 Protease - - 0.2 0.1 C12 alkyl benzene sulfonate 12.00 12.00 12.00 12.00 Zeolite A (1 micrometer) 26.00 26.00 26.00 26.00 C12-CI4 secondary (2,3) alkyl sulfate, 5.00 5.00 5.00 5.00 Na salt Sodium citrate 5.00 5.00 5.00 5.00 Optical brightener 0.10 0.10 0.10 0.10 Sodium sulfate 17.00 17.00 17.00 17.00 Fillers, water, minors balance to 100% 56 Example 29 Granular Fabric Cleaning Compositions Components Example No.
A B Linear alkyl benzene sulphonate 11.4 10.70 Tallow alkyl sulphate 1.80 2.40 C 14-15 alkyl sulphate 3.00 3.10 C 14-15 alcohol 7 times ethoxylated 4.00 4.00 Tallow alcohol 11 times ethoxylated 1.80 1.80 Dispersant 0.07 0.1 Silicone fluid 0.80 0.80 Trisodium citrate 14.00 15.00 Citric acid 3.00 2.50 Zeolite 32.50 32.10 Maleic acid acrylic acid copolymer 5.00 5.00 Diethylene triamine penta methylene 1.00 0.20 phosphonic acid Activated Protease 0.1 0.01 Lipase 0.36 0.40 Activated Amylase 0.30 0.30 Sodium silicate 2.00 2.50 Sodium sulphate 3.50 5.20 Polyvinyl pyrrolidone 0.30 0.50 Perborate 0.5 1 Phenol sulphonate 0.1 0.2 Peroxidase 0.1 0.1 Minors UP to 100 UP to 100 57 Example 30 Granular Fabric Cleaning Compositions Example No.
Components A B Sodium linear C12 alkyl benzene-sulfonate 6.5 8.0 Sodium sulfate 15.0 18.0 Zeolite A 26.0 22.0 Sodium nitrilotriacetate 5.0 5.0 Polyvinyl pyrrolidone 0.5 0.7 Tetraacetylethylene diamine 3.0 3.0 Boric acid 4.0 - Perborate 0.5 1 Phenol sulphonate 0.1 0.2 Activated Protease 0.02 0.05 Fillers (e.g., silicates; carbonates; perfumes; water) Up to 100 Up to 100 58 Example 31 Compact Granular Fabric Cleaning Composition Components Weight % Alkyl Sulphate 8.0 Alkyl Ethoxy Sulphate 2.0 Mixture of C25 and C45 alcohol 3 and 7 times ethoxylated 6.0 Polyhydroxy fatty acid amide 2.5 Zeolite 17.0 Layered silicate/citrate 16.0 Carbonate 7.0 Maleic acid acrylic acid copolymer 5.0 Soil release polymer 0.4 Carboxymethyl cellulose 0.4 Poly (4-vinylpyridine) -N-oxide 0.1 Copolymer of vinylimidazole and vinylpyrrolidone 0.1 PEG2000 0.2 Activated Protease 0.03 Lipase 0.2 Cellulase 0.2 Tetracetylethylene diamine 6.0 Percarbonate 22.0 Ethylene diarnine disuccinic acid 0.3 Suds suppressor 3.5 Disodium-4,4'-bis (2-morpholino -4-anilino-s-triazin-6- 0.25 ylamino) stilbene-2j-disulphonate Disodium-4,4'-bis (2-sulfostyril) biphenyl 0.05 Water, Perfume and Minors Up to 100 59 Example 32
Granular Fabric Cleaning Composition Component Weight % Linear alkyl benzene sulphonate 7.6 C 1 6-C 18 alkyl sulfate 1.3 C 14-15 alcohol 7 times ethoxylated 4.0 Coco-alkyl-dimethyl hydroxyethyl ammonium chloride 1.4 Dispersant 0.07 Silicone fluid 0.8 Trisodium citrate 5.0 Zeolite 4A 15.0 Maleic acid acrylic acid copolymer 4.0 Diethylene triamine penta methylene phosphonic acid 0.4 Perborate 15.0 Tetraacetylethylene diamine 5.0 Smectite clay 10.0 Poly (oxy ethylene) (MW 300,000) 0.3 Activated Protease 0.02 Lipase 0.2 Activated Arnylase 0.3 Cellulase 0.2 Sodium silicate 3.0 Sodium carbonate 10.0 Carboxymethyl cellulose 0.2 Brighteners 0.2 Water, perfume and minors Up to 100 Example 33
Granular Fabric Cleaning Composition Component Weight % Linear alkyl benzene sulfonate 6.92 Tallow alkyl sulfate 2.05 C14-15 alcohol 7 times ethoxylated 4.4 C12-15 alkyl ethoxy sulfate - 3 times ethoxylated 0.16 Zeolite 20.2 Citrate 5.5 Carbonate 15.4 Silicate 3.0 Maleic acid acrylic acid copolymer 4.0 Carboxyrnethyl cellulase 0.31 Soil release polymer 0.30 Activated Protease 0.1 Lipase 0.36 Cellulase 0.13 Perborate tetrahydrate 11.64 Perborate monohydrate 8.7 Tetraacetylethylene diarnine 5.0 Diethylene trarnine penta methyl phosphonic acid 0.38 Magnesium sulfate 0.40 Brightener 0.19 Perfume, silicone, suds suppressors 0.85 Minors Up to 100 61 Example 34 Granular Fabric Cleaniniz Comt)osition Component A B C Base Granule Components LAS/AS/AES (65/35) 9.95 - LAS/AS/AES (70/30) 12.05 7.70 Alumino silicate 14.06 15.74 17.10 Sodium carbonate 11.86 12.74 13.07 Sodium silicate 0.58 0.58 0.58 NaPAA Solids 2.26 2.26 1.47 PEG Solids 1.01 1.12 0.66 Brighteners 0.17 0.17 0.11 DTPA - - 0.70 Sulfate 5.46 6.64 4.25 DC-1400 Deaerant 0.02 0.02 0.02 Moisture 3.73 3.98 4.33 Minors 0.31 0.49 0.31 B.O.T. Spray-on Nonionic surfactant 0.50 0.50 0.50 Agglomerate Components LAS/AS (25/75) 11.70 9.60 10.47 Alumino silicate 13.73 11.26 12.28 Carbonate 8.11 6.66 7.26 PEG 4000 0.59 0.48 0.52 Moisture/1%4inors 4.88 4.00 4.36 Functional Additives Sodium carbonate 7.37 6.98 7.45 Perborate 1.03 1.03 2.56 AC Base Coating - 1.00 - NOBS - 2.40 Soil release polymer 0.41 0.41 0.31 Cellulase 0.33 0.33 0.24 Activated Protease 0.1 0.05 0.15 AE-Flake 0.40 0.40 0.29 Liquid Spray-on Perfume 0.42 0.42 0.42 62 Noionic spray-on 1.00 1.00 0.50 Minors UP to 100 Example 35 Granular Fabric Cleaning Composition A B Surfactant - Na LAS 6.40 - - KLAS - 9.90 - AS/AE3 S 6.40 4.39 - TAS 0.08 0.11 - C24AE5 3.48 Genagen - 1.88 N-cocoyl N-methyl 1.14 2.82 glucamine (fin) - C8-10 dimethyl 1.00 1.40 hydroxyethyl ammonium chloride Builder - Zeolite 20.59 13.39 - SKS-6 10.84 10.78 - Citric Acid 2.00 - Buffer Carbonate 9.60 12.07 Bicarbonate 2.00 2.00 - Sulphate 2.64 - - Silicate 0.61 0.16 Polymer Acrylic acid/maleic 1.17 1.12 acid copolymer (Na) - Carboxyinethyl 0.45 0.24 cellulose 1 63 Polymer 0.34 0.18 Hexamethylene- 1.00 1.00 diamine tetra-E24 ethoxylate, diquaternized with methyl chloride Enzyme Activated Protease 0.03 0.03 (% pure enzyme) Cellulase 0.26 0.26 Activated Arnylase 0.65 0.73 Lipase 0.27 0.15 Bleach TAED (100%) 3.85 3.50 Phenoisuifonate - 2.75 ester of N-nonanoyl-6 aminocaproic acid Percarbonate 16.20 18.30 HEDP 0.48 0.48 EDDS 0.30 0.30 Miscellaneous Malic particle 2.20 + bicarb Brightener 15149 0.077/0.014 0.07/0.014 Zinc phthalocyanine 0.0026 0.0026 sulfonate - Polydimethylsiloxane 0.25 0.24 with trimethylsilyl end blocking units Soap - 1.00 Perfume 0.45 0.55 TOTAL 100 100 64 Example 36 Granular Fabric Cleaning Composition A B Surfactant NaLAS 6.8 0.4 KLAS - 10.9 FAS 0.9 0.1 AS 0.6 1.5 C25AE3S 0.1 - AE5 4.2 N-Cocoyl-N-Methyl Glucarnine - 1.8 Genagen 1.2 C8-1 0 dimethyl hydroxyethyl - 1.0 ammonium chloride Builder SKS-6 3.3 9.0 Zeolite 17.2 18.9 Citric Acid 1.5 - Buffer Carbonate 21.1 15.0 Sodium Bicarbonate - 2.6 Sulphate 15.2 5.5 Malic Acid - 2.9 Silicate 0.1 - Polymer Acrylic acid/maleic acid copolymer 2.2 0.9 (Na) Hexamethylene-diamine tetra-E24 0.5 0.7 etboxylate, diquaternized with methyl chloride Polymer 0.1 0.1 CNIC 0.2 0.1 Enzymes Activated Protease (% pure enzyme) 0.02 0.05 Lipase 0.18 0.14 1 Activated Amylase 0.64 0.73 Cellulase 0.13 0.26 Bleach TAED 2.2 2.5 PhenoIsulfonate ester of N-nonanoyl- - 1.96 6-aminocaproic acid Sodium Percarbonate - 13.1 PB4 15.6 - EDDS 0.17 0.21 MgS04 0.35 0.47 HEDP 0.15 0.34 Miscellaneous Brightener 0.06 0.04 - Zinc phthalocyanine sulfonate 0.0015 0.0020 - Polydimethylsiloxane with 0.04 0.14 trimethylsilyl end blocking units Soap 0.5 0.7 Perfume 0.35 0.45 Speckle 0.5 0.6 Example 37
The following granular laundry detergent compositions 37 A-C are of particular utility under European machine wash conditions were prepared in accord with the invention:
Component A B C LAS 7.0 5.61 4.76 TAS - - 1.57 C45AS 6.0 2.24 3.89 C25E3S 1.0 0.76 1.18 C45E7 - 2.0 C25E3 4.0 5.5 - 66 QAS 0.8 2.0 2.0 STPP - Zeolite A 25.0 19.5 19.5 Citric acid 2.0 2.0 2.0 NaSKS-6 8.0 10.6 10.6 Carbonate 1 8.0 10.0 8.6 MA/AA 1.0 2.6 1.6 CNIC 0.5 0.4 0.4 PB4 - 12.7 Percarbonate - - 19.7 TAED 3.1 5.0 Citrate 7.0 - - DTPMP 0.25 0.2 0.2 HEDP 0.3 0.3 0.3 QEA 1 0.9 1.2 1.0 Activated Protease, 0.02 0.05 0.035 Lipase 0.15 0.25 0.15 Cellulase 0.28 0.28 0.28 Activated Arnylase 0.4 0.7 0.3 PWI/ PVNO 0.4 - 0.1 Photoactivated bleach (ppm) 15 ppm 27 ppm 27 ppm 67 Brightener 1 0.08 0.19 0.19 Brightener 2 - 0.04 0.04 Perfume 0.3 0.3 0.3 Effervescent granules malic acid 15 15 5 40%, sodium bicarbonate 40%, sodium carbonate 20%) Silicone antifoam 0.5 2.4 2.4 Minors/inerts to 100% Example 38
The following formulations are examples of compositions in accordance with the invention, which may be in the form of granules or in the form of a tablet.
Component 38 C45 ASITAS 3.0 LAS 8.0 C25AE3S 1.0 NaSKS-6 9.0 C25AES/AE3 5.0 Zeolite A 10.0 SKS-6 (I) (dry add) 2.0 MA/AA 2.0 Citric acid 1.5 EDDS 0.5 HEDP 0.2 PB1 10.0 NACA OBS 2.0 TAED 2.0 Carbonate 8.0 Sulphate 2.0 Activated Arnylase 0.3 Lipase 0.2 Enzyme 0.02 Minors (Brightener/SRP1/ 0.5 CMC/Photobleach/ MgSO4/ PWV1/Suds suppressor/ PEG) Perfume 0.5 68 Example 39
Granular laundry detergent compositions 39 A-E are of particular utility under Japanese machine wash conditions and are prepared in accordance with the invention:
Component A B c D E LAS 23.57 23.57 21.67 21.68 21.68 FAS 4.16 4.16 3.83 3.83 3.83 Nonionic surfactant 3.30 3.30 2.94 3.27 3.27 Bis (hydroxyethyl) methyl alkyl 0.47 0.47 1.20 1.20 1.20 ammonium chloride SKS-6 7.50 7.50 5.17 5.76 5.06 Polyacrylate copolymer (MW 7.03 7.03 14.36 14.36 14.36 11000) (maleic/acrylate ratio of 4:6) Zeolite 11.90 11.40 10.69 11.34 11.34 Carbonate 14.90 14.82 11.71 11.18 11.18 Silicate 12.00 12.00 12.37 12.38 12.38 Activated Protease 0.016 O.OR 0.046 0.046 0.046 Lipase - 0.28 - - Activated Arnylase 0.62 - Cellulase 0.48 0.70 NOBS 3.75 3.75 2.70 2.70 2.70 PB1 3.53 - 2.60 - - Sodium percarbonate - 4.21 - 3.16 3.16 1 69 SRP 0.52 0.52 0.70 0.70 0.70 Brightener 0.31 0.31 0.28 0.28 0.50 AE-coflake 0.17 0.20 0.17 0.17 0.17 Polydimethylsiloxane - - 0.68 0.68 0.68 Perfume 0.06 0.06 0.08 - - Perfume - - - 0.23 0.23 Hydrophobic precipitated silica 0.30 0.30 0.30 0.30 0.30 PEG4000 0.19 0.19 0.17 0.17 0.17 Minors/inerts to 100% Liquid Fabric Cleaning Compositions Liquid fabric cleaning compositions of the present invention preferably comprise an effective amount of one or more protease enzymes, preferably from about 0.0001% to about 10%, more preferably from about 0.00 1 % to about I %, and most preferably from about 0.00 1 % to about 0. 1 % by weight of active protease enzyme of the composition. (See U. S. Patent No. 5,679,630 Examples).
Example 40
Liquid Fabric Cleaning Compositions Example No.
Component A B C D E Activated Protease 0.05 0.03 0.30 0.03 0.10 Protease - - 0.1 0.20 C 12- C 14 alkyl sulfate, Na 20.00 20.00 20.00 20.00 20.00 2-Butyl octanoic acid 5.00 5.00 5.00 5.00 5.00 Sodium citrate 1.00 1.00 1.00 1.00 1.00 Clo alcohol ethoxylate (3) 13.00 13.00 13.00 13.00 13.00 Monethanolamine 2.50 2.50 2.50 2.50 2.50 Water/pMpylene glycol/ethanol 0 00: 1: 1) balance to 100% Example 41 Liquid Fabric Cleaning Compositions Example No.
Component A B C12-14 alkenyl succinic acid 3.0 8.0 Citric acid monohydrate 10.0 15.0 Sodium C12-15 alkyl sulphate 8.0 8.0 Sodium sulfate Of C 12-15 alcohol 2 times ethoxylated 3.0 C 12-15 alcohol 7 times ethoxylated 8.0 Diethylene triamine penta (methylene phosphonic acid) 0.2 - Oleic acid 1.8 - Ethanol 4.0 4.0 Propanediol 2.0 2.0 Activated Protease 0.01 0.02 Polyvinyl pyrrolidone 1.0 2.0 Suds suppressor 0.15 0.15 NaOH up to pH 7.5 Perborate 0.5 1 Phenol sulphonate 0.1 0.2 Peroxidase 0.4 0.1 Waters and minors up to 100 % 71 Example 42 Liquid Fabric Cleaning Compositions Example No.
Component 42 NaLAS (1 00%am) 16 Neodol 21.5 Citrate 6.8 EDDS 1.2 Dispersant 1.3 Perborate 12 PhenoIsulfonate ester of N-nonanoyl-6-aminocaproic acid 6 Protease (% pure enzyme) 0.03 Activated Arnylase 0.40 Cellulase 0.03 Solvent (BPP) 18.5 Polymer 0.1 Carbonate 10 FWA 15 0.2 Ti02 0.5 PEG 8000 0.4 Perfume LO-1.2 Suds suppressor 0.06 Waters and minors up to 100% 72 Example 43 Liquid Fabric Cleaning Compositions Example No.
Component A DI H20 38.63 MEA 0.48 9.0 NaOH 4.40 1.0 Pdiol 4.00 10.0 Citric acid 2.50 2.0 Sodium sulfate 1.75 - DTPA 0.50 1.0 FWA Premix (Br 15/MEA/NI 23-9) 0.15 0.15 Na C25AE 1. 80S 23.50 - AE3 S (H) - 4.0 C 11. 8HLAS 3.00 14.0 Neodol 2.00 6.0 EtOH 0.50 2.0 CaFormate 0.10 0.1 Borax premix (Borax/MEA/Pdiol/CitricAcid) 2.50 - Boric acid - 1.0 CIO APA 1.50 - TEPA 105 1.20 FA C12-18 5.00 - Neptune LC 0.50 - Dye 0.0040 0.0015 Cellulase 0.053 0.2 Activated Amylase 0.15 0.2 Activated Protease 0.1 0.1 DC 2-3597 0.12 0.2 Rapeseed FA 6.50 4.0 Waters and minors up to 100 % 73 Example 44 Liquid Fabric Cleaning Composition Component 44 NaOH 5.50 Pdiol 6.90 Citric acid 1.50 DTPA 1.50 FWA Premix (Br 15/MEA/NI 23-9) 0.15 AE3 S (H) 2.50 LAS (H) 13.0 Neodol 2.00 EtOH 3.50 CaFormate 0.10 Boric acid 1.00 Clay 4.00 Arnylase 0.15 Activated Protease 0.02 Fatty Acid 16.50 Waters and minors up to 100 % Example 45 Liquid Fabric Cleaning Composition Liquid fabric cleaning composition of particular utility under Japanese machine wash conditions is prepared in accordance with the invention:
Component 45 AE2.5S 15.00 AS 5.50 N-Cocoyl N-methyl glucamine, 5.00 Nonionic surfactant 4.50 Citric acid 3.00 r, 74 Fatty acid 5.00 Base 0.97 Monoethanolamine 5.10 1,2-Propanediol 7,44 EtOH 5.50 HXS 1.90 Boric acid 3.50 Ethoxylated tetraethylene- 3.00 pentaimine SRP 0.30 Activated Protease 0.069 Activated Arnylase 0.06 Cellulase 0.08 Lipase 0.18 Brightener 0.10 Minors/inerts to 100% Example 46 Liquid Fabric Cleaning Composition Liquid fabric cleaning composition of particular utility under Japanese machine wash conditions and for fine fabrics is prepared in accordance with the invention:
Component 46 AE2.5S 2.16 i AS 3.30 N-Cocoyl N-methyl glucamine 1.10 Nonionic surfactant 10.00 Citric acid 0.40 Fatty acid 0.70 Base 0.85 Monoethanolamine 1.01 1,2-Propanediol 1.92 EtOH 0.24 HXS 2.09 Activated Protease 0.01 Arnylase 0.06 Minors/inerts to 100% Bar Fabric Cleaning Compositions Bar fabric cleaning compositions of the present invention suitable for handwashing soiled fabrics typically contain an effective amount of one or more protease enzymes, preferably from about 0.001% to about 10%, more preferably from about 0.01% to about I% by weight active protease enzyme of the composition. (See U.S. Patent No. 5,679,630 Examples).
76 Example 47 Bar Fabric Cleaning Compositions Example No.
Component A B c D Activated Protease 0.3 0.1 0.02 Protease - - 0.4 0.1 C12-CI6 alkyl sulfate, Na 20.0 20.0 20.0 20.00 C 12-C 14 N-methyl glucam ide 5.0 5.0 5.0 5.00 Cl 1 -C 13 alkyl benzene sulfonate, Na 10.0 10.0 10.0 10.00 Sodium pyrophosphate 7.0 7.0 7.0 7.00 Sodium tripolyphosphate 7.0 7.0 7.0 7.00 Zeolite A (0. 1 -. 1 Og) 5.0 5.0 5.0 5.00 Carboxymethylcel lu lose 0.2 0.2 0.2 0.20 Polyacrylate (MW 1400) 0.2 0.2 0.2 0.20 Coconut monethanolamide 5.0 5.0 5.0 5.00 Brightener, perfume 0.2 0.2 0.2 0.20 CaSO4 1.0 1.0 1.0 1.00 M9S04 1.0 1.0 1.0 1.00 Water 4.0 4.0 4.0 4.00 Filler balance to 100% Can be selected from convenient materials such as CaC03, tale, clay, silicates, and the like. 4. Oral Cleaning CompositionsOral cleaning compositions (dentifrices, toothpaste, toothgels, toothpowders, mouthwashes, mouth sprays, mouth gels, chewing gum, lozenges, sachets, tablets, biogels, prophylaxis pastes, dental treatment solutions, and the like) typically contain a pharmaceutical ly-acceptable amount of one or more protease enzymes, preferably from about 0.0001% to about 20%, more preferably about 0.001% to about 10%, most preferably from about 0.01% to about 5% by weight active protease enzymes, useful in removing proteinaceous stains from teeth or dentures. (See also U.S. Patent No. 5,679,630 Examples).
77 Example 48 Dentifrice Composition Example No.
Component A B C D Activated Protease 0.4 0.35 0.15 0.2 Sorbitol (70% aqueous solution) 35.000 35.000 35.000 35.000 PEG-6 1.000 1.000 1.000 1.000 Silica dental abrasive" 20.000 20.000 20.000 20.000 Sodium fluoride 0.243 0.243 0.243 0.243 Titanium dioxide 0.500 0.500 0.500 0.500 Sodium saccharin 0.286 0.286 0.286 0.286 Sodium alkyl sulfate (27.9% 4.000 4.000 4.000 4.000 aqueous solution) Flavor 1.040 1.040 1.040 1.040 Carboxyvinyl Polymer 0.300 0.300 0.300 0.300 Carrageenan 0.800 0.800 0.800 0.800 Water balance to 100% PEG-6 = Polyethylene glycol having a molecular weight of 600. "Precipitated silica identified as Zeodent 119 offered by J.M. Huber. Carbopol offered by B.F. Goodrich Chemical Company. Iota Carrageenan offered by Hercules Chemical Company.
Example 49 Mouthwash Composition Example No.
Component A B C D Activated Protease 0.3 0.75 0.5 1.00 SDA 40 Alcohol 8.00 8.00 8.00 8.00 Flavor 0.08 0.08 0.08 0.08 Sodium Fluoride 0.05 0.05 0.05 0.05 Glycerin 10.00 10.00 10.00 10.00 Sweetener 0.02 0.02 0.02 0.02 Benzoic acid 0.05 0.05 0.05 0.05 Sodium hydroxide 0.20 0.20 0.20 0.20 Dye 0.04 0.04 0.04 0.04 Water balance to 100% 78 5. Denture Cleaning Compositions Denture cleaning compositions typically contain an effective amount of one or more protease enzymes, preferably from about 0.0001% to about 50%, more preferably from about 0.001% to about 35%, most preferably from about 0.01% to about 20% by weight active protease enzyme of the composition and a denture cleansing carrier. (See U.S. Patent No. 5,679, 630 Examples).
Example 50
Two-layer Effervescent Denture Cleansing Tablet Example No.
Component A B C D Acidic Lave Activated Protease 1.0 1.5 0.01 0.05 Tartaric acid 24.0 24.0 24.00 24.00 Sodium carbonate 4.0 4.0 4.00 4.00 Sulphamic acid 10.0 10.0 10.00 10.00 PEG 20,000 4.0 4.0 4.00 4.00 Sodium bicarbonate 24.5 24.5 24.50 24.50 Potassium persulfate 15.0 15.0 15.00 15.00 Sodium acid pyrophosphate 7.0 7.0 7.00 7.00 Pyrogenic silica 2.0 2.0 2.00 2.00 Tetracetylethylene diamine 7.0 7.0 7.00 7.00 Ricinoleylsulfosuccinate 0.5 0.5 0.50 0.50 Flavor 1.0 1.0 1.00 1.00 Alkaline Lave Sodium perborate monohydrate 32.0 32.0 32.00 32.00 Sodium bicarbonate 19.0 19.0 19.00 19.00 EDTA 3.0 3.0 3.00 3.00 Sodium tripolyphosphate 12.0 12.0 12.00 12.00 PEG 20,000 2.0 2.0 2.00 2.00 Potassium persulfate 26.0 26.0 26.00 26.00 Sodium carbonate 2.0 2.0 2.00 2.00 Pyrogenic silica 2.0 2.0 2.00 2.00 Dye/flavor 2.0 2.0 2.00 2.00 While particular embodiments of the subject invention have been described, it will be obvious to those skilled in the art that various changes and modifications of the subject 79 invention can be made without departing from the spirit and scope of the invention. It is intended to cover, in the appended claims, all such modifications that are within the scope of the invention.
The compositions of the present invention can be suitably prepared by any process chosen by the formulator, non-limiting examples of which are described in U.S. 5,691,297 Nassano et aL, issued November 11, 1997; U.S. 5,574,005 Welch et al., issued November 12, 1996; U.S. 5,569,645 Dinniwell et al., issued October 29, 1996; U.S. 5,565,422 Del Greco et al. , issued October 15, 1996; U.S. 5,516,448 Capeci et al., issued May 14, 1996; U.S. 5,489,392 Capeci et al., issued February 6, 1996; U.S. 5,486, 303 Capeci et al., issued January 23, 1996 all of which are incorporated herein by reference.
In addition to the above embodiments, the activated enzymes of the present invention can be formulated into any suitable detergent composition, non-limiting examples of which are described in U.S. 5,679, 630 Baeck et al., issued October 21, 1997; U.S. 5,565,145 Watson et al., issued October 15, 1996; U.S. 5,478,489 Fredj et al., issued December 26, 1995; U.S. 5,470,507 Fredj et al., issued November 28, 1995; U.S. 5,466, 802 Panandiker et al., issued November 14, 1995; U.S. 5,460,752 Fredj et al., issued October 24, 1995; U.S. 5,458,810 Fredj et al., issued October 17, 1995; U.S. 5,458,809 Fredj et al., issued October 17, 1995; U.S. 5, 288,431 Huber et al., issued February 22, 1994 all of which are incorporated herein by reference.
Having described the present invention in detail with reference to preferred embodiments, it will be clear to those skilled in the art that various changes and modifications may be made without departing from the scope of the invention, and the invention is not to be considered limited to what is described in the specification.
SEQUENCE LISTING <1lo> Mitra, Ashoke K.
<120> Method for Activating Enzymes and Cleaning Compositions Comprising Such Activated Enzymes <130> Method for Activating Enzymes <140> 60/137,285 <14l> 1999-06-03 <160> 18 <170> PatentIn Ver. 2.1 <210> 1 <21l> 21 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 1 attcatttqt ggacagtgga c 21 <210> 2 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 2 gttgatcgca cattgaacca 20 <210> 3 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 3 accccagccg accgattgtc 20 <210> 4 <21l> 20 <212> DNA <213> Unknown Organism <220> 81 <223> Description of Unknown organism: organism encoding a xyloglucanase enzyme <400> 4 cttccttacc tcaccatcat 20 <210> 5 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown organism: organism encoding a xyloglucanase enzyme <400> 5 ttaacatctt ttcaccatga 20 <210> 6 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: organism encoding a xyloglucanase enzyme <400> 6 agctttccct tctetccctt 20 <210> 7 <21l> 28 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown organism: organism encoding a xyloglucanase enzyme <400> 7 gccaccctgg cttccgctgc cagcctcc 28 <210> 8 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: organism encoding a xyloglucanase enzyme <400> 8 gacagtagca atccagcatt 20 <210> 9 <21l> 20 82 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 9 agcatcagcc gctttgtaca 20 <210> 10 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 10 ccatgaagtt caccgtattg 20 <210> 11 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 11 gcactgcttc tctcccaggt 20 <210> 12 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 12 gtgggcggcc cctcag9caa 20 <210> 13 <2li> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 13 acqctcctcc aattttctct 20 83 <210> 14 <21l> 19 <212> DNA <213> Unknown organism <220> <223> Description of Unknown Organism: organism encoding a xyloglucanase enzyme <400> 14 ggctggtagt aatgagtet 19 <210> 15 <21l> 20 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 15 ggC9cagagt ttggccaggc 20 <210> 16 <21l> 21 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown organism: Organism encoding a xyloglucanase enzyme <400> 16 caacatcccc ggt9ttctgg g 21 <210> 17 <21l> 347 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 17 aaagattcat ttgtggacag tggacgttga tc9cacattg aaccaacccc agccgaecga 60 ttgtccttcc ttacctcacc atcatttaac atcttttcac catgaagctt tcccttctct 120 cccttgecac cctggcttcc gct,gccagcc tccagcgccg cacacttctg cggtcagtgg 180 gataccgcca ccgccggtga cttcaccctg tacaacgacc tttggggcga gacggceggc 240 accggctccc agtgcactgg agtcgactcc tacagcgqcg acaccatcgc ttgtcacacc 300 aScaggtcct qgtcggagta gca9cagcgt, caagagctat gecaacg 347 <210> 18 <21l> 294 84 <212> DNA <213> Unknown Organism <220> <223> Description of Unknown Organism: Organism encoding a xyloglucanase enzyme <400> 18 cagcatctcc attgagtaat cacgttggtg ttcggtqgcc cgccgt9ttg C9t99cggag 60 gctqcc999a gacgggtggg gatggtggtq ggagagaatg tagggcgccq t9tttcagtc 120 cctaggcagg ataccggaaa accgtgtggt aggaggttta taggtttcca ggagacgctg 180 tataggggat aaatgagatt gaatggtggc cacactcaaa ccaaccaggt cctgtacata 240 caatgcatat accaattata cctaccaaaa aaaaaaaaaa aaaaaaaaaa aaaa 294

Claims (23)

  1. WHAT IS CLAIMED IS:
    I. A method for activating an enzyme comprising subjecting said enzyme to a source of microwave irradiation sufficient to activate said enzyme such that said irradiated enzyme exhibits an activity greater than said nonirradiated enzyme.
  2. 2. The method according to Claim I wherein said enzyme is a detergent enzyme.
  3. 3. The method according to Claim 2 wherein said detergent enzyme is selected from the group consisting of lipases, marmanases, cellulases, amylases, proteases, xyloglucanases and mixtures thereof.
  4. 4. The method according to Claim 3 wherein said detergent enzyme is selected from the group consisting of proteases, amylases and mixtures thereof.
  5. 5. The method according to Claim 4 wherein said detergent enzyme is a protease.
  6. 6. The method according to Claim 5 wherein said protease is obtained from Bacillus lentus.
  7. 7. The method according to Claim 6 wherein said protease is subtilisin 309.
  8. 8. The method according to Claim 5 wherein said protease is obtained from Bacillus amyloliquefaciens.
  9. 9. The method according to Claim 8 wherein said protease includes substitutions of amino acid residues at positions 76/103/104 of Bacillus amyloliquefaciens.
  10. 10. The method according to Claim 4 wherein said detergent enzyme is an amylase.
  11. 11. The method according to Claim 10 wherein said amylase is obtained from Bacillus licheniformis.
  12. 12. The method according to Claim 11 wherein said amylase includes a substitution of an amino acid residue at position 197 of Bacillus licheniformis or the homologous position variation of a similar parent amylase.
    86
  13. 13. The method according to Claim 12 wherein said amylase is an oxidative stability enhanced amylase, wherein said oxidative stability enhanced amylase is enhanced from substitution using threonine of the methionine residue located in position 197 of Bacillus licheniformis or the homologous position variation of a similar parent amylase.
  14. 14. The method according to Claim I wherein said source of microwave irradiation is a domestic microwave oven.
  15. 15. The method according to Claim I wherein said enzyme is exposed to microwaves at a frequency of from about I to about 20 GHz.
  16. 16. The method according to Claim 15 wherein said enzyme is exposed to microwaves at a frequency of from about 1 to about 10 GHz.
  17. 17. The method according to Claim I wherein said enzyme is exposed to microwaves at a power of from about 3 0 to about 1000 watts.
  18. 18. The method according to Claim 17 wherein said enzyme is exposed to microwaves at a power of from about 50 to about 500 watts.
  19. 19. The method according to Claim 18 wherein said enzyme is exposed to microwaves at a power of from about 50 to about 110 watts.
  20. 20. The method according to Claim I wherein said enzyme is irradiated for a total irradiation time of from about 15 seconds to about 20 minutes.
  21. 21. The method according to Claim 20 wherein said enzyme is irradiated for a total irradiation time of from about 30 seconds to about 5 minutes.
  22. 22. A detergent composition comprising:
    a) an activated enzyme according to Claim 1; and b) one or more cleaning adjunct materials.
    87
  23. 23. The detergent composition according to Claim 22 wherein said cleaning adjunct materials are selected from the group consisting of surfactants, builders, bleaches, bleach activators, bleach catalysts, non-activated enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, perservatives, anti-oxidants, anti-shrinkage agents, antiwrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tamish and/or anticorrosion agents, alkalinity sources, soiubilizing agents, carriers, processing aids, pigments and pH control agents
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WO2013027053A3 (en) * 2011-08-22 2013-05-10 Liverpool John Moores University Method for enhancement of enzyme activity
CN107279816A (en) * 2017-05-23 2017-10-24 辽宁阿里郎生物工程股份有限公司 A kind of preparation method of trepang compound soft capsule

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CN115067488B (en) * 2022-07-12 2023-05-23 湖北省农业科学院农产品加工与核农技术研究所 Efficient enzymolysis method for crayfish shells and preparation method for crayfish shell seasonings

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WO1993021344A1 (en) * 1992-04-16 1993-10-28 Pioneer Hi-Bred International, Inc. Microwave modification of biological macromolecules
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Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2013027053A3 (en) * 2011-08-22 2013-05-10 Liverpool John Moores University Method for enhancement of enzyme activity
GB2507711A (en) * 2011-08-22 2014-05-07 Univ Liverpool John Moores Method for enhancement of enzyme activity
GB2535920A (en) * 2011-08-22 2016-08-31 Univ Liverpool John Moores Method for enhancement of enzyme activity
GB2535920B (en) * 2011-08-22 2017-04-12 Univ Liverpool John Moores Method for enhancement of compound production by microbes
GB2507711B (en) * 2011-08-22 2017-04-12 Univ Liverpool John Moores Method for enhancement of enzyme activity
CN107279816A (en) * 2017-05-23 2017-10-24 辽宁阿里郎生物工程股份有限公司 A kind of preparation method of trepang compound soft capsule

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