CA2096256C - Liquid detergent composition containing lipase and protease - Google Patents
Liquid detergent composition containing lipase and proteaseInfo
- Publication number
- CA2096256C CA2096256C CA002096256A CA2096256A CA2096256C CA 2096256 C CA2096256 C CA 2096256C CA 002096256 A CA002096256 A CA 002096256A CA 2096256 A CA2096256 A CA 2096256A CA 2096256 C CA2096256 C CA 2096256C
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- Prior art keywords
- protease
- lipase
- detergent composition
- per gram
- composition
- Prior art date
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Classifications
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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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/66—Non-ionic compounds
- C11D1/83—Mixtures of non-ionic with anionic compounds
-
- 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
-
- 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
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
-
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/02—Anionic compounds
- C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
- C11D1/14—Sulfonic acids or sulfuric acid esters; Salts thereof derived from aliphatic hydrocarbons or mono-alcohols
-
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/38—Cationic compounds
- C11D1/52—Carboxylic amides, alkylolamides or imides or their condensation products with alkylene oxides
- C11D1/525—Carboxylic amides (R1-CO-NR2R3), where R1, R2 or R3 contain two or more hydroxy groups per alkyl group, e.g. R3 being a reducing sugar rest
-
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/66—Non-ionic compounds
- C11D1/72—Ethers of polyoxyalkylene glycols
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
Abstract
Liquid detergent compositions are disclosed which contain conventional detergency ingredients and an enzyme system, wherein the enzyme system comprises a mixture of a lipase, or mixtures thereof, and a modified bacterial serine protease, or mixtures of said proteases.
Description
W O 92/08779 PC~r/US91/08041 -2U~62~6 LIQUID DETERGENT COMPOSITION CONTAINING
LIPASE AND PROTEASE
Technical Field The present invention relates to liquid detergent compositions which contain an enzyme system. The enzyme system is a combination of a modified protease and a lipase.
Background It is well known in the art that detergent compositions may advantageously comprise enzyme systems. Such enzyme systems include cellulase, protease, lipase and amylases. The present invention is specifically aiming at providing liquid detergent compositions in which the enzyme system comprises a mixture of protease and lipase.
Formulating such a combination in a granular detergent raises no specific issue, since both enzymes can be physically separated. On the contrary, formulating such a combination in a liquid detergent raises a specific technical issue in that the protease is likely to take as a substrate any protein present in the detergent composition.
W O 92/08779 z PCT/US91/08041 2~6~56 Specifically, it has been observed that lipases which may also be present in the detergent composition are particularly subject to such proteolytic degradation; as a consequence, the residual activity of the lipase in the detergent composition will rapidly diminish with the storage time of the detergent composition, so that it was up to now impossible to formulate liquid detergent compositions comprising at the same time a lipase and a protease, said detergent compositions being sufficiently stable for a commercial exploitation.
It is thus an object of the present invention to provide a liquid detergent composition comprising an enzyme system comprising a lipase and a protease, wherein said enzyme system is stable; by stable, it is meant that the proteolytic degradation of the lipase is substantially reduced.
It has now been found that this object can be met by using anv lipase, or mixtures thereof, together with a bacterial serine protease wherein the methionine adjacent to the serine of the active site has been replaced by another amino acid, or mixtures of such proteases.
Indeed, it has been discovered that this specific combination would provide an enzyme system comprising a protease and a lipase, which would be stable in a liquid detergent composition.
This solution has the advantage of being simple because it onlv requires ingredients which are commercially available; indeed, several modified bacterial serine proteases suitable for the purpose of this invention are commercially available, as well as several lipases suitable for use in a detergent comp~sition. Furthermore, the detergent compositions according to the invention require no addition of specific lipase stabilizers, and are therefore particularly attractive in terms of product cost and environmental compatibility.
Modified bacterial serine proteases including proteases suitable for use in the compositions according to the invention are disclosed for instance in EP-A-0 328 229 as well as their use in detergent compositions.
This patent application describes among others a modified bacterial serine protease which is commercially available from GIST-BROCADES under the name MAXAPEM 15R.
Biotechnology Newswatch, published March, 1988, page 6, and EP A-O 258 268 describe a lipase enzyme which is commercially available from NOVO NORDISK A/S under the trade name LIPOLASER. This European patent application mentions that LIPOLASER can be combined with proteases to form a granular enzymatic detergent additive.
EP-A-O 381 262 describes detergent compositions comprising a protease and a lipase, preferably LIPOLASER, together with a stabilizing system. The proteases disclosed in this reference include bacterial proteases.
Summary of the invention Accordingly, the present invention is a liquid detergent composition comprising from about 5% to about 60% by weight of an organic surface active agent selected from nonionic, anionic, cationic, and zwitterionic surface active agents and mixtures thereof, and an enzyme system comprising a,lipase derived from Humico 1a 7anuginosa a bacterial serine protease derived from Baci11us subti1is selected from the group consisting of a Baci11us subti1is which has been modified by replacing the methionine at position 197 in its amino acid sequence with cysteine or a Baci11us subti1is which has been modified by replacing the methionine at position 216 in its amino acid sequence with cysteine and wherein said lipase is present in an amount sufficient to provide from 0.1 to 10,000 Lipolytic Units per gram and wherein said protease is present in the amount of from 0.005 to 10 mg of active protease per gram of finished product, and from 0.01% to 5% by weight of the composition of an enzyme stabilization system selected from the group consisting of boric acid, 1,2-propanediol, carboxylic acids, and mixtures thereof and wherein said composition has a pH of from 7.0 to 8.5.
Detailed description of the invention The enzyme system according to the present invention comprises a lipase and a protease. Any lipase suitable for use in a detergent composition can be used in the compositions according to the invention, as described for instance in EP 0 381 262 or EP 271 152. The preferred lipase to be used in the compositions according to the present invention C
f W O 92/08779 P ~ /US91/08041 - 20~6~ 6 4 ~,_ ~ is a lipase derived from Humicola lanu~inosa, as described in EP-A-0 258 068 to NOVO INDUSTRI A/S. This patent application describes how to obtain said specific lipase, but said specific lipase is also commercially available from NOVO NORDISK A/S under the trade name LIPOLASER. Other commercially available lipases suitable for use herein are Amono-P Lipase R, Amono-B Lipase R, Amono CES Lipase R, Amono AKG
Lipase R, all from Amono Pharmaceuticals, Japan; Toyo Jozo Co, Japan and US biochemical Corp. USA as well as Diosynth Co, NL also commercialize suitable lipases for use in the compositions according to the present invention.
The compositions according to the present invention typically comprise from 0.l to l0000 Lipolytic Units per gram of finished product, preferably from l0 to 2500 Lipolytic Units per gram of finished product. Lipolytic units are defined for instance in EP 0 258 268, page 5 line 38..
The proteases to be used according to the present invention are modified bacterial serine proteases. All native bacterial serine proteases are characterized in that the active site invariably comprises a triade of amino acids which are serine, histidine and aspartic acid.
These amino acids are positioned in the native form of the enzyme in such a way that they catalyse the cleavage of internal peptide bonds of proteins. Another common point between these bacterial serine prote~ses is that there always is a methionine adjacent to the serine of .he active site, in the native sequence. The bacterial serine proteaseS
suitable for use according to the present invention are those wherein the methionine adjacent to the serine of the active site has been substituted by another amino acid. The serine of the active site can also be defined as the serine which is homologuous to the serine in position 221 in the amino acid sequence of the bacterial subtilisin protease produced by Bacillus Subtilis; said sequence is listed herein after in figure l.
W O 92/08779 5 P ~ /US91/08041 ~g62~G
In the sequence of this bacterial subtilisin protease produced by Bacillus Subtilis, the methionine is immediately after the serine in position 221 and therefore it is the methionine in position 222 which needs to be substituted by another amino acid. It is possible that, in the sequence of other bacterial serine proteases, this methionine would not be immediately following the serine of the active site; in such a case, it is the methionine homologuous to the methionine in position 222 in the sequence of this bacterial subtilisin protease produced by Bacillus Subtilis which needs to be substituted by another amino acid.
It is to be understood that the present invention does not reside in these modified proteases per se, rather in ehe particular applica~ion of these modified proteases to liquid detergent compositions also comprising a lipase; it is therefore not the aim of the present description to specify how these modified proteases can be obtained;
This modification can be done bv site-directed mutagenesis or any other genetic engeneering technique well known in the art for this purpose:
for instance, EP-A-0 328 229, to GIST-BROCADES N.V. describes how to obtain such proteases. Another suitable method is described in EP 130 756, which also describes a mofified bacterial serine protease suitable for use in the compositions according .o the invention.
Furthermore, some modified bacterial serine proteases suitable for use in the compositions according to the invention are commerciall.
available, such as DURAZY~ R from NOVO, which is the methionine moaified version of SAVINASE R; another e~ample of available modified protease is .YAXAPEM 15 from GIST-BROCADES, ~hich is ~he modified verSion of .~.CA' wherein the methionine in position 216 has been subs.i.uted. Also available are experimental samples of modified OPTICLE~ R and OPTIMASER, from SOLVAY enzymefi; both are modified in that the methionine in position 222 is substituted by a c~steine. Preferred modified bacterial serine protease according to the present invention are .~AXAPEM
15R from GIST BROCADES and DURAZYM R from NOVO.
The compositions according to the present invention typically will contain from 0.005 to 10 mg of active protease per gram of finished product, preferably from 0.01 to 5.0 mg of active protease per gram of W O 92/08779 P ~ /US91/08041 finished product2 ~19xtur~es of the modified bacterial serine protease described herein above are also suitable for use in the compositions according to the invention.
The rest of the liquid detergent composition according to the present invention is made of conventional detergency ingredients, i.e.
water, surfactants, builders and others. The following description of these ingredients is for the sake of completeness of the description and is not to be construed as limiting the compositions of the present invention to those conventional ingredients described.
The liquid detergent compositions herein comprises from 5% to 60% by weight of the total liquid detergent composition, preferably from 10% by weight to 40~ by weight of an organic surface-active agent selected from nonionic, anionic, cationic and zwitterionic surface-active agents and mixtures thereof.
Suitable anionic surface-active salts are selected from the group of sulfonates and sulfates. The like anionic surfactants are well-known in the detergent arts and have found wide applica.ion in com~ercial detergents. Preferred anionic water-soluble sulfonate or sulfate salts have in their molecular structure an alkvl radical containing from abou.
LIPASE AND PROTEASE
Technical Field The present invention relates to liquid detergent compositions which contain an enzyme system. The enzyme system is a combination of a modified protease and a lipase.
Background It is well known in the art that detergent compositions may advantageously comprise enzyme systems. Such enzyme systems include cellulase, protease, lipase and amylases. The present invention is specifically aiming at providing liquid detergent compositions in which the enzyme system comprises a mixture of protease and lipase.
Formulating such a combination in a granular detergent raises no specific issue, since both enzymes can be physically separated. On the contrary, formulating such a combination in a liquid detergent raises a specific technical issue in that the protease is likely to take as a substrate any protein present in the detergent composition.
W O 92/08779 z PCT/US91/08041 2~6~56 Specifically, it has been observed that lipases which may also be present in the detergent composition are particularly subject to such proteolytic degradation; as a consequence, the residual activity of the lipase in the detergent composition will rapidly diminish with the storage time of the detergent composition, so that it was up to now impossible to formulate liquid detergent compositions comprising at the same time a lipase and a protease, said detergent compositions being sufficiently stable for a commercial exploitation.
It is thus an object of the present invention to provide a liquid detergent composition comprising an enzyme system comprising a lipase and a protease, wherein said enzyme system is stable; by stable, it is meant that the proteolytic degradation of the lipase is substantially reduced.
It has now been found that this object can be met by using anv lipase, or mixtures thereof, together with a bacterial serine protease wherein the methionine adjacent to the serine of the active site has been replaced by another amino acid, or mixtures of such proteases.
Indeed, it has been discovered that this specific combination would provide an enzyme system comprising a protease and a lipase, which would be stable in a liquid detergent composition.
This solution has the advantage of being simple because it onlv requires ingredients which are commercially available; indeed, several modified bacterial serine proteases suitable for the purpose of this invention are commercially available, as well as several lipases suitable for use in a detergent comp~sition. Furthermore, the detergent compositions according to the invention require no addition of specific lipase stabilizers, and are therefore particularly attractive in terms of product cost and environmental compatibility.
Modified bacterial serine proteases including proteases suitable for use in the compositions according to the invention are disclosed for instance in EP-A-0 328 229 as well as their use in detergent compositions.
This patent application describes among others a modified bacterial serine protease which is commercially available from GIST-BROCADES under the name MAXAPEM 15R.
Biotechnology Newswatch, published March, 1988, page 6, and EP A-O 258 268 describe a lipase enzyme which is commercially available from NOVO NORDISK A/S under the trade name LIPOLASER. This European patent application mentions that LIPOLASER can be combined with proteases to form a granular enzymatic detergent additive.
EP-A-O 381 262 describes detergent compositions comprising a protease and a lipase, preferably LIPOLASER, together with a stabilizing system. The proteases disclosed in this reference include bacterial proteases.
Summary of the invention Accordingly, the present invention is a liquid detergent composition comprising from about 5% to about 60% by weight of an organic surface active agent selected from nonionic, anionic, cationic, and zwitterionic surface active agents and mixtures thereof, and an enzyme system comprising a,lipase derived from Humico 1a 7anuginosa a bacterial serine protease derived from Baci11us subti1is selected from the group consisting of a Baci11us subti1is which has been modified by replacing the methionine at position 197 in its amino acid sequence with cysteine or a Baci11us subti1is which has been modified by replacing the methionine at position 216 in its amino acid sequence with cysteine and wherein said lipase is present in an amount sufficient to provide from 0.1 to 10,000 Lipolytic Units per gram and wherein said protease is present in the amount of from 0.005 to 10 mg of active protease per gram of finished product, and from 0.01% to 5% by weight of the composition of an enzyme stabilization system selected from the group consisting of boric acid, 1,2-propanediol, carboxylic acids, and mixtures thereof and wherein said composition has a pH of from 7.0 to 8.5.
Detailed description of the invention The enzyme system according to the present invention comprises a lipase and a protease. Any lipase suitable for use in a detergent composition can be used in the compositions according to the invention, as described for instance in EP 0 381 262 or EP 271 152. The preferred lipase to be used in the compositions according to the present invention C
f W O 92/08779 P ~ /US91/08041 - 20~6~ 6 4 ~,_ ~ is a lipase derived from Humicola lanu~inosa, as described in EP-A-0 258 068 to NOVO INDUSTRI A/S. This patent application describes how to obtain said specific lipase, but said specific lipase is also commercially available from NOVO NORDISK A/S under the trade name LIPOLASER. Other commercially available lipases suitable for use herein are Amono-P Lipase R, Amono-B Lipase R, Amono CES Lipase R, Amono AKG
Lipase R, all from Amono Pharmaceuticals, Japan; Toyo Jozo Co, Japan and US biochemical Corp. USA as well as Diosynth Co, NL also commercialize suitable lipases for use in the compositions according to the present invention.
The compositions according to the present invention typically comprise from 0.l to l0000 Lipolytic Units per gram of finished product, preferably from l0 to 2500 Lipolytic Units per gram of finished product. Lipolytic units are defined for instance in EP 0 258 268, page 5 line 38..
The proteases to be used according to the present invention are modified bacterial serine proteases. All native bacterial serine proteases are characterized in that the active site invariably comprises a triade of amino acids which are serine, histidine and aspartic acid.
These amino acids are positioned in the native form of the enzyme in such a way that they catalyse the cleavage of internal peptide bonds of proteins. Another common point between these bacterial serine prote~ses is that there always is a methionine adjacent to the serine of .he active site, in the native sequence. The bacterial serine proteaseS
suitable for use according to the present invention are those wherein the methionine adjacent to the serine of the active site has been substituted by another amino acid. The serine of the active site can also be defined as the serine which is homologuous to the serine in position 221 in the amino acid sequence of the bacterial subtilisin protease produced by Bacillus Subtilis; said sequence is listed herein after in figure l.
W O 92/08779 5 P ~ /US91/08041 ~g62~G
In the sequence of this bacterial subtilisin protease produced by Bacillus Subtilis, the methionine is immediately after the serine in position 221 and therefore it is the methionine in position 222 which needs to be substituted by another amino acid. It is possible that, in the sequence of other bacterial serine proteases, this methionine would not be immediately following the serine of the active site; in such a case, it is the methionine homologuous to the methionine in position 222 in the sequence of this bacterial subtilisin protease produced by Bacillus Subtilis which needs to be substituted by another amino acid.
It is to be understood that the present invention does not reside in these modified proteases per se, rather in ehe particular applica~ion of these modified proteases to liquid detergent compositions also comprising a lipase; it is therefore not the aim of the present description to specify how these modified proteases can be obtained;
This modification can be done bv site-directed mutagenesis or any other genetic engeneering technique well known in the art for this purpose:
for instance, EP-A-0 328 229, to GIST-BROCADES N.V. describes how to obtain such proteases. Another suitable method is described in EP 130 756, which also describes a mofified bacterial serine protease suitable for use in the compositions according .o the invention.
Furthermore, some modified bacterial serine proteases suitable for use in the compositions according to the invention are commerciall.
available, such as DURAZY~ R from NOVO, which is the methionine moaified version of SAVINASE R; another e~ample of available modified protease is .YAXAPEM 15 from GIST-BROCADES, ~hich is ~he modified verSion of .~.CA' wherein the methionine in position 216 has been subs.i.uted. Also available are experimental samples of modified OPTICLE~ R and OPTIMASER, from SOLVAY enzymefi; both are modified in that the methionine in position 222 is substituted by a c~steine. Preferred modified bacterial serine protease according to the present invention are .~AXAPEM
15R from GIST BROCADES and DURAZYM R from NOVO.
The compositions according to the present invention typically will contain from 0.005 to 10 mg of active protease per gram of finished product, preferably from 0.01 to 5.0 mg of active protease per gram of W O 92/08779 P ~ /US91/08041 finished product2 ~19xtur~es of the modified bacterial serine protease described herein above are also suitable for use in the compositions according to the invention.
The rest of the liquid detergent composition according to the present invention is made of conventional detergency ingredients, i.e.
water, surfactants, builders and others. The following description of these ingredients is for the sake of completeness of the description and is not to be construed as limiting the compositions of the present invention to those conventional ingredients described.
The liquid detergent compositions herein comprises from 5% to 60% by weight of the total liquid detergent composition, preferably from 10% by weight to 40~ by weight of an organic surface-active agent selected from nonionic, anionic, cationic and zwitterionic surface-active agents and mixtures thereof.
Suitable anionic surface-active salts are selected from the group of sulfonates and sulfates. The like anionic surfactants are well-known in the detergent arts and have found wide applica.ion in com~ercial detergents. Preferred anionic water-soluble sulfonate or sulfate salts have in their molecular structure an alkvl radical containing from abou.
3 to about 22 carbon atoms.
Examples of such preferred anionic surfactan. salts are the react on ?roducts obtained by sulfating Cg-Clg fat,y alconols deri.~ed from e.g.
tallow oil, palm oil, palm kernel oil and coconut oil; alkylbenzene sulfonates wherein the alkyl group contains from about 9 to abou~ 15 carbon atoms; sodium alkylglyceryl ether sulfonates; ether sulfates of fatty alcohols derived from tallow and coconut oils; coconut fatty acid monoglyceride sulfates and sulfonates; and water-soluble salts of paraffin sulfonates having from about 8 to about 22 carbon atoms in the alkyl chain. Sulfonated olefin surfactants as more fully descr bed in e.g. ~.S. Patent Specification '.332.880 can aiso be used. The W O 92/08779 7 P ~ /~S91/08041 2~9625~
neutralizing cation for the anionic synthetic sulfonaees and/or sulfates is represented by conventional cations which are widely used in detergené technology such as sodium, potassium or alkanolammonium.
A suitable anionic synthetic surfactant component herein is represented by the water-soluble salts of an alkylbenzene sulfonic acid, preferably sodium alkylbenzene sulfonates, preferably sodium alkylbenzene sulfonates having from about 10 to 13 carbon atoms in the alkyl group.Another preferred anionic surfactant component herein is sodium alkyl sulfates having from about 10 to 15 carbon atoms in the alkyl group.
The nonionic surfactants suitable for use herein include those produced by condensing ethylene oxide with a hydrocarbon having a reactive hydrogen atom, e.g., a hydroxyl, carboxyl, or amido group, in the presence of an acidic or basic catalyst, and include compounds having the general formula RA(CH2CH2O)nH wherein R represents the hydrophobic moiety, A represents the group carrying the reactive hydrogen atom and n represents the average number of ethylene oxide moieties. R typically contains from about 8 to 22 carbon atoms They can also be formed by the condensation of propylene oxide with a lower molecular weight compound. n usually varies from about 2 to about 24.
A preferred class of nonionic ethoxylates is represented by the condensation product of a fatty alcohol having from 12 to 15 carbon atoms and from about 4 to 10 moles of ethvlene oxide per mole or fattv -alcohol. Suitable species of this class of ethoxylates include : thecondensation product of C12-Cls oxo-alcohols and 3 to 9 moles of ethylene oxide per mole of alcohol; the condensation product or narrow cut C14-Cls oxo-alcohols and 3 to 9 moles of ethylene oxide per mole of fatty(oxo)alcohol; the condensation product of a narrow cut C12-C13 fatty(oxo)alcohol and 6,5 moles of ethylene oxide per mole of fatty alcohol; and the condensation products of a Clo-C14 coconut fatty alcohol with a degree of ethoxylation (moles E0/mole fatty alcohol) in the range from 4 to 8. The fatty oxo alcohols while mainly linear can have, depending upon the processing conditions and raw material olefins, W O 92/08779 2 0'9 6 2 S 6 8 P ~ /US91/08041 a certain degree of br~n~hine, particularly short chain such as methyl branching. A degree of br~nching in the range from 15% to 50% (weight%) is frequently found in commercial oxo alcohols.
Suitable cationic surfactants include quaternary ammonium compounds of the formula RlR2R3R4N+ where Rl,R2 and R3 are methyl groups, and R4 is a C12 15 alkyl group, or where Rl is an ethyl or hydroxy ethyl group, R2 and R3 are methyl groups and R4 is a C12 15 alkyl group.
Zwitterionic surfactants include derivatives of aliphatic quaternary ammonium, phosphonium, and sulfonium compounds in which the aliphatic moiety can be straight or branched chain and wherein one of the aliphatic substituents contains from about 8 to about 24 carbon atoms and another substituent contains, at least, an anionic water-solubilizing group. Particularly preferred zwitterionic materials are the ethoxylated ammonium sulfonates and sulfates disclosed in U.S.
Patents 3,925,262, Laughlin et al., issued December 9, 1975 and 3,929,678, Laughlin et al., issued December 30, 1975.
Semi-polar nonionic surfactants include water-soluble amine oxides cont~i~ing one alkyl or hydroxy alkyl moiety of from about 8 to about 28 carbon atoms and two moieties selected from the group consisting of alkyl groups and hydroxy alkyl groups, containing from 1 to about 3 carbon atoms which can optionally be joined into ring structures.
Also suitable are Poly hydroxy fatty acid amide surfactants of .he formula R2-C-N-Z, wherein Rl is H, O Rl Cl 4hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R2 is Cs 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, Rl is methyl, R2 is a straight Cll 15 alkyl or alkenyl chain or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction.
W O 92/08779 9 P ~ /US91/08041 The compositions according to the present invention may further comprise 8 builder system. Any conventional builder system is suitable, but preferred is a mixture of citric acid and a substituted succinic acid.
The citric acid builder employed in the practicé of this invention will be present in the finished product in the form of any water-soluble salt of citric acid. Such salts include, for example, sodium, potassium, ammonium or alkanolammonium salts. In practice it is convenient to use a citric acid monohydrate slurry as a starting material, which will be neutralized in situ, so as to form the above mentioned salts.
The substituted succinic acid builders herein are of the general formula R-CH(COOH)CH2(COOH), i.e., derivatives of succinic acid, wherein R is Clo-Cl6 alkyl or alkenyl, preferably Cl2-Cl4 alkenyl.
These substituted succinic acid builders are preferably in the finished product in the form of their water-soluble salts, including the sodium, potassium, ammonium and alkanolammonium salts (e.g., mono-, di-, or tri-ethanolammonium).
As raw materials, it is preferred to use these succinic acid derivatives in their diacid or anhydride form. The diacid will be neutralized in situ, while the anhydride will undergo a hydrolysis/neutralization process.
Specific examples of substituted succinic acid builders include :
lauryl succinic acid, myristyl succinic acid, palmityl succinic acid, 2-dodecenyl succinic acid (preferred), 2-tetradecenyl succinic acid, and the like.
A preferred builder system comprises from 4% to 12% by weight of the total composition of the above substituted succinic acid builders, and from 4% to 12% by weight of the total composition of citric acid.
As an alternative builder, the compositions according to the invention may also contain a fatty acid. Preferred are oleic and palmitoleic acid.
It is well known from the man skilled in the art that the pH of the W O 92/08779 10 P ~ /US91/08041 composition may~sign~f~cQntly affect the enzyme system's performance.~_~
Accordingly, the compositions according to the invention preferably have a pH adjusted in the range of from 6 to 10, preferably from 7.5 to 8Ø
The compositions according to the invention may also comprise an enzyme stabilizing system. Indeed, the present invention provides a system wherein the protease does not significantly attack the native lipase, but the enzyme system or components thereof may still be subject to unstability problem due to the other detergency ingredients.
Therefore, stabilizing agents may be needed, which are conventional and well known in the art. A preferred enzyme stabilizing system is selected from boric acid, 1,2-propanediol, carboxylic acids, and mixtures thereof. These enzyme stabilizing systems are typically present in amounts of from 0.01% to 5% by weight of the total composition.
The compositions of the invention may also comprise other enzymes.
such as cellulases or amylases. Amylases, particularly, seem to be stable in the presence of protease, and the compositions of the invention therefore preferably comprise an amylase.
The compositions herein can contain a series of further optional ingredients. Examples of the like additives include : suds regulants, opacifiers, agents .to improve the ~chinP compatibility in relation to enamel-coated surfaces, bactericides, dyes, perfumes, bleaches including perborate and percarbonate, brighteners, soil release agents, softening agents and the like.
The liquid compositions herein can contain further additives, typically at levels of from 0.05 to 5%. These additives include polyaminocarboxylates such as ethylenediaminotetracetic acid, diethylenetriaminopentacetic acid, ethylenediamino disuccinic acid or water-soluble alkali metals thereof. Other additives include organo-phosphonic acids; particularly preferred are ethylenediamino tetramethylenephosphonic acid, hexamethylenediamino tetramethylenephosphonic acid, diethylenetriamino pentamethylenephosphonic acid and aminotrimethylenephosphonic acid.
20962~6 .~ 11 EXAMPLES
The following compositions according to the invention are made by mixing the listed ingredients in the listed proportions.
- Linear alkyl benzene sulfonate 12 7 6 7 8 - Sodium C12 15 alkyl sulfate 2 2 3 3 2 - C14 15 alkyl 2.5 times ethoxylated 0 0 2 2 0 sulfate - C12 glucose amide 0 0 6 6 0 - C12 lsalcohol 7 times ethoxylated 8 0 0 0 0 - C12 lsalcohol 5 times ethoxylated 0 8 0 0 8 - Oleic Acid 2 0 0 0 0 - Citric Acid 3 9 9 13 15 - C12 14 alkenyl substituted 10 5 5 7 6 succinic acid -.Ethanol 4 4 3 4 5 - 1,2-propanediol 2 3 3 l 2 - NaOH 6 8 8 ll ll - diethylene triamine 0.5 0.7 0.7 penta(methylene phosphonic acid) - Amylase(143KNU/g) 0.1 0.1 0.05 0.2 0.1 - LipolaseR(lOOKLU/g 0.4 0.2 0.3 0.3 0.3 commercial solution) - PEMlSR(50mg/g Commercial solution) 0.3 0 0 0 0.4 - DurazymR (39 mg/g Commercial solution) 0 0.2 0 0 0 - Opticlean M222CR (experimental sample) 0 0.1 0 0.4 0 - Optimase M222CR (experimental sample) 0 0 0.3 0 0 - CaC12 0.01 0 0.01 0.01 0.02 - Na metaborate 2.2 2 2 4 3 - Sodium formate 0 0 0 0 0 - Fatty Acids 0 0 0 0 0 - Uater and Minors -------------Balance to 100~------W O 92/08779 PC~r/US91/08041 2 0 9 6 2 ~ 6 12 ~~
EXAMPLES
The following compositions according to the invention are made by mixing the listed ingredients in the listed proportions - Linear alkyl benzene sulfonate 5 7 9 8 10 - Sodium C12 15 alkyl sulfate 5 2 1.75 0 3 - C14 15 alkyl 2.5 times ethoxylated 2 0 2 0 0 sulfate - C12 glucose amide 6 0 7 0 0 - C12 15alcohol 7 times ethoxylated 0 0 0.5 0 11.6 - C12 15alcohol 5 times ethoxylated 0 8 0 8 - Oleic Acid 0 0 0 3.5 2.5 - Citric Acid 10 9 9.5 4 - C12 14 alkenyl substituted 11 ~ 11.5 0 0 succinic acid - Zeolite 0 0 0 26 0 - Ethanol 6 4 4 3 6 - 1,2-propanediol 3 2 2 2 1.5 - NaOH 9 9 9.8 9 3.5 - diethylene triamine 1.0 1.0 1.0 0.5 0.8 penta(methylene phosphonic acid) - Amylase(143KNU/g) 0.2 0.1 0.2 0.05 - LipolaseR(100KLU/g 0.5 0.5 0.3 0.2 0.3 commercial solution) - PEM15R(50mg/g Commercial solution) 0.4 0 0 C 0.2 - DurazymR (39 mg/g Commercial solution) 0 0 0.5 0 0.2 - Opticlean M222CR (experimental sample) 0 0 0 0.3 0 - Optimase M222CR (experimental sample) 0 0.5 0 0 0 - CaC12 0.01 0.01 0.02 0.02 0.01 - Na metaborate 4 2 4 3 0 - Sodium formate 0 0 0 0 - Fatty Acids 0 0 0 0 12 - Water and Minors ---------------Balance to 100%--------W O 92/08779 PC~r/US91/08041 _ 13 2~6256 EXAMPLES
The following compositions according to the invention are made by mixing the listed ingredients in the listed proportions ' 11 12 13 14 15 - Linear alkyl benzene sulfonate 5 7 9 8 10 - Sodium C12 15 alkyl sulfate 5 2 1.75 0 3 - C14 15 alkyl 2.5 times ethoxylated 2 0 2 0 0 sulfate - C12 glucose amide 6 0 7 0 0 - C12 lsalcohol 7 times ethoxylated 0 0 0.5 0 11.6 - C12 lsalcohol 5 times ethoxylated 0 8 0 8 - Oleic Acid 0 0 0 3.5 2.5 - Citric Acid 10 9 9.5 4 - C12 14 alkenyl substituted 11 0 11.5 0 0 succinic acid - Tartrate monosuccinate 0 15 0 17 20 - Diethoxylated poly (1,2 propylene terephtalate) 1.0 0.5 0.7 0 0.5 - Ethanol 6 4 4 3 6 - 1,2-propanediol 3 2 2 2 1.5 - NaOH 9 9 9.8 9 3.5 - diethylene triamine 1.0 1.0 1.0 0.5 0.8 penta(methylene phosphonic acid) - Amylase(143KNU/g) 0.2 0.1 0.2 0.05 - LipolaseR(lOOKLU/g 0.5 0.5 0.3 0.2 0.3 commercial solution) - PEM15R(50mg/g Commercial solution) 0.4 0 0 0 0.2 - DurazymR (39 mg/g Commercial solution) 0 0 0.5 0 0.2 - Opticlean M222CR (experimental sample) 0 0 0 0.3 0 - Optimase M222CR (experimental sample) 0 0.5 0 0 0 - CaC12 0.01 0.01 0.02 0.02 0.01 - Na ~etaborate 4 2 4 3 0 - T~A 0 0 0 0 6 - Sodium formate 0 0 0 0 - Fatty Acids 0 0 0 0 12 - Water ~hd~Mi,~r5 ---------------Balance to 100~--------
Examples of such preferred anionic surfactan. salts are the react on ?roducts obtained by sulfating Cg-Clg fat,y alconols deri.~ed from e.g.
tallow oil, palm oil, palm kernel oil and coconut oil; alkylbenzene sulfonates wherein the alkyl group contains from about 9 to abou~ 15 carbon atoms; sodium alkylglyceryl ether sulfonates; ether sulfates of fatty alcohols derived from tallow and coconut oils; coconut fatty acid monoglyceride sulfates and sulfonates; and water-soluble salts of paraffin sulfonates having from about 8 to about 22 carbon atoms in the alkyl chain. Sulfonated olefin surfactants as more fully descr bed in e.g. ~.S. Patent Specification '.332.880 can aiso be used. The W O 92/08779 7 P ~ /~S91/08041 2~9625~
neutralizing cation for the anionic synthetic sulfonaees and/or sulfates is represented by conventional cations which are widely used in detergené technology such as sodium, potassium or alkanolammonium.
A suitable anionic synthetic surfactant component herein is represented by the water-soluble salts of an alkylbenzene sulfonic acid, preferably sodium alkylbenzene sulfonates, preferably sodium alkylbenzene sulfonates having from about 10 to 13 carbon atoms in the alkyl group.Another preferred anionic surfactant component herein is sodium alkyl sulfates having from about 10 to 15 carbon atoms in the alkyl group.
The nonionic surfactants suitable for use herein include those produced by condensing ethylene oxide with a hydrocarbon having a reactive hydrogen atom, e.g., a hydroxyl, carboxyl, or amido group, in the presence of an acidic or basic catalyst, and include compounds having the general formula RA(CH2CH2O)nH wherein R represents the hydrophobic moiety, A represents the group carrying the reactive hydrogen atom and n represents the average number of ethylene oxide moieties. R typically contains from about 8 to 22 carbon atoms They can also be formed by the condensation of propylene oxide with a lower molecular weight compound. n usually varies from about 2 to about 24.
A preferred class of nonionic ethoxylates is represented by the condensation product of a fatty alcohol having from 12 to 15 carbon atoms and from about 4 to 10 moles of ethvlene oxide per mole or fattv -alcohol. Suitable species of this class of ethoxylates include : thecondensation product of C12-Cls oxo-alcohols and 3 to 9 moles of ethylene oxide per mole of alcohol; the condensation product or narrow cut C14-Cls oxo-alcohols and 3 to 9 moles of ethylene oxide per mole of fatty(oxo)alcohol; the condensation product of a narrow cut C12-C13 fatty(oxo)alcohol and 6,5 moles of ethylene oxide per mole of fatty alcohol; and the condensation products of a Clo-C14 coconut fatty alcohol with a degree of ethoxylation (moles E0/mole fatty alcohol) in the range from 4 to 8. The fatty oxo alcohols while mainly linear can have, depending upon the processing conditions and raw material olefins, W O 92/08779 2 0'9 6 2 S 6 8 P ~ /US91/08041 a certain degree of br~n~hine, particularly short chain such as methyl branching. A degree of br~nching in the range from 15% to 50% (weight%) is frequently found in commercial oxo alcohols.
Suitable cationic surfactants include quaternary ammonium compounds of the formula RlR2R3R4N+ where Rl,R2 and R3 are methyl groups, and R4 is a C12 15 alkyl group, or where Rl is an ethyl or hydroxy ethyl group, R2 and R3 are methyl groups and R4 is a C12 15 alkyl group.
Zwitterionic surfactants include derivatives of aliphatic quaternary ammonium, phosphonium, and sulfonium compounds in which the aliphatic moiety can be straight or branched chain and wherein one of the aliphatic substituents contains from about 8 to about 24 carbon atoms and another substituent contains, at least, an anionic water-solubilizing group. Particularly preferred zwitterionic materials are the ethoxylated ammonium sulfonates and sulfates disclosed in U.S.
Patents 3,925,262, Laughlin et al., issued December 9, 1975 and 3,929,678, Laughlin et al., issued December 30, 1975.
Semi-polar nonionic surfactants include water-soluble amine oxides cont~i~ing one alkyl or hydroxy alkyl moiety of from about 8 to about 28 carbon atoms and two moieties selected from the group consisting of alkyl groups and hydroxy alkyl groups, containing from 1 to about 3 carbon atoms which can optionally be joined into ring structures.
Also suitable are Poly hydroxy fatty acid amide surfactants of .he formula R2-C-N-Z, wherein Rl is H, O Rl Cl 4hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R2 is Cs 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, Rl is methyl, R2 is a straight Cll 15 alkyl or alkenyl chain or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction.
W O 92/08779 9 P ~ /US91/08041 The compositions according to the present invention may further comprise 8 builder system. Any conventional builder system is suitable, but preferred is a mixture of citric acid and a substituted succinic acid.
The citric acid builder employed in the practicé of this invention will be present in the finished product in the form of any water-soluble salt of citric acid. Such salts include, for example, sodium, potassium, ammonium or alkanolammonium salts. In practice it is convenient to use a citric acid monohydrate slurry as a starting material, which will be neutralized in situ, so as to form the above mentioned salts.
The substituted succinic acid builders herein are of the general formula R-CH(COOH)CH2(COOH), i.e., derivatives of succinic acid, wherein R is Clo-Cl6 alkyl or alkenyl, preferably Cl2-Cl4 alkenyl.
These substituted succinic acid builders are preferably in the finished product in the form of their water-soluble salts, including the sodium, potassium, ammonium and alkanolammonium salts (e.g., mono-, di-, or tri-ethanolammonium).
As raw materials, it is preferred to use these succinic acid derivatives in their diacid or anhydride form. The diacid will be neutralized in situ, while the anhydride will undergo a hydrolysis/neutralization process.
Specific examples of substituted succinic acid builders include :
lauryl succinic acid, myristyl succinic acid, palmityl succinic acid, 2-dodecenyl succinic acid (preferred), 2-tetradecenyl succinic acid, and the like.
A preferred builder system comprises from 4% to 12% by weight of the total composition of the above substituted succinic acid builders, and from 4% to 12% by weight of the total composition of citric acid.
As an alternative builder, the compositions according to the invention may also contain a fatty acid. Preferred are oleic and palmitoleic acid.
It is well known from the man skilled in the art that the pH of the W O 92/08779 10 P ~ /US91/08041 composition may~sign~f~cQntly affect the enzyme system's performance.~_~
Accordingly, the compositions according to the invention preferably have a pH adjusted in the range of from 6 to 10, preferably from 7.5 to 8Ø
The compositions according to the invention may also comprise an enzyme stabilizing system. Indeed, the present invention provides a system wherein the protease does not significantly attack the native lipase, but the enzyme system or components thereof may still be subject to unstability problem due to the other detergency ingredients.
Therefore, stabilizing agents may be needed, which are conventional and well known in the art. A preferred enzyme stabilizing system is selected from boric acid, 1,2-propanediol, carboxylic acids, and mixtures thereof. These enzyme stabilizing systems are typically present in amounts of from 0.01% to 5% by weight of the total composition.
The compositions of the invention may also comprise other enzymes.
such as cellulases or amylases. Amylases, particularly, seem to be stable in the presence of protease, and the compositions of the invention therefore preferably comprise an amylase.
The compositions herein can contain a series of further optional ingredients. Examples of the like additives include : suds regulants, opacifiers, agents .to improve the ~chinP compatibility in relation to enamel-coated surfaces, bactericides, dyes, perfumes, bleaches including perborate and percarbonate, brighteners, soil release agents, softening agents and the like.
The liquid compositions herein can contain further additives, typically at levels of from 0.05 to 5%. These additives include polyaminocarboxylates such as ethylenediaminotetracetic acid, diethylenetriaminopentacetic acid, ethylenediamino disuccinic acid or water-soluble alkali metals thereof. Other additives include organo-phosphonic acids; particularly preferred are ethylenediamino tetramethylenephosphonic acid, hexamethylenediamino tetramethylenephosphonic acid, diethylenetriamino pentamethylenephosphonic acid and aminotrimethylenephosphonic acid.
20962~6 .~ 11 EXAMPLES
The following compositions according to the invention are made by mixing the listed ingredients in the listed proportions.
- Linear alkyl benzene sulfonate 12 7 6 7 8 - Sodium C12 15 alkyl sulfate 2 2 3 3 2 - C14 15 alkyl 2.5 times ethoxylated 0 0 2 2 0 sulfate - C12 glucose amide 0 0 6 6 0 - C12 lsalcohol 7 times ethoxylated 8 0 0 0 0 - C12 lsalcohol 5 times ethoxylated 0 8 0 0 8 - Oleic Acid 2 0 0 0 0 - Citric Acid 3 9 9 13 15 - C12 14 alkenyl substituted 10 5 5 7 6 succinic acid -.Ethanol 4 4 3 4 5 - 1,2-propanediol 2 3 3 l 2 - NaOH 6 8 8 ll ll - diethylene triamine 0.5 0.7 0.7 penta(methylene phosphonic acid) - Amylase(143KNU/g) 0.1 0.1 0.05 0.2 0.1 - LipolaseR(lOOKLU/g 0.4 0.2 0.3 0.3 0.3 commercial solution) - PEMlSR(50mg/g Commercial solution) 0.3 0 0 0 0.4 - DurazymR (39 mg/g Commercial solution) 0 0.2 0 0 0 - Opticlean M222CR (experimental sample) 0 0.1 0 0.4 0 - Optimase M222CR (experimental sample) 0 0 0.3 0 0 - CaC12 0.01 0 0.01 0.01 0.02 - Na metaborate 2.2 2 2 4 3 - Sodium formate 0 0 0 0 0 - Fatty Acids 0 0 0 0 0 - Uater and Minors -------------Balance to 100~------W O 92/08779 PC~r/US91/08041 2 0 9 6 2 ~ 6 12 ~~
EXAMPLES
The following compositions according to the invention are made by mixing the listed ingredients in the listed proportions - Linear alkyl benzene sulfonate 5 7 9 8 10 - Sodium C12 15 alkyl sulfate 5 2 1.75 0 3 - C14 15 alkyl 2.5 times ethoxylated 2 0 2 0 0 sulfate - C12 glucose amide 6 0 7 0 0 - C12 15alcohol 7 times ethoxylated 0 0 0.5 0 11.6 - C12 15alcohol 5 times ethoxylated 0 8 0 8 - Oleic Acid 0 0 0 3.5 2.5 - Citric Acid 10 9 9.5 4 - C12 14 alkenyl substituted 11 ~ 11.5 0 0 succinic acid - Zeolite 0 0 0 26 0 - Ethanol 6 4 4 3 6 - 1,2-propanediol 3 2 2 2 1.5 - NaOH 9 9 9.8 9 3.5 - diethylene triamine 1.0 1.0 1.0 0.5 0.8 penta(methylene phosphonic acid) - Amylase(143KNU/g) 0.2 0.1 0.2 0.05 - LipolaseR(100KLU/g 0.5 0.5 0.3 0.2 0.3 commercial solution) - PEM15R(50mg/g Commercial solution) 0.4 0 0 C 0.2 - DurazymR (39 mg/g Commercial solution) 0 0 0.5 0 0.2 - Opticlean M222CR (experimental sample) 0 0 0 0.3 0 - Optimase M222CR (experimental sample) 0 0.5 0 0 0 - CaC12 0.01 0.01 0.02 0.02 0.01 - Na metaborate 4 2 4 3 0 - Sodium formate 0 0 0 0 - Fatty Acids 0 0 0 0 12 - Water and Minors ---------------Balance to 100%--------W O 92/08779 PC~r/US91/08041 _ 13 2~6256 EXAMPLES
The following compositions according to the invention are made by mixing the listed ingredients in the listed proportions ' 11 12 13 14 15 - Linear alkyl benzene sulfonate 5 7 9 8 10 - Sodium C12 15 alkyl sulfate 5 2 1.75 0 3 - C14 15 alkyl 2.5 times ethoxylated 2 0 2 0 0 sulfate - C12 glucose amide 6 0 7 0 0 - C12 lsalcohol 7 times ethoxylated 0 0 0.5 0 11.6 - C12 lsalcohol 5 times ethoxylated 0 8 0 8 - Oleic Acid 0 0 0 3.5 2.5 - Citric Acid 10 9 9.5 4 - C12 14 alkenyl substituted 11 0 11.5 0 0 succinic acid - Tartrate monosuccinate 0 15 0 17 20 - Diethoxylated poly (1,2 propylene terephtalate) 1.0 0.5 0.7 0 0.5 - Ethanol 6 4 4 3 6 - 1,2-propanediol 3 2 2 2 1.5 - NaOH 9 9 9.8 9 3.5 - diethylene triamine 1.0 1.0 1.0 0.5 0.8 penta(methylene phosphonic acid) - Amylase(143KNU/g) 0.2 0.1 0.2 0.05 - LipolaseR(lOOKLU/g 0.5 0.5 0.3 0.2 0.3 commercial solution) - PEM15R(50mg/g Commercial solution) 0.4 0 0 0 0.2 - DurazymR (39 mg/g Commercial solution) 0 0 0.5 0 0.2 - Opticlean M222CR (experimental sample) 0 0 0 0.3 0 - Optimase M222CR (experimental sample) 0 0.5 0 0 0 - CaC12 0.01 0.01 0.02 0.02 0.01 - Na ~etaborate 4 2 4 3 0 - T~A 0 0 0 0 6 - Sodium formate 0 0 0 0 - Fatty Acids 0 0 0 0 12 - Water ~hd~Mi,~r5 ---------------Balance to 100~--------
Claims (6)
1. A liquid detergent composition comprising from about 5% to about 60%
by weight of an organic surface active agent selected from nonionic, anionic, cationic, and zwitterionic surface active agents and mixtures thereof, and an enzyme system comprising a lipase derived from Humicola lanuginosa, a bacterial serine protease derived from Bacillus subtilis selected from the group consisting of a Bacillus subtilis which has been modified by replacing the methionine at position 197 in its amino acid sequence with cysteine or a Bacillus subtilis which has been modified by replacing the methionine at position 216 in its amino acid sequence with cysteine and wherein said lipase is present in an amount sufficient to provide from 0.1 to 10,000 Lipolytic Units per gram and wherein said protease is present in the amount of from 0.005 to 10 mg of active protease per gram of finished product, and from 0.01% to 5% by weight of the composition of an enzyme stabilization system selected from the group consisting of boric acid, 1,2-propanediol, carboxylic acids, and mixtures thereof and wherein said composition has a pH of from 7.0 to 8.5.
by weight of an organic surface active agent selected from nonionic, anionic, cationic, and zwitterionic surface active agents and mixtures thereof, and an enzyme system comprising a lipase derived from Humicola lanuginosa, a bacterial serine protease derived from Bacillus subtilis selected from the group consisting of a Bacillus subtilis which has been modified by replacing the methionine at position 197 in its amino acid sequence with cysteine or a Bacillus subtilis which has been modified by replacing the methionine at position 216 in its amino acid sequence with cysteine and wherein said lipase is present in an amount sufficient to provide from 0.1 to 10,000 Lipolytic Units per gram and wherein said protease is present in the amount of from 0.005 to 10 mg of active protease per gram of finished product, and from 0.01% to 5% by weight of the composition of an enzyme stabilization system selected from the group consisting of boric acid, 1,2-propanediol, carboxylic acids, and mixtures thereof and wherein said composition has a pH of from 7.0 to 8.5.
2. A detergent composition according to Claim 1 which comprises a lipase in amounts so as to obtain from 10 to 2,500 Lipolytic Units per gram of finished product.
3. A detergent composition according to Claim 1 which comprises a protease according to Claim 1 or mixtures thereof, in amounts such as to obtain from 0.01 to 5.0 mg of active protease per gram of finished product.
4. A detergent composition according to Claim 1 which comprises an additional enzyme component selected from cellulases, amylases, and mixtures thereof.
5. A liquid detergent composition containing especially stable combinations of protease and lipase detergent enzymes, which composition comprises:
(A) from 10% to 40% by weight of a surface active agent selected from anionic surfactants, nonionic surfactants and combinations thereof;
(B) from 4% to 12% by weight of a detergent builder;
(C) from 10 to 2,500 Lipolytic Units per gram of composition of a lipase derived from Humicola lanuginosa; and (D) from 0.1 to 5.0 mg of active protease per gram of composition of a serine protease which is derived from Bacillus subtilis and which has been modified by replacing the serine at, or homologous to, position 216 in its amino acid sequence with cysteine;
said composition having a pH of from 7.0 to 8.5.
(A) from 10% to 40% by weight of a surface active agent selected from anionic surfactants, nonionic surfactants and combinations thereof;
(B) from 4% to 12% by weight of a detergent builder;
(C) from 10 to 2,500 Lipolytic Units per gram of composition of a lipase derived from Humicola lanuginosa; and (D) from 0.1 to 5.0 mg of active protease per gram of composition of a serine protease which is derived from Bacillus subtilis and which has been modified by replacing the serine at, or homologous to, position 216 in its amino acid sequence with cysteine;
said composition having a pH of from 7.0 to 8.5.
6. A liquid detergent composition according to Claim 5 wherein:
(A) the surface active agent comprises a combination of both i) anionic surfactants comprising sulfonate or sulfate salts containing in their structure an alkyl radical from about 8 to 22 carbon atoms; and ii) nonionic surfactants selected from a) fatty alcohol ethoxylates having from 12 to 15 carbon atoms and from about 4 to 10 moles of ethylene oxide per mole; and b) polyhydroxy fatty acid amide surfactants of the formula wherein R2 is straight chain C11-15 alkyl or alkenyl, and Z is derived from a reducing sugar selected from glucose, fructose, maltose, and lactose, in a reductive amination reaction; and c) combinations of these nonionic surfactants; and (B) the detergent builder is selected from citric acid and succinic acid derivatives.
(A) the surface active agent comprises a combination of both i) anionic surfactants comprising sulfonate or sulfate salts containing in their structure an alkyl radical from about 8 to 22 carbon atoms; and ii) nonionic surfactants selected from a) fatty alcohol ethoxylates having from 12 to 15 carbon atoms and from about 4 to 10 moles of ethylene oxide per mole; and b) polyhydroxy fatty acid amide surfactants of the formula wherein R2 is straight chain C11-15 alkyl or alkenyl, and Z is derived from a reducing sugar selected from glucose, fructose, maltose, and lactose, in a reductive amination reaction; and c) combinations of these nonionic surfactants; and (B) the detergent builder is selected from citric acid and succinic acid derivatives.
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP90870212.9 | 1990-11-14 | ||
| EP90870212 | 1990-11-14 | ||
| EP91200149.2 | 1991-01-25 | ||
| EP19910200149 EP0486073B1 (en) | 1990-11-14 | 1991-01-25 | Liquid detergent composition containing lipase and protease |
| PCT/US1991/008041 WO1992008779A1 (en) | 1990-11-14 | 1991-11-04 | Liquid detergent composition containing lipase and protease |
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|---|---|
| CA2096256A1 CA2096256A1 (en) | 1992-05-15 |
| CA2096256C true CA2096256C (en) | 1999-05-11 |
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|---|---|---|---|
| CA002096256A Expired - Fee Related CA2096256C (en) | 1990-11-14 | 1991-11-04 | Liquid detergent composition containing lipase and protease |
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|---|---|
| EP (1) | EP0486073B1 (en) |
| JP (1) | JPH06504555A (en) |
| CN (1) | CN1062374A (en) |
| AU (1) | AU9041691A (en) |
| CA (1) | CA2096256C (en) |
| DE (1) | DE69121059T2 (en) |
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| ES (1) | ES2091280T3 (en) |
| IE (1) | IE913951A1 (en) |
| MX (1) | MX9102022A (en) |
| NZ (1) | NZ240571A (en) |
| TR (1) | TR27423A (en) |
| TW (1) | TW215108B (en) |
| WO (1) | WO1992008779A1 (en) |
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| CA2109526C (en) * | 1991-04-30 | 1998-01-20 | Dwight M. Peterson | Liquid detergents with an aryl boroic acid |
| CA2119362A1 (en) * | 1991-10-16 | 1993-04-29 | Carlo J. Van Den Bergh | Aqueous enzymatic detergent compositions |
| US5442100A (en) * | 1992-08-14 | 1995-08-15 | The Procter & Gamble Company | β-aminoalkyl and β-N-peptidylaminoalkyl boronic acids |
| JP2859520B2 (en) * | 1993-08-30 | 1999-02-17 | ノボ ノルディスク アクティーゼルスカブ | Lipase, microorganism producing the same, method for producing lipase, and detergent composition containing lipase |
| DE69434635D1 (en) | 1993-10-08 | 2006-04-27 | Novo Nordisk As | Amylasevarianten |
| DE4344154A1 (en) * | 1993-12-23 | 1995-06-29 | Henkel Kgaa | Liquid detergent containing enzymes |
| JP4733861B2 (en) * | 2001-06-20 | 2011-07-27 | 花王株式会社 | Enzyme particles |
| US7491362B1 (en) * | 2008-01-28 | 2009-02-17 | Ecolab Inc. | Multiple enzyme cleaner for surgical instruments and endoscopes |
| BR112012017060A2 (en) * | 2009-12-21 | 2016-11-29 | Danisco Us Inc | "Thermobifide lipase-containing detergent compositions, method for hydrolyzing a lipid present in a dirt or stain on a surface and method for performing a transesterification reaction |
| CN102444018B (en) * | 2011-10-26 | 2013-07-31 | 芜湖南翔羽绒有限公司 | Biochemical combination precision washing technology for eiderdown |
| CN102604754B (en) * | 2012-02-03 | 2013-07-03 | 深圳市绿微康生物工程有限公司 | Biological enzyme cleaning agent and method for preparing same |
| DE102013224250A1 (en) | 2013-11-27 | 2015-05-28 | Henkel Ag & Co. Kgaa | Lipase stabilization in dishwashing detergents |
| BR112017027402B1 (en) * | 2015-06-26 | 2022-05-10 | Unilever Ip Holdings B.V. | Detergent composition for washing clothes and method of domestic treatment of a fabric |
| WO2017036917A1 (en) * | 2015-08-28 | 2017-03-09 | Unilever N.V. | Liquid detergency composition comprising lipase and protease |
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| US4760025A (en) * | 1984-05-29 | 1988-07-26 | Genencor, Inc. | Modified enzymes and methods for making same |
| US4980288A (en) * | 1986-02-12 | 1990-12-25 | Genex Corporation | Subtilisin with increased thermal stability |
| ES2058119T3 (en) * | 1986-08-29 | 1994-11-01 | Novo Nordisk As | ENZYMATIC DETERGENT ADDITIVE. |
| DK571587D0 (en) * | 1987-11-02 | 1987-11-02 | Novo Industri As | ENZYMATIC DETERGENT COMPOSITION |
| PT89702B (en) * | 1988-02-11 | 1994-04-29 | Gist Brocades Nv | PROCESS FOR PREPARING NEW PROTEOLITIC ENZYMES AND DETERGENTS THAT CONTAINS THEM |
| CA2006527A1 (en) * | 1988-12-30 | 1990-06-30 | Martin S. Cardinali | Enzymatic liquid detergent compositions |
| US4959179A (en) * | 1989-01-30 | 1990-09-25 | Lever Brothers Company | Stabilized enzymes liquid detergent composition containing lipase and protease |
| US5030378A (en) * | 1990-01-02 | 1991-07-09 | The Procter & Gamble Company | Liquid detergents containing anionic surfactant, builder and proteolytic enzyme |
-
1991
- 1991-01-25 DK DK91200149T patent/DK0486073T3/en active
- 1991-01-25 EP EP19910200149 patent/EP0486073B1/en not_active Expired - Lifetime
- 1991-01-25 DE DE1991621059 patent/DE69121059T2/en not_active Expired - Lifetime
- 1991-01-25 ES ES91200149T patent/ES2091280T3/en not_active Expired - Lifetime
- 1991-11-04 JP JP4500878A patent/JPH06504555A/en active Pending
- 1991-11-04 AU AU90416/91A patent/AU9041691A/en not_active Abandoned
- 1991-11-04 CA CA002096256A patent/CA2096256C/en not_active Expired - Fee Related
- 1991-11-04 WO PCT/US1991/008041 patent/WO1992008779A1/en active Application Filing
- 1991-11-12 MX MX9102022A patent/MX9102022A/en not_active IP Right Cessation
- 1991-11-13 IE IE395191A patent/IE913951A1/en unknown
- 1991-11-13 NZ NZ24057191A patent/NZ240571A/en unknown
- 1991-11-14 CN CN 91111550 patent/CN1062374A/en active Pending
- 1991-12-04 TR TR106991A patent/TR27423A/en unknown
-
1992
- 1992-01-25 TW TW81100525A patent/TW215108B/zh active
Also Published As
| Publication number | Publication date |
|---|---|
| CN1062374A (en) | 1992-07-01 |
| NZ240571A (en) | 1994-11-25 |
| JPH06504555A (en) | 1994-05-26 |
| MX9102022A (en) | 1992-07-08 |
| WO1992008779A1 (en) | 1992-05-29 |
| DE69121059D1 (en) | 1996-08-29 |
| DE69121059T2 (en) | 1997-03-06 |
| EP0486073B1 (en) | 1996-07-24 |
| IE913951A1 (en) | 1992-05-20 |
| TR27423A (en) | 1995-04-21 |
| EP0486073A2 (en) | 1992-05-20 |
| ES2091280T3 (en) | 1996-11-01 |
| CA2096256A1 (en) | 1992-05-15 |
| DK0486073T3 (en) | 1996-12-09 |
| TW215108B (en) | 1993-10-21 |
| EP0486073A3 (en) | 1993-06-23 |
| AU9041691A (en) | 1992-06-11 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| MKLA | Lapsed |