EP0929636B1 - Flüssige reinigungsmittel, die proteolytisches enzym, peptidaldehyd und eine borsäurequelle enthalten - Google Patents

Flüssige reinigungsmittel, die proteolytisches enzym, peptidaldehyd und eine borsäurequelle enthalten Download PDF

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EP0929636B1
EP0929636B1 EP97941697A EP97941697A EP0929636B1 EP 0929636 B1 EP0929636 B1 EP 0929636B1 EP 97941697 A EP97941697 A EP 97941697A EP 97941697 A EP97941697 A EP 97941697A EP 0929636 B1 EP0929636 B1 EP 0929636B1
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ala
leu
group
gly
alkyl
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French (fr)
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EP0929636A1 (de
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John Mcmillan Mciver
Alan Carl Huber
Kirsten Louise Mckillop
Laurence Anthony Smith
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Procter and Gamble Co
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Procter and Gamble Co
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    • 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
    • C11D3/38663—Stabilised liquid enzyme compositions
    • 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
    • C11D3/38618—Protease or amylase in liquid compositions only

Definitions

  • This invention relates to liquid detergent compositions containing enzymes. More specifically, this invention pertains to liquid detergent compositions containing a detersive surfactant, a proteolytic enzyme, a peptide aldehyde, and boric acid. The combination of peptide aldehyde and boric acid act to provide improved protease inhibitor benefits.
  • protease-containing liquid aqueous detergents are well-known, especially in the context of laundry washing and care.
  • a commonly encountered problem in such protease-containing liquid aqueous detergents is the degradation phenomenon by the proteolytic enzyme of second enzymes in the composition, such as lipase, amylase and cellulase, or on the protease itself.
  • second enzymes such as lipase, amylase and cellulase
  • peptide aldehydes are rather expensive and create complexities for the formulators, especially for liquid detergents.
  • Other inhibitors such as calcium and boric acids are less expensive but do not stabilize enzymes as well as peptide aldehydes. It is thus an object of the present invention to provide a protease inhibitor system which is economical, effective and suitable for use in a liquid detergent composition.
  • the present invention proposes to use a combination of boric acid or a source thereof and peptide aldehydes as reversible protease inhibitors in aqueous liquid detergent compositions.
  • the presence of both boric acid and peptide aldehyde provides economical, improved stabilization of the protease.
  • This novel combination provides the formulator added flexibility in designing a stabilization system.
  • the levels of peptide aldehyde and boric acid can be adjusted to deliver the most cost effective formula and to minimize product stability problems that often arise from the presence of divalent ions in a liquid detergent matrix.
  • the present invention allows for the use of very low levels of peptide aldehydes in the liquid detergent compositions herein. This is particularly critical in the formulation of relatively inexpensive, concentrated liquid detergent compositions which are encompassed by the present invention.
  • Another advantage of the present invention is that even enzymes which are highly sensitive to proteolytic degradation can now be incorporated in liquid detergent compositions comprising a protease.
  • EP 293 881 discloses the use of peptide boronic acids as inhibitors of trypsin-like serine proteases.
  • EP 185 390 and US 4,399,065 disclose the use of certain peptide aldehydes derivatives for the inhibition of blood coagulation.
  • J 90029670 discloses the use of optically active alpha amino aldehydes for the inhibition of enzymes in general. See also “Inhibition of Thrombin and Trypsin by Tripeptide Aldehydes", Int. J. Peptide Protein Res. , Vol 12 (1978), pp.
  • the invention herein is a liquid detergent composition
  • a liquid detergent composition comprising:
  • the detergent compositions of this invention further comprise an effective amount of a source of calcium ions.
  • liquid detergent compositions herein comprise, by weight of composition:
  • the proteolytic enzyme useful herein is preferably a subtilisin-type protease and may be selected from the group consisting of Alcalase®, Subtilisin BPN', Protease A, Protease B, and mixtures thereof.
  • the boron composition comprises boric acid or a source of boric acid ion selected from the group consisting of boric oxide, borax, other alkali metal borates, substituted boric acids; the polyol is preferably a diol and is preferably selected from 1,2 propanediol.
  • the source of calcium ion for use herein is preferably selected from calcium formate, calcium chloride, calcium acetate, calcium sulfate, calcium xylene sulfonate, and mixtures thereof.
  • the liquid detergent compositions further comprise an effective amount of one or more of the following enzymes: lipase, amylase, cellulase, and mixtures thereof.
  • the second enzyme is lipase and is obtained by cloning the gene from Humicola Lanuginosa and expressing the gene in Aspergillus Oryzae .
  • Lipase is utilized in an amount of from about 10 to about 18000 lipase units per gram, preferably from about from about 60 to about 6000 units per gram.
  • the second enzyme is a cellulase derived from Humicola Insolens and is utilized in an amount of from about 0.0001% to about 0.1% by weight of the total composition of said cellulase.
  • compositions herein may contain further detersive adjuncts, including but not limited to, one or more of the following: suds boosters, builders, soil release polymers, polyacrylate polymers, dispersing agents, dye transfer inhibitors, dyes, perfumes, processing aids, brighteners, and mixtures thereof.
  • the present detergent compositions comprise an "effective amount” or a "stain removal-improving amount” of individual components defined herein.
  • An “effective amount” or “stain removal-improving amount” is any amount capable of measurably improving soil cleaning or stain removal from a substrate, i.e., soiled fabric or soiled dishware, when it is washed by the consumer. In general, this amount may vary quite widely.
  • the liquid aqueous detergent compositions according to the present invention comprise four essential ingredients: (A) a peptide aldehyde or a mixture thereof, (B) a proteolytic enzyme or a mixture thereof, (C) a detersive surfactant, and (D) a baron composition comprising a source of boric acid and a polyol.
  • compositions according to the present invention preferably further comprise (E) a detergent-compatible second enzyme or a mixture thereof, and may further comprise (F) other optional ingredients.
  • Peptide aldehydes - The detergent compositions according to the present invention comprise, as a first essential ingredient, a peptide aldehyde having the formula: Z-B-NH-CH(R)-C(O)H wherein B is a peptide chain comprising from 1 to 5 amino acid moieties; Z is an N-capping moiety selected from the group consisting of phosphoramidate [(R"O) 2 (O)P-], sulfenamide [(SR")-], sulfonamide [(R"(O) 2 S-], sulfonic acid [SO 3 H], phosphinamide [(R") 2 (O)P-], sulfamoyl derivative [R"O(O) 2 S-], thiourea [(R") 2 N(S)C-], thiocarbamate [R"O(S)C-], phosphonate [R"-P(O)OH], amidophosphate [R"O(OH)(O)P-],
  • R moieties are selected from the group consisting of methyl, isopropyl, sec-butyl, iso-butyl, -C 6 H 5 , -CH 2 -C 6 H 5 , and -CH 2 CH 2 -C 6 H 5 , which respectively may be derived from the amino acids Ala, Val, Ile, Leu, PGly (phenylglycine), Phe, and HPhe (homophenylalanine) by converting the carboxylic acid group to an aldehyde group.
  • Preferred B peptide chains are selected from the group consisting of peptide chains having the amino acid sequences according to the general formula: Z-A 5 -A 4 -A 3 -A 2 -A 1 -NH-CH(R)-C(O)H such that the following amino acids, when present, are :
  • aldehydes may be prepared from the corresponding amino acid whereby the C-terminal end of said amino acid is converted from a carboxylic group to an aldehyde group.
  • Such aldehydes may be prepared by known processes, for instance as described in US 5015627, EP 185 930, EP 583,534, and DE 32 00 812.
  • the peptide aldehydes according to the present invention bind to the proteolytic enzyme in the liquid detergent composition, thereby inhibiting said proteolytic enzyme. Upon dilution in water, the proteolytic activity is restored by dissociation of the proteolytic enzyme/peptide aldehyde complex.
  • N-terminal end of said protease inhibitors according to the present invention is protected by one of the N-capping moiety protecting groups selected from the group consisting of carbamates, ureas, sulfonamides, phosphonamides,thioureas, sulfenamides, sulfonic acids, phosphinamides, thiocarbamates, amidophosphates, and phosphoramidate.
  • the N-terminal end of said protease inhibitor is protected by a methyl, ethyl or benzyl carbamate [CH 3 O-(O)C-; CH 3 CH 2 O-(O)C-; or C 6 H 5 CH 2 O-(O)C-], methyl, ethyl or benzyl urea [CH 3 NH-(O)C-; CH 3 CH 2 NH-(O)C-; or C 6 H 5 CH 2 NH-(O)C-], methyl, ethyl or benzyl sulfonamide [CH 3 SO 2 -; CH 3 CH 2 SO 2 -; or C 6 H 5 CH 2 SO 2 -], and methyl, ethyl or benzyl amidophosphate [CH 3 O(OH)(O)P-; CH 3 CH 2 O(OH)(O)P-; or C 6 H 5 CH 2 O(OH)(O)P-] groups.
  • N-capping groups can be found in the following references: Protective Groups in Organic Chemistry , Greene, T., Wuts, P., John Wiley & Sons, New York, 1991, pp 309-405; March, J, Advanced Organic Chemistry , Wiley Interscience, 1985, pp. 445, 469, Carey, F. Sundberg, R., Advanced Organic Chemistry , Part B, Plenum Press, New York, 1990, pp. 686-89; Atherton, E., Sheppard, R., Solid Phase Peptide Synthesis , Pierce Chemical, 1989, pp. 3-4; Grant, G., Synthetic Peptides , W. H. Freeman & Co. 1992, pp.
  • Examples of peptide aldehydes for use herein are: CH 3 SO 2 Phe-Gly-Ala-Leu-H, CH 3 SO 2 Val-Ala-Leu-H, C 6 H 5 CH 2 O(OH)(O)P-Val-Ala-Leu-H, CH 3 CH 2 SO 2 -Phe-Gly-Ala-Leu-H, C 6 H 5 CH 2 SO 2 -Val-Ala-Leu-H, C 6 H 5 CH 2 O(OH)(O)P-Leu-Ala-Leu-H, C 6 H 5 CH 2 O(OH)(O)P-Phe-Ala-Leu-H, and CH 3 O(OH)(O)P-Leu-Gly-Ala-Leu-H.
  • Moc-Leu-OH-L-Leucine (5.0 g, 38.2 mmol) is dissolved in 38 ml IN NaOH and cooled to 0°C.
  • Methyl chloroformate (3.1 ml, 40.0 mmol) is added dropwise while in a separate addition funnel IN NaOH is added as to maintain pH at 9.0-9.5.
  • Moc-Leu-LeuH-A solution containing 4.4 g (10.41 mmol) Dess-Martin periodinane suspended in 100 ml CH 2 Cl 2 is prepared and stirred for 10 minutes.
  • 1.0 g (3.47 mmol) Moc-Leu-Leucinol is added and the solution stirred 2 h at room temperature followed by pouring into 100 ml of saturated NaHCO 3 containing 18 g (72.87 mmol) Na 2 S 2 O 3 .
  • This solution is stirred 10 minutes and then extracted with EtOAc (2X, 125ml), dried (MgSO 4 ) and the solvent evaporated. Chromatography on silica affords 0.550 g of pure product.
  • Additional peptide aldehydes are synthesized according to the following procedures. Some of the intermediates are purchased from suppliers and in these instances it is noted within the procedure. Dess-Martin periodinane is synthesized according to the procedure of Martin, J.Org. Chem., 1983 , 48, 4155.
  • proteolytic Enzyme Another essential ingredient in the present liquid detergent compositions is active proteolytic enzyme. Mixtures of proteolytic enzyme are also included.
  • the proteolytic enzyme can be of animal, vegetable or microorganism (preferred) origin.
  • the proteases for use in the detergent compositions herein include (but are not limited to) trypsin, subtilisin, chymotrypsin and elastase-type proteases.
  • Preferred for use herein are subtilisin-type proteolytic enzymes.
  • Particularly preferred is bacterial serine proteolytic enzyme obtained from Bacillus subtilis and/or Bacillus licheniformis.
  • Protease enzymes are usually present in such liquid detergent compositions at levels sufficient to provide from 0.005 to 0.1 Anson units (AU) of activity per gram of composition.
  • AU Anson units
  • Suitable proteolytic enzymes include Novo Industri A/S Alcalase® (preferred), Esperase® , Savinase® (Copenhagen, Denmark), Gist-brocades' Maxatase®, Maxacal® and Maxapem 15® (protein engineered Maxacal®) (Delft, Netherlands), and subtilisin BPN and BPN'(preferred), which are commercially available.
  • Preferred proteolytic enzymes are also modified bacterial serine proteases, such as those made by Genencor International, Inc.(San Francisco, California) which are described in European Patent 251,446, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and U.S.
  • Protease A a modified bacterial serine proteolytic enzyme
  • BPN' modified bacterial serine proteolytic enzyme
  • Preferred proteolytic enzymes are selected from the group consisting of Alcalase® (Novo Industri A/S), BPN', Protease A and Protease B (Genencor), and mixtures thereof. Protease B is most preferred.
  • 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.
  • proteases are also described in PCT publications: WO 95/30010 published Novenber 9, 1995 by The Procter & Gamble Company; WO 95/30011 published Novenber 9, 1995 by The Procter & Gamble Company; WO 95/29979 published Novenber 9, 1995 by The Procter & Gamble Company.
  • any water-soluble calcium salt can be used as a source of calcium ions, including calcium acetate, calcium formate, calcium xylene sulfonate, and calcium propionate.
  • Divalent ions such as zinc and magnesium ions, can replace the calcium ion completely or in part.
  • the source of calcium ions can be partially or completely substituted with a source of another divalent ion.
  • the calcium useful herein is enzyme-accessible. Therefore, the claimed compositions are substantially free of sequestrants, for example, polyacids capable of forming calcium complexes which are soluble in the composition. However, minor amounts of sequestrants such as polyacids or mixtures of polyacids can be used.
  • the enzyme-accessible calcium is defined as the amount of calcium-ions effectively available to the enzyme component. From a practical standpoint the enzyme-accessible calcium is therefore the soluble calcium in the composition in the absence of any storage sequestrants, e.g., having an equilibrium constant of complexation with calcium equal to or greater than 1.5 at 20°C.
  • compositions herein contain from about 0.25% to about 10%, preferably from about 0.5% to about 5%, more preferably from about 0.75% to about 3%, by weight of boric acid or a compound capable of forming boric acid in the composition (calculated on the basis of the boric acid).
  • Boric acid is preferred, although other compounds such as boric oxide, borax and other alkali metal borates (e.g., sodium ortho-, meta-, pyroborate, and sodium pentaborate) are suitable.
  • Substituted boric acids e.g., phenylboronic acid, butane boronic acid, and p-bromo phenylboronic acid
  • compositions of the present invention also contain polyols, especially diols, containing only carbon, hydrogen and oxygen atoms. They preferably contain from about 2 to about 6 hydroxy groups. Examples include propylene glycol (especially 1,2 propanediol, which is preferred), ethylene glycol, glycerol, sorbitol, mannitol, glucose, and mixtures thereof
  • the polyol generally represents from about 1% to about 15%, preferably from about 1.5% to about 10%, more preferably from about 2% to about 7%, by weight of the composition.
  • Detersive Surfactant An effective amount, typically from about 1 to 95, preferably about 8 to 70, weight %, of detersive surfactant is yet another essential ingredient in the present invention.
  • the detersive surfactant can be selected from the group consisting of anionics, nonionics, cationics, ampholytics, zwitterionics, and mixtures thereof.
  • the present detergent compositions can be formulated to be used in the context of laundry cleaning or in other different cleaning applications, particularly including dishwashing. The particular surfactants used can therefore vary widely depending upon the particular end-use envisioned.
  • compositions containing ingredients that are harsh to enzymes such as certain detergency builders and surfactants.
  • surfactants include (but are not limited to) anionic surfactants such as alkyl ether sulfate linear alkyl benzene sulfonate, alkyl sulfate, etc. Suitable surfactants are described below.
  • Anionic Surfactants One type of anionic surfactant which can be utilized encompasses alkyl ester sulfonates. These are desirable because they can be made with renewable, non-petroleum resources. Preparation of the alkyl ester sulfonate surfactant component can be effected according to known methods disclosed in the technical literature. For instance, linear esters of C 8 -C 20 carboxylic acids can be sulfonated with gaseous SO 3 according to "The Journal of the American Oil Chemists Society," 52 (1975), pp. 323-329. Suitable starting materials would include natural fatty substances as derived from tallow, palm, and coconut oils, etc.
  • the preferred alkyl ester sulfonate surfactant comprises alkyl ester sulfonate surfactants of the structural formula: wherein R 3 is a C 8 -C 20 hydrocarbyl, preferably an alkyl, or combination thereof, R 4 is a C 1 -C 6 hydrocarbyl, preferably an alkyl, or combination thereof, and M is a soluble salt-forming cation.
  • Suitable salts include metal salts such as sodium, potassium, and lithium salts, and substituted or unsubstituted ammonium salts, such as methyl-, dimethyl, -trimethyl, and quaternary ammonium cations, e.g.
  • R 3 is C 10 -C 16 alkyl
  • R 4 is methyl, ethyl or isopropyl.
  • methyl ester sulfonates wherein R 3 is C 14 -C 16 alkyl.
  • Alkyl sulfate surfactants are another type of anionic surfactant of importance for use herein.
  • dissolution of alkyl sulfates can be obtained, as well as improved formulability in liquid detergent formulations are water soluble salts or acids of the formula ROSO 3 M wherein R preferably is a C 10 -C 24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C 10 -C 20 alkyl component, more preferably a C 12 -C 18 alkyl or hydroxyalkyl, and M is H or a cation, e.g., an alkali metal cation (e.g., sodium, potassium, lithium), substituted or unsubstituted ammonium cations such as methyl-, dimethyl-, and trimethyl ammonium and quatern
  • Alkyl alkoxylated sulfate surfactants are another category of useful anionic surfactant. These surfactants are water soluble salts or acids typically of the formula RO(A) m SO 3 M wherein R is an unsubstituted C 10 -C 24 alkyl or hydroxyalkyl group having a C 10 -C 24 alkyl component, preferably a C 12 -C 20 alkyl or hydroxyalkyl, more preferably C 12 -C 18 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, and M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium cation.
  • R is an unsubstituted C 10 -C 24 alkyl or hydroxyalkyl group having
  • Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein.
  • Specific examples of substituted ammonium cations include methyl-, dimethyl-, trimethyl-ammonium and quaternary ammonium cations, such as tetramethyl-ammonium, dimethyl piperidinium and cations derived from alkanolamines, e.g. monoethanolamine, diethanolamine, and triethanolamine, and mixtures thereof.
  • Exemplary surfactants are C 12 -C 18 alkyl polyethoxylate (1.0) sulfate, C 12 -C 18 alkyl polyethoxylate (2.25) sulfate, C 12 -C 18 alkyl polyethoxylate (3.0) sulfate, and C 12 -C 18 alkyl polyethoxylate (4.0) sulfate wherein M is conveniently selected from sodium and potassium.
  • Anionic Surfactants can also be included in the compositions hereof. These can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di- and triethanolamine salts) of soap, C 9 -C 20 linear alkylbenzenesulphonates, C 8 -C 22 primary or secondary alkanesulphonates, C 8 -C 24 olefinsulphonates, sulphonated polycarboxylic acids prepared by sulphonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No.
  • salts including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di- and triethanolamine salts
  • C 9 -C 20 linear alkylbenzenesulphonates C 8 -C 22 primary or secondary alkanesulphonates
  • C 8 -C 24 olefinsulphonates C 8 -C
  • alkyl glycerol sulfonates alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isothionates such as the acyl isothionates, N-acyl taurates, fatty acid amides of methyl tauride, alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinate (especially saturated and unsaturated C 12 -C 18 monoesters) diesters of sulfosuccinate (especially saturated and unsaturated C 6 -C 14 diesters), N-acyl sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of alkylpolygluco
  • Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil. Further examples are given in "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perry and Berch). A variety of such surfactants are also generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975 to Laughlin, et al. at Column 23, line 58 through Column 29, line 23 (herein incorporated by reference).
  • Nonionic Detergent Surfactants - Suitable nonionic detergent surfactants are generally disclosed in U.S. Patent 3,929,678, Laughlin et al., issued December 30, 1975, at column 13, line 14 through column 16, line 6, incorporated herein by reference. Exemplary, non-limiting classes of useful nonionic surfactants are listed below.
  • the polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are preferred. These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 12 carbon atoms in either a straight chain or branched chain configuration with the alkylene oxide.
  • the ethylene oxide is present in an amount equal to from about 5 to about 25 moles of ethylene oxide per mole of alkyl phenol.
  • nonionic surfactants of this type include Igepal® CO-630, marketed by the GAF Corporation; and Triton® X-45, X-114, X-100, and X-102, all marketed by the Rohm & Haas Company. These compounds are commonly referred to as alkyl phenol alkoxylates, (e.g., alkyl phenol ethoxylates).
  • the condensation products of aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Particularly preferred are the condensation products of alcohols having an alkyl group containing from about 10 to about 20 carbon atoms with from about 2 to about 18 moles of ethylene oxide per mole of alcohol.
  • nonionic surfactants of this type include Tergitol® 15-S-9 (the condensation product of C 11 -C 15 linear secondary alcohol with 9 moles ethylene oxide), Tergitol® 24-L-6 NMW (the condensation product of C 12 -C 14 primary alcohol with 6 moles ethylene oxide with a narrow molecular weight distribution), both marketed by Union Carbide Corporation; Neodol® 45-9 (the condensation product of C 14 -C 15 linear alcohol with 9 moles of ethylene oxide), Neodol® 23-6.5 (the condensation product of C 12 -C 13 linear alcohol with 6.5 moles of ethylene oxide), Neodol® 45-7 (the condensation product of C 14 -C 15 linear alcohol with 7 moles of ethylene oxide), Neodol® 45-4 (the condensation product of C 14 -C 15 linear alcohol with 4 moles of ethylene oxide), marketed by Shell Chemical Company, and Kyro® EOB (the condensation product of C 13 -C 15 alcohol with 9 moles ethylene oxide), marketed by The Procter
  • the hydrophobic portion of these compounds preferably has a molecular weight of from about 1500 to about 1800 and exhibits water insolubility.
  • the addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide.
  • Examples of compounds of this type include certain of the commercially-available Pluronic® surfactants, marketed by BASF.
  • the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine consist of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000.
  • This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000.
  • this type of nonionic surfactant include certain of the commercially available Tetronic® compounds, marketed by BASF.
  • Semi-polar nonionic surfactants are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.
  • Semi-polar nonionic detergent surfactants include the amine oxide surfactants having the formula wherein R 3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereof containing from about 8 to about 22 carbon atoms; R 4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is from 0 to about 3; and each R 5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups.
  • the R 5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure.
  • amine oxide surfactants in particular include C 10 -C 18 alkyl dimethyl amine oxides and C 8 -C 12 alkoxy ethyl dihydroxy ethyl amine oxides.
  • Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties.
  • the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside.
  • the intersaccharide bonds can be, e.g., between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.
  • a polyalkylene-oxide chain joining the hydrophobic moiety and the polysaccharide moiety.
  • the preferred alkyleneoxide is ethylene oxide.
  • Typical hydrophobic groups include alkyl groups, either saturated or unsaturated, branched or unbranched containing from about 8 to about 18, preferably from about 10 to about 16, carbon atoms.
  • the alkyl group is a straight chain saturated alkyl group.
  • the alkyl group can contain up to about 3 hydroxy groups and/or the polyalkyleneoxide chain can contain up to about 10, preferably less than 5, alkyleneoxide moieties.
  • Suitable alkyl polysaccharides are octyl, nonyl, decyl, undecyldodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, and octadecyl, di-, tri-, tetra-, penta-, and hexaglucosides, galactosides, lactosides, glucoses, fructosides, fructoses and/or galactoses.
  • Suitable mixtures include coconut alkyl, di-, tri-, tetra-, and pentaglucosides and tallow alkyl tetra-, penta-, and hexa-glucosides.
  • the preferred alkylpolyglycosides have the formula R 2 O(C n H 2n O) t (glycosyl) x wherein R 2 is selected from the group consisting of alkyl, alkyl-phenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7.
  • the glycosyl is preferably derived from glucose.
  • the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1-position).
  • the additional glycosyl units can then be attached between their 1-position and the preceding glycosyl units 2-, 3-, 4- and/or 6-position, preferably predominantly the 2-position.
  • Fatty acid amide surfactants having the formula: wherein R 6 is an alkyl group containing from about 7 to about 21 (preferably from about 9 to about 17) carbon atoms and each R 7 is selected from the group consisting of hydrogen, C 1 -C 4 alkyl, C 1 -C 4 hydroxyalkyl, and -(C 2 H 4 O) x H where x varies from about 1 to about 3.
  • Preferred amides are C 8 -C 20 ammonia amides, monoethanolamides, diethanolamides, and isopropanolamides.
  • Cationic Surfactants - Cationic detersive surfactants can also be included in detergent compositions of the present invention.
  • Cationic surfactants include the ammonium surfactants such as alkyldimethylammonium halogenides, and those surfactants having the formula: [R 2 (OR 3 ) y ][R 4 (OR 3 ) y ] 2 R 5 N + X - wherein R 2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R 3 is selected from the group consisting of -CH 2 CH 2 - , -CH 2 CH(CH 3 )-, -CH 2 CH(CH 2 OH)-, -CH 2 CH 2 CH 2 -, and mixtures thereof; each R 4 is selected from the group consisting of C 1 -C 4 alkyl, C 1 -C 4 hydroxyalkyl, benzyl, ring structures formed by joining the two R 4 groups, -
  • Surfactants - Ampholytic surfactants can be incorporated into the detergent compositions hereof. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight chain or branched.
  • One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water-solubilizing group, e.g., carboxy, sulfonate, sulfate. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, lines 18-35 for examples of ampholytic surfactants.
  • Zwitterionic surfactants can also be incorporated into the detergent compositions hereof. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, line 38 through column 22, line 48 for examples of zwitterionic surfactants. Ampholytic and zwitterionic surfactants are generally used in combination with one or more anionic and/or nonionic surfactants.
  • the liquid detergent compositions hereof may also contain an enzyme-enhancing amount of polyhydroxy fatty acid amide surfactant.
  • enzyme-enhancing is meant that the formulator of the composition can select an amount of polyhydroxy fatty acid amide to be incorporated into the compositions that will improve enzyme cleaning performance of the detergent composition. In general, for conventional levels of enzyme, the incorporation of about 1%, by weight, polyhydroxy fatty acid amide will enhance enzyme performance.
  • the detergent compositions herein will typically comprise about 1% weight basis, polyhydroxy fatty acid amide surfactant, preferably from about 3% to about 30%, of the polyhydroxy fatty acid amide.
  • the polyhydroxy fatty acid amide surfactant component comprises compounds of the structural formula: wherein: R 1 is H, C 1 -C 4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl, or a mixture thereof, preferably C 1 -C 4 alkyl, more preferably C 1 or C 2 alkyl, most preferably C 1 alkyl (i.e., methyl); and R 2 is a C 5 -C 31 hydrocarbyl, preferably straight chain C 7 -C 19 alkyl or alkenyl, more preferably straight chain C 9 -C 17 alkyl or alkenyl, most preferably straight chain C 11 -C 15 alkyl or alkenyl, or mixtures thereof; and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3
  • Z preferably will be derived from a reducing sugar in a reductive amination reaction; more preferably Z will be a glycityl.
  • Suitable reducing sugars include glucose, fructose, maltose, lactose, galactose, mannose, and xylose.
  • high dextrose corn syrup, high fructose corn syrup, and high maltose corn syrup can be utilized as well as the individual sugars listed above. These corn syrups may yield a mix of sugar components for Z. It should be understood that it is by no means intended to exclude other suitable raw materials.
  • Z preferably will be selected from the group consisting of -CH 2 -(CHOH) n -CH 2 OH, -CH(CH 2 OH)-(CHOH) n-1 -CH 2 OH, -CH 2 -(CHOH) 2 (CHOR')(CHOH)-CH 2 OH, and alkoxylated derivatives thereof, where n is an integer from 3 to 5, inclusive, and R' is H or a cyclic or aliphatic monosaccharide. Most preferred are glycityls wherein n is 4, particularly -CH 2 -(CHOH) 4 -CH 2 OH.
  • R' can be, for example, N-methyl, N-ethyl, N-propyl, N-isopropyl, N-butyl, N-2-hydroxy ethyl, or N-2-hydroxy propyl.
  • R 2 -CO-N ⁇ can be, for example, cocamide, stearamide, oleamide, lauramide, myristamide, capricamide, palmitamide, tallowamide, etc.
  • Z can be 1-deoxyglucityl, 2-deoxyfructityl, 1-deoxymaltityl, 1-deoxylactityl, 1-deoxygalactityl, 1-deoxymannityl, 1-deoxymaltotriotityl, etc.
  • polyhydroxy fatty acid amides are known in the art. In general, they can be made by reacting an alkyl amine with a reducing sugar in a reductive amination reaction to form a corresponding N-alkyl polyhydroxyamine, and then reacting the N-alkyl polyhydroxyamine with a fatty aliphatic ester or triglyceride in a condensation/amidation step to form the N-alkyl, N-polyhydroxy fatty acid amide product.
  • Processes for making compositions containing polyhydroxy fatty acid amides are disclosed, for example, in G.B. Patent Specification 809,060, published February 18, 1959, by Thomas Hedley & Co., Ltd., U.S.
  • Second Enzyme - Preferred compositions herein further comprise a performance-enhancing amount of a detergent-compatible second enzyme.
  • detergent-compatible is meant compatibility with the other ingredients of a liquid detergent composition, such as detersive surfactant and detergency builder.
  • second enzymes are preferably selected from the group consisting of lipase, amylase, cellulase, and mixtures thereof.
  • second enzyme excludes the proteolytic enzymes discussed above, so each composition which has a second enzyme contains at least two kinds of enzyme, including at least one proteolytic enzyme. The amount of second enzyme used in the composition varies according to the type of enzyme.
  • weight % of these second enzymes are preferably used.
  • Mixtures of the same class of enzymes (e.g. lipase) or two or more classes (e.g. cellulase and lipase) may be used.
  • Purified or non-purified forms of the enzyme may be used.
  • Any lipolytic enzyme suitable for use in a liquid detergent composition can be used in these compositions.
  • Suitable lipase enzymes for use herein include those of bacterial and fungal origin.
  • Suitable bacterial lipases include those produced by microorganisms of the Pseudomonas groups, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034, incorporated herein by reference. Suitable lipases include those which show a positive immunological cross-reaction with the antibody of the lipase produced by the microorganism Pseudomonas fluorescens IAM 1057. This lipase and a method for its purification have been described in Japanese Patent Application 53-20487, laid open on February 24, 1978. This lipase is available from Amano Pharmaceutical Co.
  • Lipase P Lipase P
  • Amano-P Lipase P
  • Such lipases should show a positive immunological cross-reaction with the Amano-P antibody, using the standard and well-known immunodiffusion procedure according to Ouchterlony (Acta. Med. Scan., 133, pages 76-79 (1950)).
  • Ouchterlony Acta. Med. Scan., 133, pages 76-79 (1950)
  • These lipases, and a method for their immunological cross-reaction with Amano-P are also described in U.S. Patent 4,707,291, Thom et al., issued November 17, 1987, incorporated herein by reference.
  • Typical examples thereof are the Amano-P lipase, the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade name Amano-B), lipase ex Pseudomonas nitroreducens var. lipolyticum FERM P 1338 (available under the trade name Amano-CES), lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var. lipolyticum NRRLB 3673, commercially available from Toyo Jozo Co., Tagata, Japan; and further Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli .
  • Amano-P lipase the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade name Amano-B),
  • Suitable fungal lipases include those producible by Humicola lanuginosa and Thermomyces lanuginosus . Most preferred is lipase obtained by cloning the gene from Humicola lanuginosa and expressing the gene in Aspergillus oryzae as described in European Patent Application 0 258 068 (Novo Industri A/S), commercially available from Novo Nordisk A/S under the trade name Lipolase®.
  • lipase units per gram (LU/g) of lipase can be used in these compositions.
  • a lipase unit is that amount of lipase which produces 1 mmol of titratable fatty acid per minute in a pH stat, where pH is 9.0, temperature is 30°C, substrate is an emulsion of 3.3wt % of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca ++ and 20 mmol/l NaCl in 5 mmol/l Tris-buffer.
  • Suitable cellulase enzymes for use herein include those from bacterial and fungal origins. Preferably, they will have a pH optimum of between 5 and 9.5. From about 0.0001 to 0.1 weight % cellulase can be used.
  • Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgaard et al., issued March 6, 1984, incorporated herein by reference, which discloses fungal cellulase produced from Humicola insolens. Suitable cellulases are also disclosed in GB-A-2.075.028, GB-A-2.095.275 and DE-OS-2.247.832.
  • cellulases examples include cellulases produced by a strain of Humicola insolens (Humicola grisea var. thermoidea), particularly the Humicola strain DSM 1800, and cellulases produced by a fungus of Bacillus N or a cellulase 212-producing fungus belonging to the genus Aeromonas, and cellulase extracted from the hepatopancreas of a marine mollusc (Dolabella Auricula Solander).
  • Amylases include, for example, amylases obtained from a special strain of B.licheniformis , described in more detail in British Patent Specification No. 1,296,839 (Novo).
  • Amylolytic proteins include, for example, Rapidase R , International Bio-Synthetics, Inc. and Termamyl R Novo Industries.
  • amylase From about 0.0001% to 0.55, preferably 0.0005 to 0.1, wt. % amylase can be used.
  • Optional Ingredients - Detergent builders can optionally be included in the compositions herein. From 0 to about 50 weight % detergency builder can be used herein. Inorganic as well as organic builders can be used. When present, the compositions will typically comprise at least about 1% builder. Liquid formulations preferably comprise from about 3% to 30%, more preferably about 5 to 20%, by weight, of detergent builder.
  • Inorganic 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 aluminosilicates.
  • Borate builders, as well as builders containing borate-forming materials that can produce borate under detergent storage or wash conditions hereinafter, collectively “borate builders"
  • non-borate builders are used in the compositions of the invention intended for use at wash conditions less than about 50°C, especially less than about 40°C.
  • silicate builders are the alkali metal silicates, particularly those having a SiO 2 :Na 2 O ratio in the range 1.6:1 to 3.2:1 and layered silicates, such as the layered sodium silicates described in U.S. Patent 4,664,839, issued May 12, 1987 to H. P. Rieck, incorporated herein by reference.
  • layered silicates such as the layered sodium silicates described in U.S. Patent 4,664,839, issued May 12, 1987 to H. P. Rieck, incorporated herein by reference.
  • other silicates may also be useful such as for example magnesium silicate, which can serve as a crispening agent in granular formulations, as a stabilizing agent for oxygen bleaches, and as a component of suds control systems.
  • carbonate builders are the alkaline earth and alkali metal carbonates, including sodium carbonate and sesquicarbonate and mixtures thereof with ultra-fine calcium carbonate as disclosed in German Patent Application No. 2,321,001 published on November 15, 1973, the disclosure of which is incorporated herein by reference.
  • 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: M z (zAlO 2 ⁇ ySiO 2 ) wherein M is sodium, potassium, ammonium or substituted ammonium, z is from about 0.5 to about 2; and y is 1; this material having a magnesium ion exchange capacity of at least about 50 milligram equivalents of CaCO 3 hardness per gram of anhydrous aluminosilicate.
  • Preferred alumino-silicates are zeolite builders which have the formula: Na z [(AlO 2 ) z (SiO 2 ) y ] ⁇ xH 2 O wherein z and y are integers of at least 6, the molar ratio of z to y is in the range from 1.0 to about 0.5, and x is an integer from about 15 to about 264.
  • aluminosilicate ion exchange materials are commercially available. These aluminosilicates can be crystalline or amorphous in structure and can be naturally-occurring aluminosilicates or synthetically derived. A method for producing aluminosilicate ion exchange materials is disclosed in U.S. Patent 3,985,669, Krummel, et al., issued October 12, 1976, incorporated herein by reference. Preferred synthetic crystalline aluminosilicate ion exchange materials useful herein are available under the designations Zeolite A, Zeolite P (B), and Zeolite X.
  • the crystalline aluminosilicate ion exchange material has the formula: Na 12 [(AlO 2 ) 12 (SiO 2 ) 12 ] ⁇ xH 2 O wherein x is from about 20 to about 30, especially about 27.
  • This material is known as Zeolite A.
  • the aluminosilicate has a particle size of about 0.1-10 microns in diameter.
  • polyphosphates are the alkali metal tripolyphosphates, sodium, potassium and ammonium pyrophosphate, sodium and potassium and ammonium pyrophosphate, sodium and potassium orthophosphate, sodium polymeta phosphate in which the degree of polymerization ranges from about 6 to about 21, and salts of phytic acid.
  • phosphonate builder salts are the water-soluble salts of ethane 1-hydroxy-1, 1-diphosphonate particularly the sodium and potassium salts, the water-soluble salts of methylene diphosphonic acid e.g. the trisodium and tripotassium salts and the water-soluble salts of substituted methylene diphosphonic acids, such as the trisodium and tripotassium ethylidene, isopyropylidene benzylmethylidene and halo methylidene phosphonates.
  • Phosphonate builder salts of the aforementioned types are disclosed in U.S. Patent Nos.
  • Organic detergent builders preferred for the purposes of the present invention include a wide variety of polycarboxylate compounds.
  • 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.
  • alkali metals such as sodium, potassium, and lithium, or alkanolammonium salts are preferred.
  • polycarboxylate builders include a variety of categories of useful materials.
  • One important category of polycarboxylate builders encompasses the ether polycarboxylates.
  • a number of ether polycarboxylates have been disclosed for use as detergent builders.
  • Examples of useful ether polycarboxylates include oxydisuccinate, as disclosed in Berg, U.S. Patent 3,128,287, issued April 7, 1964, and Lamberti et al., U.S. Patent 3,635,830, issued January 18, 1972, both of which are incorporated herein by reference.
  • a specific type of ether polycarboxylates useful as builders in the present invention also include those having the general formula: CH(A)(COOX)-CH(COOX)-O-CH(COOX)-CH(COOX)(B) wherein A is H or OH; B is H or -O-CH(COOX)-CH 2 (COOX); and X is H or a salt-forming cation.
  • a and B are both H, then the compound is oxydissuccinic acid and its water-soluble salts. If A is OH and B is H, then the compound is tartrate monosuccinic acid (TMS) and its water-soluble salts.
  • TDS tartrate disuccinic acid
  • Suitable ether polycarboxylates also include cyclic compounds, particularly alicyclic compounds, such as those described in U.S. Patents 3,923,679; 3,835,163; 4,158,635; 4,120,874 and 4,102,903, all of which are incorporated herein by reference.
  • ether hydroxypolycarboxylates represented by the structure: HO-[C(R)(COOM)-C(R)(COOM)-O] n -H wherein M is hydrogen or a cation wherein the resultant salt is water-soluble, preferably an alkali metal, ammonium or substituted ammonium cation, n is from about 2 to about 15 (preferably n is from about 2 to about 10, more preferably n averages from about 2 to about 4) and each R is the same or different and selected from hydrogen, C 1-4 alkyl or C 1-4 substituted alkyl (preferably R is hydrogen).
  • Still other ether polycarboxylates include copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1, 3, 5-trihydroxy benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid.
  • Organic polycarboxylate builders also include the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids. Examples include the sodium, potassium, lithium, ammonium and substituted ammonium salts of ethylenediamine tetraacetic acid, and nitrilotriacetic acid.
  • polycarboxylates such as mellitic acid, succinic acid, oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid, and 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, but can also be used in granular compositions.
  • carboxylate builders include the carboxylated carbohydrates disclosed in U.S. Patent 3,723,322, Diehl, issued March 28, 1973, incorporated herein by reference.
  • Also suitable in the detergent compositions of the present invention are the 3,3-dicarboxy-4-oxa-1,6-hexanedioates and the related compounds disclosed in U.S. Patent 4,566,984, Bush, issued January 28, 1986, incorporated herein by reference.
  • Useful succinic acid builders include the C 5 -C 20 alkyl succinic acids and salts thereof.
  • a particularly preferred compound of this type is dodecenylsuccinic acid.
  • Alkyl succinic acids typically are of the general formula R-CH(COOH)CH 2 (COOH) i.e., derivatives of succinic acid, wherein R is hydrocarbon, e.g., C 10 -C 20 alkyl or alkenyl, preferably C 12 -C 16 or wherein R may be substituted with hydroxyl, sulfo, sulfoxy or sulfone substituents, all as described in the above-mentioned patents.
  • R is hydrocarbon, e.g., C 10 -C 20 alkyl or alkenyl, preferably C 12 -C 16 or wherein R may be substituted with hydroxyl, sulfo, sulfoxy or sulfone substituents, all as described in the above-mentioned patents.
  • the succinate builders are preferably used in the form of their water-soluble salts, including the sodium, potassium, ammonium and alkanolammonium salts.
  • succinate builders include: laurylsuccinate, myristylsuccinate, palmitylsuccinate, 2-dodecenylsuccinate (preferred), 2-pentadecenylsuccinate, and the like. Laurylsuccinates are the preferred builders of this group, and are described in European Patent Application 86200690.5/0,200,263, published November 5, 1986.
  • useful builders also include sodium and potassium carboxymethyloxymalonate, carboxymethyloxysuccinate, cis-cyclo-hexane-hexacarboxylate, cis-cyclopentane-tetracarboxylate, water-soluble polyacrylates (these polyacrylates having molecular weights to above about 2,000 can also be effectively utilized as dispersants), and the copolymers of maleic anhydride with vinyl methyl ether or ethylene.
  • polyacetal carboxylates are the polyacetal carboxylates disclosed in U.S. Patent 4,144,226, Crutchfield et al., issued March 13, 1979, incorporated herein by reference. These polyacetal carboxylates can be prepared by bringing together, under polymerization conditions, an ester of glyoxylic acid and a polymerization initiator. The resulting polyacetal carboxylate ester is then attached to chemically stable end groups to stabilize the polyacetal carboxylate against rapid depolymerization in alkaline solution, converted to the corresponding salt, and added to a surfactant.
  • Polycarboxylate builders are also disclosed in U.S. Patent 3,308,067, Diehl, issued March 7, 1967, incorporated herein by reference. Such materials include the water-soluble salts of homo- and copolymers of aliphatic carboxylic acids such as maleic acid, itaconic acid and methylenemalonic acid.
  • organic builders known in the art can also be used.
  • monocarboxylic acids, and soluble salts thereof, having long chain hydrocarbyls can be utilized. These would include materials generally referred to as "soaps.” Chain lengths of C 10 -C 20 are typically utilized.
  • the hydrocarbyls can be saturated or unsaturated.
  • soil release agents include soil release agents, chelating agents, clay soil removal/anti redeposition agents, polymeric dispersing agents, bleaches, brighteners, suds suppresors, solvents and aesthetic agents.
  • the detergent composition herein can be formulated as a variety of compositions, for instance as laundry detergents as well as hard surface cleaners or dishwashing compositions.
  • compositions according to the present invention are further illustrated by the following examples.
  • compositions are made by combining the listed ingredients in the listed proportions.
  • one or more of the following peptide aldehydes are used:

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Claims (10)

  1. Flüssige Reinigungszusammensetzung, umfassend:
    (a) 1 bis 95 Gew.-% der Zusammensetzung eines Waschtensids;
    (b) ein aktives proteolytisches Enzym;
    (c) eine Borzusammensetzung umfassend eine Borsäurequelle und ein Polyol; und
    (d) ein Peptidaldehyd der Formel: Z-B-NH-CH(R)-C(O)H
    worin B eine Peptidkette mit 1 bis 5 Aminosäuregruppen ist; Z eine N-Kappengruppe ist, gewählt aus der Gruppe, bestehend aus Phosphoramidat [(R"O)2(O)P-], Sulfenamid [(SR")-], Sulfonamid [(R"(O)2S-], Sulfonsäure [SO3H], Phosphinamid [(R")2(O)P-], Sulfamoylderivat [R"O(O)2S-], Thioharnstoff [(R"2N(S)C-], Thiocarbamat [R"O(S)C-], Phosphonat [R"-P(O)OH], Amidophosphat [R"O(OH)(O)P-], Carbamat (R"O(O)C-) und Harnstoff (R"NH(O)C-),
    worin jedes R" unabhängig gewählt ist aus der Gruppe, bestehend aus geradem oder verzweigtem, unsubstituiertem C1-C6-Alkylphenyl, C7-C9-Alkylaryl und Cycloalkylgruppen, worin der Cycloalkylring über C4-C8 spannen kann und ein oder mehrere Heteroatome enthalten kann, gewählt aus der O, N und S umfassenden Gruppen; und R gewählt ist aus der Gruppe, bestehend aus geradem oder verzweigtem, unsubstituiertem C1-C6-Alkyl, Phenyl und C7-C9-Alkylarylgruppen.
  2. Flüssige Reinigungszusammensetzung nach Anspruch 1, wobei die R-Gruppen aus der Gruppe gewählt sind, bestehend aus Methyl, iso-Propyl, sec-Butyl, iso-Butyl, -C6H5, -CH2-C6H5 und -CH2CH2-C6H5.
  3. Flüssige Reinigungszusammensetzung nach Anspruch 2, wobei die B-Peptidketten aus der Gruppe gewählt sind, bestehend aus Peptidketten mit den Aminosäuresequenzen gemäß der allgemeinen Formel: Z-A5-A4-A3-A2-A1-NH-CH(R)-C(O)H sodass die folgenden Aminosäuren, falls vorhanden, sind:
    A1 gewählt aus Ala, Gly;
    A2, falls vorhanden, gewählt aus Val, Ala, Gly, Ile;
    A3, falls vorhanden, gewählt aus Phe, Leu, Val, Ile;
    A4, falls vorhanden, irgendeine Aminosäure;
    A5, falls vorhanden, irgendeine Aminosäure.
  4. Flüssige Reinigungszusammensetzung nach Anspruch 3, wobei das N-terminale Ende geschützt ist durch eine der N-Kappengruppe-Schutzgruppen, gewählt aus der Gruppe, bestehend aus Carbamaten, Harnstoffen, Sulfonamiden, Phosphonamiden, Thioharnstoffen, Sulfenamiden, Sulfonsäuren, Phosphinamiden, Thiocarbamaten, Amidophosphaten und Phophoramidat.
  5. Flüssige Reinigungszusammensetzung nach Anspruch 4, wobei das N-terminale Ende des Proteaseinhibitors geschützt ist durch eine Methyl-, Ethyloder Benzylcarbamat- [CH3O-(O)C-; CH3CH2O-(O)C-; oder C6H5CH2NH-(O)C], Methyl-, Ethyl- oder Benzylharnstoff- [CH3NH-(O)C-; CH3CH2NH-(O)C-; oder C6H5CH2NH-(O)C-], Methyl-, Ethyl- oder Benzylsulfonamid-[CH3SO2-; CH3CH2SO2-; oder C6H5CH2SO2-], und Methyl-, Ethyl- oder Benzylamidophosphat- [CH3O(OH)(O)P-; CH3CH2O(OH)(O)P-; oder C6H5CH2O(OH)(O)P-]-Gruppen.
  6. Flüssige Reinigungszusammensetzung nach Anspruch 1, wobei das Peptidaldehyd aus der Gruppe gewählt ist, bestehend aus: CH3SO2Phe-Gly-Ala-Leu-H, CH3SO2Val-Ala-Leu-H, C6H5CH2O(OH)(O)P-Val-Ala-Leu-H, CH3CH2SO2-Phe-Gly-Ala-Leu-H, C6H5CH2SO2-Val-Ala-Leu-H, C6H5CH2O(OH)(O)P-Leu-Ala-Leu-H, C6H5CH2O(OH)(O)P-Phe-Ala-Leu-H und CH3O(OH)(O)P-Leu-Gly-Ala-Leu-H.
  7. Flüssige Reinigungszusammensetzung nach Anspruch 1, wobei die Borzusammensetzung Borsäure oder eine Borsäurequelle umfasst, gewählt aus der Gruppe, bestehend aus Boroxid, Borax, anderen Alkalimetallboraten, substituierten Borsäuren und Mischungen hiervon; und das Polyol ein Diol ist.
  8. Flüssige Reinigungszusammensetzung nach Anspruch 1, umfassend weiterhin eine wirksame Menge einer Calciumionenquelle.
  9. Flüssige Reinigungszusammensetzung nach Anspruch 8, umfassend:
    a) 8 bis 70% des Waschtensids;
    b) 0,001% bis 5% eines aktiven proteolytischen Enzyms;
    c) die Borzusammensetzung, umfassend 0,25% bis 10%, bezogen auf Gewicht, Borsäure oder eine Verbindung, welche zur Bildung von Borsäure in der Zusammensetzung fähig ist, und 1% bis 15%, bezogen auf das Gewicht der Zusammensetzung, Polyol;
    d) 0,00001% bis 5% des Peptidaldehyds; und
    e) 0,01% bis 1% Calciumionen.
  10. Flüssige Reinigungszusammensetzung nach Anspruch 1, umfassend weiterhin eine wirksame Menge eines oder mehrerer der folgenden Enzyme: Lipase, Amylase, Cellulase und Mischungen hiervon.
EP97941697A 1996-09-24 1997-09-19 Flüssige reinigungsmittel, die proteolytisches enzym, peptidaldehyd und eine borsäurequelle enthalten Expired - Lifetime EP0929636B1 (de)

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US2664796P 1996-09-24 1996-09-24
US26647P 1996-09-24
PCT/US1997/016626 WO1998013462A1 (en) 1996-09-24 1997-09-19 Liquid detergents containing proteolytic enzyme, peptide aldehyde and a source of boric acid

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EP (1) EP0929636B1 (de)
JP (1) JP2000506933A (de)
CN (1) CN1238002A (de)
AR (1) AR009817A1 (de)
AT (1) ATE229066T1 (de)
BR (1) BR9712115A (de)
CA (1) CA2266487A1 (de)
DE (1) DE69717652T2 (de)
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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8778650B2 (en) 2009-04-30 2014-07-15 Kao Corporation Alkaline protease variants

Families Citing this family (43)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE19857543A1 (de) * 1998-12-14 2000-06-15 Henkel Kgaa Verwendung von Protease in flüssigen bis gelförmigen Wasch- und Reinigungsmitteln
DK1385870T3 (da) 2000-07-21 2010-07-05 Schering Corp Peptider som inhibitorer af NS3-serinprotease fra hepatitis C-virus
HUP0303358A3 (en) * 2000-07-21 2005-10-28 Schering Corp Novel peptides as ns3-serine protease inhibitors of hepatitis c virus and pharmaceutical compositions containing them
US7244721B2 (en) 2000-07-21 2007-07-17 Schering Corporation Peptides as NS3-serine protease inhibitors of hepatitis C virus
DZ3349A1 (fr) 2000-07-28 2002-02-07 Henkel Kgaa Nouvelle enzyme amylolytique issue de bacillus sp. a 7-7 (dsm 12368) ainsi que produits de lavage et nettoyage contenant ledit enzyme amylolytique
ES2290184T3 (es) 2000-11-28 2008-02-16 Henkel Kommanditgesellschaft Auf Aktien Ciclodextrina-glucanotransferasa (cgtasa) a partir de bacillus agaradherens (dsm 9948) asi como agentes para el lavado y la limpeiza con esta nueva ciclodextrina-glucanotransferasa.
US20020183226A1 (en) * 2001-02-28 2002-12-05 Chandrika Kasturi Liquid detergent composition exhibiting enhanced alpha-amylase enzyme stability
DE10163884A1 (de) 2001-12-22 2003-07-10 Henkel Kgaa Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE10257387A1 (de) 2002-12-06 2004-06-24 Henkel Kgaa Mehrkomponenten-Flüssigwaschmittel
US20060293212A1 (en) * 2005-05-05 2006-12-28 Ecolab Inc. Stable solid compositions of spores, bacteria, fungi and/or enzyme
RU2510662C2 (ru) 2008-03-26 2014-04-10 Новозимс А/С Стабилизированные жидкие ферментные композиции
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JP6067409B2 (ja) 2012-04-10 2017-01-25 花王株式会社 アルカリプロテアーゼの溶解性向上方法
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WO2017005816A1 (en) 2015-07-06 2017-01-12 Novozymes A/S Lipase variants and polynucleotides encoding same
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JP2023538740A (ja) 2020-08-25 2023-09-11 ノボザイムス アクティーゼルスカブ ファミリー４４キシログルカナーゼの変異体
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WO2024131880A2 (en) 2022-12-23 2024-06-27 Novozymes A/S Detergent composition comprising catalase and amylase

Family Cites Families (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4537706A (en) * 1984-05-14 1985-08-27 The Procter & Gamble Company Liquid detergents containing boric acid to stabilize enzymes
AU3667189A (en) * 1988-06-23 1990-01-04 Unilever Plc Enzyme-containing liquid detergents
US4959179A (en) * 1989-01-30 1990-09-25 Lever Brothers Company Stabilized enzymes liquid detergent composition containing lipase and protease
DK204290D0 (da) * 1990-08-24 1990-08-24 Novo Nordisk As Enzymatisk detergentkomposition og fremgangsmaade til enzymstabilisering
US5284829A (en) * 1991-11-26 1994-02-08 The Regents Of The University Of California Synthetic tetrapeptides for the prevention of schistosome parasite infection
ES2098483T3 (es) * 1992-08-14 1997-05-01 Procter & Gamble Detergentes liquidos que contienen un aldehido peptidico.

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8778650B2 (en) 2009-04-30 2014-07-15 Kao Corporation Alkaline protease variants

Also Published As

Publication number Publication date
CA2266487A1 (en) 1998-04-02
ATE229066T1 (de) 2002-12-15
JP2000506933A (ja) 2000-06-06
DE69717652T2 (de) 2003-09-18
BR9712115A (pt) 1999-08-31
WO1998013462A1 (en) 1998-04-02
DE69717652D1 (de) 2003-01-16
EP0929636A1 (de) 1999-07-21
CN1238002A (zh) 1999-12-08
AR009817A1 (es) 2000-05-03

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