JPH06504555A - Liquid detergent composition containing lipase and protease - Google Patents

Abstract

(57) [Summary] This bulletin contains application data before electronic filing, so abstract data is not recorded.

Description

[Detailed description of the invention] Liquid detergent composition technology containing lipase and protease The present invention relates to liquid detergent compositions containing enzyme systems.

This enzyme system is a combination of a modified protease and a lipase.

background The inclusion of enzyme systems in detergent compositions is known. Examples of such enzyme systems include includes cellulases, proteases, lipases and amylases. The purpose of the invention is to develop a liquid detergent composition in which this enzyme system is a mixture of protease and lipase. The goal is to provide products.

Since both enzymes are physically separated, formulating such a mixture in granular detergents requires There are no particular problems. On the other hand, formulating such mixtures into liquid detergents is A technical problem arose in that tease uses proteins present in detergent compositions as substrates. Ru. In particular, lipases simultaneously present in detergent compositions may It has been observed that they are particularly susceptible to degradation. As a result, lipase in detergent compositions The residual activity of lipase and protea rapidly decreases upon storage of detergent compositions. detergents that are sufficiently stable to be suitable for commercial purposes by co-formulating them into liquid detergent compositions. Until now, it has been impossible to manufacture.

The object of the present invention is to provide a liquid detergent composition containing an enzyme system consisting of lipase and protease. The enzyme system substantially reduces proteolytic degradation of lipase. It is stable in the sense that it is stable.

The object of the present invention is to use lipases of any kind or mixtures thereof. It turns out that this can also be achieved by using bacterial serine proteases. did.

Here, this protease has a methionine adjacent to the serine in the active site that is linked to other amino acids. or a mixture of such proteases. It is.

In fact, this special combination provides stable protease and It has been found that a mixed enzyme system of lipases can be provided.

This solution has the advantage of being simple, requiring only commercially available ingredients; Various modified bacterial serine proteases suitable for the purpose of the invention are used in various detergent lipids. It is commercially available along with other enzymes. Furthermore, the detergent composition of the present invention contains a lipase stabilizer. therefore, it is an attractive commercial product in terms of production costs and environmental friendliness. It is a quality product.

Modified bacterial serine proteins including proteases suitable for use in the present invention Aases are described in EP-A-0328229 with instructions for use in detergent compositions. There is a disclosure. This patent application is filed under the trade name rMAXAPEM 15RJ. Modified bacterial serine protea commercially available from T-BROCADES It mainly discloses

``Biotechnology News Watch 2 (Biotechnology Ne wsvatch), March 1988 issue, page 6, and EP-A-02582 In Publication No. 68, the trademark name r LIPOL from N0VON0RDISK^/S company There is a description of a lipase enzyme commercially available as ASERJ.

In this EP application, LIPOLAR9ER is a granular enzyme with protease. It is disclosed that basic detergent additives can be formed.

In EP-A-0381262, proteases and lipases, especially LIP Detergent compositions using OLASER with a stabilizer system are disclosed. This document The proteases disclosed in the present invention include bacterial proteases. The present invention relates to a liquid detergent composition containing an enzyme system, wherein the enzyme system is a modified bacterial serine. Consisting of protease or mixture thereof and lipase or mixture thereof It is characterized by This bacterial serine protease has an active site adjacent to the serine It is modified so that methionine is replaced with another amino acid.

Detailed description of the invention The enzyme system of the invention comprises a lipase and a protease. suitable for detergents Any type of pase is acceptable (for example, EP 0 381 262 and similar 271, see No. 152). The lipase suitable for use in the present invention is Hu+w1c It is derived from ola Ianuglnosa, and N0VOINDUSTRI A/S Company +7) EP-A-0258068. This patent application describes a method for obtaining this particular lipase, which has the trade name r LIPOLAs ERJ To L Te N0VON0RDISK A/S company Kara commercially available It is. Other lipases that can be used in the present invention are rAMONO-P Lipas e RJ, rA+gono-B Lipase”J, rAmono-CBS LipaseRJ, r　Awono　AKG　Agon as LipaseRJ o Commercially available from Pharsceutleals (Japan); Toyo Jozo Co., Ltd. and US Biochemical Company (USA) also manufactures lipase that can be used in the present invention. Ru.

The compositions of the invention generally contain between 0.1 and 10,000 lipolytic units per duram of the final product. The range of 10 to 2500 lipolytic units is preferable, and the lipolytic units include For example, it is defined in EP O258268, page 5, line 38.

The proteases used in the present invention are modified bacterial serine proteases. Heaven Natural bacterial serine proteases have all active sites consisting of serine, histidine, and It consists of triades of amino acids, which are aspartic acid and aspartic acid. this These amino acids can be fermented in a manner that catalyzes the cleavage of peptide bonds within proteins. It is located inside a natural cedar tree. Another commonality is that these bacterial serine proteases In the natural sequence, methionine is always adjacent to serine in the active site of enzymes. It is. Bacterial serine proteases suitable for use in the present invention include active site This methionine adjacent to serine is replaced with another amino acid. similar The active site serine is produced by Bacillus 5ubtllls. Homologous to serine at position 221 in the amino acid sequence of bacterial subtilisin protease can be defined as serine; the sequence is as shown in FIG.

This bacterial subtilisin produced by Bacillus 5ubt. In the rotease sequence, this methionine is located immediately downstream of serine at position 221. It is the methane at position 222 that therefore needs to be replaced by another amino acid. It's Onin. In the sequences of other bacterial serine proteases, this methionine is Since it does not directly follow the active site serine, in such cases other amino acids All that is required to be replaced by Bacillus 5ubtilis is the methionine at position 222 in the sequence of this bacterial subtilisin protease. It is a homologous methionine.

The present invention is not inventive in these modified proteases themselves, but in the lipase The application of these modified proteases to liquid detergent compositions simultaneously containing Therefore, it is an objective of the present invention to specify the method for producing these modified proteases. Not the point. For example, EP-A-0328229 (GIST-BROCADE SN, v,) Niha A method for producing such a protease is described, and the above modification is using site-directed mutagenesis techniques or other genetic engineering techniques known to those skilled in the art. It can be done by Other suitable methods are disclosed in EP 130 756. This includes modified bacterial serine proteases suitable for use in the present invention. is also disclosed.

Furthermore, the modified bacterial serine broteases that can be used in the present invention (trade name: DUR) AZYM R (manufactured by NOVO) L7 is commercially available, and this product has the trade name 5A. This is a methionine-modified variant of VINASE R, and the other commercially available example is MAXACAL. Product name MAXAPE is a modified form of R, in which methionine at position 216 is substituted. M15 (manufactured by GIST-BROCARDES).

5OLVAYII Sosha Kara (7) Modified 0PTICLEAN Oyohi OPTIMA SB” was provided as an experimental sample, and in both cases, methionine at position 222 is cysteine. It has been replaced by Bacterial serine proteases suitable for the present invention include G.I. ST BROCADES 11 MAXAPEM 15 Oyohi N0VO DIIRAZYM'te.

The compositions of the invention typically contain between 0.005 and 10 mg of active protease in the final product. The content is preferably 0.01 to 5.0 mg. Modified Bacterial Umbrella Mixtures of ambroteases are also suitable for use in the present invention.

Other components of the liquid detergent composition of the present invention include water, builders, etc., which are known cleaning components. occupy The following description of these components is for the purpose of sufficient explanation. The composition of the present invention is limited to these known components. should not be construed as such.

The liquid detergent compositions described herein preferably contain 5 to 60% by weight of the total liquid detergent composition. contains 10 to 40% by weight of nonionic, anionic and zwitterionic surfactants and and mixtures thereof.

Anionic surfactants are made from sulfonates and sulfates. selected. This anionic surfactant is well known in the industry and is widely used in commercial detergents. It has been adopted. Preferred water-soluble anionic sulfonates or sulfates are It has an alkyl group containing from about 3 to about 22 carbon atoms in its molecular backbone.

Examples of preferred anionic surfactants include, for example, animal fatty oils, balm oils, perfusate oils, For the sulfation of C8-018 fatty alcohols derived from mussel kernel oil and coconut oil reaction product; alkylbenzene sulfone with an alkyl group having about 9 to about 15 carbon atoms; ethers of aliphatic alcohols derived from animal fatty oils and coconut oil Sulfates; Coconut oil fatty acid monoglyceride sulfates and sulfonates Paraffin sulfonates having about 8 to about 22 carbon atoms in the alkyl chain Water-soluble salts of. Regarding sulfonated olefin surfactants, US special It is described in detail in Japanese Patent No. 3.332.880 and can also be used in the present invention. . Neutralizing cations for anionic synthetic sulfonates and/or sulfates are widely used in the detergent industry, such as sodium, potassium or alkanol ammonium. These are commonly used cations.

The anionic synthetic surfactant component preferably used in the present invention is alkylbenzene Water-soluble salts of sulfonic acids, preferably sodium alkylbenzene sulfonates etc., preferably sodium alkyl bases having about 10 to 13 carbon atoms in the alkyl group. They are zenesulfonates. Other preferred anionic surfactant components include alkaline surfactants. Sodium alkyl sulfates having 10 to 15 carbon atoms in the group. Ru.

Examples of nonionic surfactants used in the present invention include, for example, the general formula: RA ( CH2CH20) nH [wherein, R represents a lipophilic site, and A represents a reactive hydrogen atom. a group having ethylene oxide, n represents the average number of ethylene oxide], or and a reactive hydrogen atom, such as a hydroxyl group, a carboxyl group, or an amide group. The hydrocarbon and ethylene oxide are condensed in the presence of an acidic or basic catalyst. This includes compounds obtained by R typically contains 8 to 22 carbon atoms. these are It can also be obtained by condensation of propylene oxide and low molecular weight compounds. n is about 2~ It is about 24.

Preferred examples of nonionic ethoxylates include aliphatic alkali having 12 to 15 carbon atoms. Condensation of coal with about 4 to 10 moles of ethylene oxide per mole of aliphatic allul products. Preferred examples of such ethylene oxylates include: Condensation of Cl2-Cl3 oxo alcohols with 3 to 9 moles of ethylene oxide 3 to 9 moles of ethylene oxide per mole of aliphatic (oxo)alcohol condensate with C14-Cl3 oxo alcohols of narrow boiling point range; narrow boiling point range C12”-013f8 aliphatic (oxo) alcohol and aliphatic alcohol per mole 6.5 moles of ethylene oxide condensate; and C10'14 coconut oil fat Group alcohols and degree of ethoxylate (number of moles of EO per mole of aliphatic alcohol) Condensation products having from 4 to 8 are included. These aliphatic oxo alcohols are mainly Although it is a straight chain, it may contain a certain amount of methyl content depending on the manufacturing conditions or the raw olefin. It has particularly short branches, such as branches. The degree of branching in commercially available oxo alcohols is It is often 15 to 50% by weight.

Examples of suitable cationic surfactants include those having the general formula RIRRRN" [where R, R and and R3 is a methyl group, R4 is a C12'15 alkyl group, or R is ethyl. or hydroxyethyl group, R2 and R are methyl groups and R is C1 Quaternary ammonium compounds represented by 2-C15 alkyl group are included. Ru.

Examples of zwitterionic surfactants include aliphatic quaternary ammoniums, phosphoniums, and and sulfonium compounds, in which the aliphatic moiety can be linear or branched. and one of the aliphatic substituents has about 8 to about 24 carbon atoms, and the other substituents have a small number of carbon atoms. It has at least an anionic water-soluble group. Particularly preferred zwitterionic materials are U.S. Patent No. 3.925.262 (Laughllnr et al.) (December 9, 1975) ) and Publication No. 3.929.687 (Laughllnr et al.) (1975 ethoxylate ammonium sulfonate and monkeys disclosed in December 30, 2013) It is Fate.

Semipolar nonionic surfactants include one alkyl group having from about 8 to about 28 carbon atoms or includes water-soluble amine oxides containing a hydroxyalkyl moiety. The a 1 to about 3 atoms in the alkyl and hydroxyalkyl groups that may optionally form a ring. contains carbon atoms.

■ [Wherein, R is a hydrogen atom, C hydrocarbyl, 2-hydroxyethyl, 2-hydro oxypropyl or a mixture thereof, R is C hydrocarbyl, and Z is in the chain a straight hydrocarpyl chain having at least three directly attached hydroxyl groups; or their alkoxylate derivatives] Fatty acid amide surfactants are also suitable. Preferably, R is methyl, R is linear C1 1-15 alkyl or alkylene chain or a mixture thereof, Z is gluco from reducing sugars such as sugar, fructose, maltose, and lactose. This is a compound derived from a minization reaction.

Additionally, the compositions of the invention may contain a builder system.

The builder system may be any known builder system, but preferably citric acid and substituted succinic acid. It is a mixture of

The citric acid builder is included in the final composition in the form of a water-soluble citrate salt. It takes Salts include, for example, sodium, potassium, ammonium or alkanols. amine salts are included. In practice, citric acid monohydrate slurry is used as the starting material. It is convenient to use salt, and it neutralizes it like making salts on the spot.

Substituted succinic acid builders have the general formula R-CH(COOH)CH2(COOH), That is, a succinic acid derivative, where R is Cto-te alkyl or alkenyl. , preferably C alkenyl].

These substituted succinate builders include sodium, potassium, ammonium and Lukanolamine salts (i.e., mono-, di-, or tri-ethanolamine salts) preferably present in the final product in the form of water-soluble salts containing .

As raw materials, these succinic acid derivatives are used in their diacid or anhydride form. It is better to Diacids are neutralized in situ and anhydrides are hydrolyzed/neutralized.

Among the substituted succinic acid building blocks are laurylconollic acid, myristylsuccinic acid, Valmitylsuccinic acid, 2-dodecenylsuccinic acid (preferred), 2-tetradecenyl Includes luconoic acid and the like.

A preferred builder system comprises 4 to 12% by weight of the above-mentioned substituted succinic bisaccharides, based on the total composition. Lugu, and 4-12% by weight of citric acid. Fat as other builders Acids may also be used. Oleic acid and valmitic acid are the preferred fatty acids.

It is known in the industry that the pH of a composition has a significant impact on the performance of enzyme systems.

Therefore, the pH of the composition of the present invention is adjusted to 6 to 10, preferably 7.5 to 8.0. It is preferable to do so.

The compositions of the invention also contain an enzyme stabilization system. According to the invention, the protease is Although it does not appreciably attack natural lipase, its enzyme system or composition It still has the problem of being destabilized by the presence of other detergent ingredients. did Therefore, it is preferred that known enzyme stabilizers be present in the final product. suitable enzyme Stable systems include boric acid, 1,2-propanediol, carboxylic acid, and mixtures thereof. selected from things. The amount used is from 0.01 to 5% by weight (based on the total composition).

The composition of the present invention can contain other enzymes such as cellulases and amylases.

In particular, amylases are stable in the presence of proteases and therefore the composition of the present invention Preferably, the composition contains amylase.

The composition may further contain a series of optional ingredients.

Examples of such additives include: foam control agents, opacifying agents, related to enamelled surfaces. Includes machine compatibility enhancers, fungicides, dyes, fragrances, perborates and percarbonates Included are bleaches, brighteners, stain removers, softeners, and the like.

The composition of the present invention may further contain about 0.05 to 5% by weight of additives. this Among their targets are ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, and ethylenediaminetetraacetic acid. diamine nicosuccinic acid or their water-soluble alkali salts. Other accompaniments As an additive, organic phosphonic acids, particularly ethylene diamino tetramethylene are preferred. Pentamethylene phosphonic acid, diethylenetriamino, pentamethylene phosphonic acid and amino Trimethylenephosphonic acid is mentioned.

Example A composition of the invention was prepared by mixing the ingredients in the following proportions.

Φ1,2-Propanediol 23312-NaOI (688111) Amylase (143KNU/g) 0.1 0.1 0.05 0.2 0. to Ribolase R (100KLU/g commercial solution) 0.4 0.2 0.3 0J O,3・P E M 15 R (50 mg/g commercially available solution) 0.3 0 0 0 0.4・Du r az ymR (39 g/g commercially available solution) 00.200 0.0pticlean M222CR (experimental sample) 0 0.1 0 0.4 0-0ptosase M222cR (experimental sample) 0 0 0.3 0 0 ・Sodium formate salt oooo.

Example A composition of the invention was prepared by mixing the ingredients in the following proportions.

llNaCl2-15 alkyl sulfate 5 21.75 0 3・CI2 Glucoseamide 60700' Cl2-15 Flucol 7x Ethoxy Ii -to0 0 0.5 0 11.8・C12-15 alcohol 5 times ethoxylate 0808-Oleic acid 0 0 0 3.5 2.5 Citric acid 10 9 9.5 4 1' Kenyl-substituted succinic acid in Cl2-147 11 011.5 0 0-5 TPP 020 0 0 0 ・Zeolite 000260 ・Ethanol 64436 ・1,2-Propanediol 3 2 2 2 1.5-NaOH999,89 3J ・Amylase (143KNU/g) 0.2 0.1 0.2 0.05 Tori Borase R (100KLU/g commercial solution) 0.5 0.5 0.3 0.2 0.3-optIclean M222CR (*Iil sample) 0 0 0 Q , 3 0-Optoao-0ptoaase Experimental Trial 11) 0 0.5 0 o O・CaCl20-01 0.01 0.02 0.02 0.01・Na meta Borate 42430 -TEA 0 0 0 0 6 ・Sodium formate salt 00001 ・Fatty acids 000012 ・Water and others...Remaining amount up to 100%...Example A composition of the invention was prepared by mixing the ingredients in the following proportions.

1 top 12 Yu 1141Σ ・Linear alkylbenzene 579810 ・Citric acid 10 9 9.5 4 1 and jetoxylated poly(1,2-7° and lenterephthalate) 1.0 0.5 0.7 0 0.5・Ethanol 64436 -1.2-Propanediol 3 2 2 2 1.5・NaOH999,89 3,5 ・Diethylenetriaminepenta(methylenephosphone II) 1.0 1.0 1 ．． 0 0.5 0.8 Amylase (143KNU/g) 0.2 0.1 0.2 0.05 Tripolase R (100KLU/g commercial solution) 0.5 0 ．． 5 0.3 0.2 0.3 PEM15R (50 g/g commercial solution>0 ．． 4　0　　　0　0.2・Du r az ym” (39 mg/g commercially available) solution) 0 0 0.5 0 0.2ψ0ptlclean M222CR (actual Test sample) 0 0 0 0.3 0・OptO1aSeM222CR (Experiment sample ＞　0　0.5　0　0　0・TEA　0　0　0　0　6 ・Sodium formate salt 00001 ・Fatty acids 000.012 ・Water and others...remaining amount up to 100%...Procedure amendment (method) February 1994 7a Dengai Director General of the Patent Office 1 Display of incident 1992 Original Patent No. 500878 PC/US 91108041 , name of invention 3 Person making the amendment Relationship to the case: Patent applicant international search report Continuation of front page (81) Designated countries 0A (BF, BJ, CF, CG.

CI, CM, GA, GN, ML, MR, SN, TD, TG), AT, AU, BB, BG, BR, CA, CH, C3, DE, DK, ES, FI, GB, HU, JP, KP, KR, LK, LU, MC, MG, MN , MW, NL.

No, PL, RO, SD, SE, SU, US (72) Inventor Tuan, Qu Listiaan Arthur Jacques Camiel Belgium, Haastonk, Bekwaitfustraat, 4

Claims (11)

[Claims] 1. Enzyme systems consisting of lipases or mixtures thereof and proteases and known A liquid detergent composition comprising a detergent component, wherein the protease Bacterial serine proteases in which the methionine adjacent to the methionine is replaced with another amino acid or a mixture of said proteases. 2. A liquid detergent composition according to claim 1, wherein the lipase is LIPOLASER. thing. 3. An amount such that the lipolysis units per gram of the final product are between 0.1 and 10,000. The detergent composition according to claim 1 or 2, comprising a lipase. 4. The active protease per gram of the final product should be between 0.005 and 10 mg. 4. The protease according to claims 1 to 3, comprising the protease or the mixture thereof in an amount of A detergent composition according to any one of the items. 5. Modified bacterial serine protease MAXAPEM15R, DURAZYMR, M222COPTICLEANR and M222COPTIMASER, or a mixture thereof. , the detergent composition according to any one of claims 1 to 4. 6. The detergent according to any one of claims 1 to 5, further comprising amylase. Composition. 7. The detergent set according to any one of claims 1 to 6, further comprising an enzyme stabilizing system. A product. 8. 8. The enzyme stabilizing system is boric acid at 0.05-5% by weight of the total composition. Detergent compositions. 9. Enzyme stabilization system contains 1,2-propanediol and/or carboxylic acids. and a mixture thereof. 10. The detergent composition according to any one of claims 1 to 9, having a pH of 6 to 10. 11. The detergent according to any one of claims 1 to 10, having a pH of 7.0 to 8.5. Composition.