EP0271153A2 - Enzyme enthaltendes Reinigungsmittel - Google Patents
Enzyme enthaltendes Reinigungsmittel Download PDFInfo
- Publication number
- EP0271153A2 EP0271153A2 EP87202385A EP87202385A EP0271153A2 EP 0271153 A2 EP0271153 A2 EP 0271153A2 EP 87202385 A EP87202385 A EP 87202385A EP 87202385 A EP87202385 A EP 87202385A EP 0271153 A2 EP0271153 A2 EP 0271153A2
- Authority
- EP
- European Patent Office
- Prior art keywords
- lipase
- lipases
- detergent
- pseudomonas
- detergent composition
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 35
- 239000003599 detergent Substances 0.000 title claims abstract description 29
- 230000002255 enzymatic effect Effects 0.000 title description 2
- 239000004367 Lipase Substances 0.000 claims abstract description 48
- 102000004882 Lipase Human genes 0.000 claims abstract description 47
- 108090001060 Lipase Proteins 0.000 claims abstract description 47
- 235000019421 lipase Nutrition 0.000 claims abstract description 47
- 108091005804 Peptidases Proteins 0.000 claims abstract description 22
- 239000004365 Protease Substances 0.000 claims abstract description 20
- 102000035195 Peptidases Human genes 0.000 claims abstract description 18
- 230000002366 lipolytic effect Effects 0.000 claims abstract description 8
- 230000002797 proteolythic effect Effects 0.000 claims description 6
- 230000037029 cross reaction Effects 0.000 claims description 4
- 230000001900 immune effect Effects 0.000 claims description 4
- 239000004094 surface-active agent Substances 0.000 claims description 3
- 241000589513 Burkholderia cepacia Species 0.000 claims description 2
- 241000589540 Pseudomonas fluorescens Species 0.000 claims description 2
- 241000589538 Pseudomonas fragi Species 0.000 claims description 2
- 241000204735 Pseudomonas nitroreducens Species 0.000 claims description 2
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims description 2
- 241000145542 Pseudomonas marginata Species 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 abstract description 9
- 108090000790 Enzymes Proteins 0.000 abstract description 9
- 229940088598 enzyme Drugs 0.000 description 8
- 239000000427 antigen Substances 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 238000000034 method Methods 0.000 description 6
- 239000002671 adjuvant Substances 0.000 description 5
- 239000000271 synthetic detergent Substances 0.000 description 5
- 241001135516 Burkholderia gladioli Species 0.000 description 4
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 4
- 108010056079 Subtilisins Proteins 0.000 description 4
- 102000005158 Subtilisins Human genes 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 239000011149 active material Substances 0.000 description 3
- 239000007844 bleaching agent Substances 0.000 description 3
- 235000014113 dietary fatty acids Nutrition 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000000839 emulsion Substances 0.000 description 3
- 239000000194 fatty acid Substances 0.000 description 3
- 229930195729 fatty acid Natural products 0.000 description 3
- 150000004665 fatty acids Chemical class 0.000 description 3
- 108010020132 microbial serine proteinases Proteins 0.000 description 3
- 239000002689 soil Substances 0.000 description 3
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 125000002947 alkylene group Chemical group 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- JEGUKCSWCFPDGT-UHFFFAOYSA-N h2o hydrate Chemical compound O.O JEGUKCSWCFPDGT-UHFFFAOYSA-N 0.000 description 2
- 235000019626 lipase activity Nutrition 0.000 description 2
- 108010003855 mesentericopeptidase Proteins 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 244000215068 Acacia senegal Species 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 241000146387 Chromobacterium viscosum Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 229920000084 Gum arabic Polymers 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 241000364057 Peoria Species 0.000 description 1
- GOOHAUXETOMSMM-UHFFFAOYSA-N Propylene oxide Chemical compound CC1CO1 GOOHAUXETOMSMM-UHFFFAOYSA-N 0.000 description 1
- 241000589774 Pseudomonas sp. Species 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 239000004115 Sodium Silicate Substances 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 239000004904 UV filter Substances 0.000 description 1
- 239000000205 acacia gum Substances 0.000 description 1
- 235000010489 acacia gum Nutrition 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- -1 bars Substances 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000007859 condensation product Substances 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 150000002191 fatty alcohols Chemical class 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- HWGNBUXHKFFFIH-UHFFFAOYSA-I pentasodium;[oxido(phosphonatooxy)phosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O HWGNBUXHKFFFIH-UHFFFAOYSA-I 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- 239000003208 petroleum Substances 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000003352 sequestering agent Substances 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- FRPJTGXMTIIFIT-UHFFFAOYSA-N tetraacetylethylenediamine Chemical compound CC(=O)C(N)(C(C)=O)C(N)(C(C)=O)C(C)=O FRPJTGXMTIIFIT-UHFFFAOYSA-N 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
Classifications
-
- 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
Definitions
- the present invention relates to an enzymatic detergent composition
- an enzymatic detergent composition comprising as detergent active material solely a nonionic synthetic detergent, and a mixture of lipolytic and proteolytic enzymes.
- Lipolytic enzymes are well known in detergent compositions. Lipolytic enzymes have been mentioned in the prior art as possible enzymes for detergent compositions, but there is relatively little prior art directly concerned with lipases for inclusion in detergent compositions.
- nonionic synthetic detergents in general do not negatively influence the activity of proteolytic and lipolytic enzymes, in contrast with e.g. anionic synthetic detergents, which often negatively influence the proteases and lipases.
- lipases are basically proteins, they would be susceptible to proteolytic action by the proteases if lipases were used in conjunction with proteases. It would therefore be expected that the inclusion of proteases in a detergent composition comprising lipases and as detergent-active material solely a nonionic detergent surfactant (which does not affect either the lipase or the protease), would cause the lipase activity to be destroyed by the proteolytic action of the proteases.
- the class of lipases to be used according to the present invention embraces those lipases which show a positive immunological cross-reaction with the antibody of the lipase produced by the microorganism Chromobacter viscosum var. lipolyticum NRRL B 3673.
- This lipase has been described in Dutch Patent Specification 154,269 of Toyo Jozo KK, and the microorganism is available to the public from the collection of the United States Department of Agriculture, Agricultural Research Service, Northern Utilization and Development Division, Peoria, Illinois, under N o NRRL B 3673.
- This lipase will be referred to hereinafter as "Toyo Jozo" lipase.
- the lipases of the present invention should show a positive immunological cross-reaction with the Toyo Jozo lipase antibody, using the standard and well-known immunodiffusion procedure according to Ouchterlony (Acta. Med. Scan., 133 , pages 76-79 (1950)).
- the preparation of the antiserum is carried out as follows: Equal volumes of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an emulsion is obtained. Two female rabbits are injected with 2 ml samples of the emulsion according to the following scheme: day 0 : antigen in complete Freund's adjuvant day 4 : antigen in complete Freund's adjuvant day 32 : antigen in incomplete Freund's adjuvant day 60 : booster of antigen in incomplete Freund's adjuvant.
- the serum containing the required antibody is prepared by centrifugation of clotted blood, taken on day 67.
- the titre of the anti-Toyo Jozo-lipase antiserum is determined by the inspection of precipitation of serial dilutions of antigen and antiserum according to the Ouchterlony procedure. A 25 dilution of antiserum was the dilution that still gave a visible precipitation with an antigen concentration of 0.1 mg/ml.
- lipases showing a positive immunological cross-reaction with the Toyo Jozo lipase antibody as hereabove described are lipases according to the present invention. Typical examples thereof are the lipase ex Pseudomonas fluorescens IAM 1057 (available under the trade name Amano-P), the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade name Amano-B), lipase ex Pseudomonas nitroreducens var. lipolyticum FERM P 1338, the lipase ex Pseudomonas sp.
- the lipase ex Pseudomonas fluorescens IAM 1057 available under the trade name Amano-P
- the lipase ex Pseudomonas fragi FERM P 1339 available under the trade name Amano-B
- lipases ex Chromobacter viscosum , e.g. Chromobacter viscosum var. lipolyticum NRRL B 3673, commercially available from Toyo Jozo Co., Tagata, Japan; and further C . viscosum lipases from US Biochemical Corp., U.S.A., and Diosynth Co., The Netherlands, and lipases ex Pseudomonas gladioli .
- the lipases of the present invention are included in the detergent composition in such an amount that the final detergent composition has a lipolytic enzyme activity of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition.
- lipases can be used in their non-purified form or in a purified form, e.g. purified with the aid of well-known adsorption methods, such as phenyl sepharose adsorption techniques.
- proteases used according to the present invention are the well-known detergent proteases and mixtures thereof.
- the proteases are used in such an amount that the final detergent composition has a proteolytic activity of 0.1 to 50 GU/mg, preferably 0.5 to 30 GU/mg.
- GU Glycine Unit; one GU is the amount of enzyme which under standard incubation conditions produces an amount of terminal NH2-groups equivalent to 1 microgr./ml glycine.
- the detergent composition further comprises as detergent-active material solely a nonionic synthetic detergent.
- This type of detergent is well known in the art.
- Nonionics usually consist of a hydrophobic moiety derived from fatty alcohols, fatty acid amides and alkylphenols, and a hydrophilic moiety consisting of alkylene oxide units. Typical examples are the condensation products of alkylene oxides such as ethylene oxide, propylene oxide and butylene oxide and mixtures thereof with C8-C18 primary or secondary, branched or straight chain alcohols, C8-C18 fatty acid amides, C9-C18 alkylphenols, etc. Further suitable examples are given in M. Schick "Nonionic surfactants" (1967).
- the composition contains from 1-50%, usually from 2-45%, and commonly from 5-30% by weight of the nonionic detergent. Mixtures of various nonionic detergents may also be used.
- the detergent composition may furthermore include the usual detergent ingredients in the usual amounts.
- the composition may contain from 1-60%, preferably from 5-30% by weight of one or more organic and/or inorganic builders. Furthermore, it may contain from 1-35% of a bleaching agent or a bleaching system comprising a bleaching agent and an activator therefor, e.g. sodium perborate with tetraacetyl ethylene diamine.
- compositions may furthermore comprise lather boosters, foam depressors, anti-corrosion agents, soil-suspending agents, sequestering agents, anti-soil redeposition agents, perfumes, dyes, solvents, stabilising agents for the enzymes and bleaching agents and so on. They may also comprise from 0.01-10% by weight of enzymes other than lipases and proteases, such as amylases, oxidases and cellulases.
- compositions of the present invention can be formulated in any desired form, such as powders, bars, pastes, liquids, etc.
- washing experiments were carried out in a Tergotometer under the following conditions: wash time and temperature: 10 minutes at 40°C; three rinses with cold water water hardness: 14 and 40°FH detergent composition concentration: 2 and 6 g/l number soil/wash cycles : 4 protease concentration: 20 GU/ml lipase concentration: 1 LU/ml As lipases were used: Amano-P, Diosynth and a lipase ex Pseudomonas gladioli The detergent composition used had the following formulation:
- the reflectance of the test cloths and the residual weight percentage of fatty material on the test cloths were determined after the fourth wash cycle.
- the reflectance was measured in a Reflectometer at 460 nm with a UV filter in the light pathway, and the fatty matter by extracting the dried test cloths with petroleum ether, and determining the amount of fatty matter from the weight loss of the test cloth.
- Example 1 The procedure of Example 1 was repeated, but under the following conditions: detergent composition concentration: 2 g/l number of soil/wash cycles : 4 wash time and temperature: 10 minutes at 40°C, three rinses with cold water water hardness: 14°FH agitation: 100 rpm lipase: ex Pseudomonas gladioli 1 LU/ml protease: 20 GU/ml As proteases, Savinase, Alcalase, Maxatase, Maxacal, Kazuzase and Esperase were used.
- the stability of lipases according to the present invention in the presence of proteases and varying amounts of a nonionic detergent was tested by determining the residual lipase activity with the pH-stat. method.
- a composition comprising 0.7 g pentasodium triphosphate, 0.7 g sodium sulphate and 0.2 sodium silicate and varying amounts of C13-C15 alcohol, condensed with 7 and 3 moles of ethylene oxide, respectively (product A and product B) was used.
- the temperature was 30°C, the water hardness 14°FH and the pH 9.5.
- the lipase was either lipase ex Pseudomonas gladioli , or Amano-P, at 15 LU/ml, and the protease was Savinase, at 20 GU/ml.
- Example 1 was repeated, using various lipases. The following results were obtained:
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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)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB868629535A GB8629535D0 (en) | 1986-12-10 | 1986-12-10 | Enzymatic detergent composition |
GB8629535 | 1986-12-10 |
Publications (3)
Publication Number | Publication Date |
---|---|
EP0271153A2 true EP0271153A2 (de) | 1988-06-15 |
EP0271153A3 EP0271153A3 (en) | 1988-08-10 |
EP0271153B1 EP0271153B1 (de) | 1990-03-14 |
Family
ID=10608785
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP87202385A Expired - Lifetime EP0271153B1 (de) | 1986-12-10 | 1987-12-02 | Enzyme enthaltendes Reinigungsmittel |
Country Status (9)
Country | Link |
---|---|
EP (1) | EP0271153B1 (de) |
JP (1) | JPH0696717B2 (de) |
AU (1) | AU605806B2 (de) |
BR (1) | BR8706682A (de) |
CA (1) | CA1288368C (de) |
DE (1) | DE3761910D1 (de) |
ES (1) | ES2014465B3 (de) |
GB (1) | GB8629535D0 (de) |
ZA (1) | ZA879296B (de) |
Cited By (14)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1989004361A1 (en) * | 1987-11-02 | 1989-05-18 | Novo-Nordisk A/S | Enzymatic detergent composition |
EP0368589A2 (de) * | 1988-11-08 | 1990-05-16 | Unilever Plc | Enzymhaltige Waschmittel |
US4933287A (en) * | 1985-08-09 | 1990-06-12 | Gist-Brocades N.V. | Novel lipolytic enzymes and their use in detergent compositions |
US4950417A (en) * | 1989-05-01 | 1990-08-21 | Miles Inc. | Detergent formulations containing alkaline lipase derived from Pseudomonas plantarii |
WO1990009440A1 (en) * | 1989-02-20 | 1990-08-23 | Novo Nordisk A/S | Enzyme containing granulate and method for production thereof |
EP0407225A1 (de) * | 1989-07-07 | 1991-01-09 | Unilever Plc | Enzyme und enzymhaltiges Reinigungsmittel |
US5100796A (en) * | 1988-02-22 | 1992-03-31 | Synfina-Oleofina | Methods for producing a new pseudomonas lipase and protease and detergent washing compositions containing same |
WO1994007984A1 (en) * | 1992-09-25 | 1994-04-14 | The Procter & Gamble Company | Detergent composition comprising lime soap dispersant and lipase enzymes |
WO1994007985A1 (en) * | 1992-09-25 | 1994-04-14 | The Procter & Gamble Company | Detergent composition comprising lime soap dispersant and lipase enzymes |
US5658871A (en) * | 1989-07-07 | 1997-08-19 | Lever Brothers Company, Division Of Conopco, Inc. | Microbial lipase muteins and detergent compositions comprising same |
US5733763A (en) * | 1988-08-19 | 1998-03-31 | Novo Nordisk A/S | Enzyme granulate formed of an enzyme-containing core and an enzyme-containing shell |
US5772786A (en) * | 1993-08-13 | 1998-06-30 | The Procter & Gamble Company | Detergent composition comprising lime soap dispersant and lipase enzymes |
DE19954181A1 (de) * | 1999-11-10 | 2001-05-31 | Eppendorf Geraetebau Netheler | Verwendung nichtionogener Tenside zur Durchführung enzymatischer Reaktionen |
CN110804506A (zh) * | 2019-11-13 | 2020-02-18 | 领先生物农业股份有限公司 | 一种微生物毛洗涤剂及其使用方法 |
Families Citing this family (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB8629536D0 (en) * | 1986-12-10 | 1987-01-21 | Unilever Plc | Enzymatic detergent composition |
JPH0489897A (ja) * | 1990-07-30 | 1992-03-24 | Solvay Enzyme Prod Inc | アルカリ性リパーゼを含む洗剤配合物 |
WO2011080835A1 (ja) | 2009-12-28 | 2011-07-07 | トヨタ自動車株式会社 | 車両用フード構造 |
Citations (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE1930636A1 (de) * | 1968-06-24 | 1970-07-09 | Albright & Wilson | Reinigungsmittel |
DE1767413A1 (de) * | 1967-08-14 | 1971-09-09 | Henkel & Cie Gmbh | Als Textilwaschmittel brauchbare Tensidkombinationen sowie diese enthaltende Wasch- oder Waschhilfsmittel |
EP0130064A1 (de) * | 1983-06-23 | 1985-01-02 | Novo Nordisk A/S | Enzymatischer Detergens-Zusatz, ein Detergens und ein Waschverfahren |
EP0205208A2 (de) * | 1985-06-11 | 1986-12-17 | Unilever N.V. | Enzymhaltiges Reinigungsmittel |
EP0206390A2 (de) * | 1985-06-11 | 1986-12-30 | Unilever N.V. | Enzymhaltiges Reinigungsmittel |
EP0214761A2 (de) * | 1985-08-07 | 1987-03-18 | Novo Nordisk A/S | Enzymatischer Reinigungsmittelzusatz, Reinigungsmittel und Waschverfahren |
Family Cites Families (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB8629536D0 (en) * | 1986-12-10 | 1987-01-21 | Unilever Plc | Enzymatic detergent composition |
-
1986
- 1986-12-10 GB GB868629535A patent/GB8629535D0/en active Pending
-
1987
- 1987-12-02 ES ES87202385T patent/ES2014465B3/es not_active Expired - Lifetime
- 1987-12-02 EP EP87202385A patent/EP0271153B1/de not_active Expired - Lifetime
- 1987-12-02 DE DE8787202385T patent/DE3761910D1/de not_active Expired - Fee Related
- 1987-12-08 AU AU82226/87A patent/AU605806B2/en not_active Ceased
- 1987-12-08 CA CA000553755A patent/CA1288368C/en not_active Expired - Fee Related
- 1987-12-09 JP JP62311792A patent/JPH0696717B2/ja not_active Expired - Lifetime
- 1987-12-09 BR BR8706682A patent/BR8706682A/pt not_active IP Right Cessation
- 1987-12-10 ZA ZA879296A patent/ZA879296B/xx unknown
Patent Citations (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE1767413A1 (de) * | 1967-08-14 | 1971-09-09 | Henkel & Cie Gmbh | Als Textilwaschmittel brauchbare Tensidkombinationen sowie diese enthaltende Wasch- oder Waschhilfsmittel |
DE1930636A1 (de) * | 1968-06-24 | 1970-07-09 | Albright & Wilson | Reinigungsmittel |
EP0130064A1 (de) * | 1983-06-23 | 1985-01-02 | Novo Nordisk A/S | Enzymatischer Detergens-Zusatz, ein Detergens und ein Waschverfahren |
EP0205208A2 (de) * | 1985-06-11 | 1986-12-17 | Unilever N.V. | Enzymhaltiges Reinigungsmittel |
EP0206390A2 (de) * | 1985-06-11 | 1986-12-30 | Unilever N.V. | Enzymhaltiges Reinigungsmittel |
EP0214761A2 (de) * | 1985-08-07 | 1987-03-18 | Novo Nordisk A/S | Enzymatischer Reinigungsmittelzusatz, Reinigungsmittel und Waschverfahren |
Cited By (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4933287A (en) * | 1985-08-09 | 1990-06-12 | Gist-Brocades N.V. | Novel lipolytic enzymes and their use in detergent compositions |
WO1989004361A1 (en) * | 1987-11-02 | 1989-05-18 | Novo-Nordisk A/S | Enzymatic detergent composition |
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US5733763A (en) * | 1988-08-19 | 1998-03-31 | Novo Nordisk A/S | Enzyme granulate formed of an enzyme-containing core and an enzyme-containing shell |
EP0368589A3 (de) * | 1988-11-08 | 1990-10-31 | Unilever Plc | Enzymhaltige Waschmittel |
EP0368589A2 (de) * | 1988-11-08 | 1990-05-16 | Unilever Plc | Enzymhaltige Waschmittel |
WO1990009440A1 (en) * | 1989-02-20 | 1990-08-23 | Novo Nordisk A/S | Enzyme containing granulate and method for production thereof |
US4950417A (en) * | 1989-05-01 | 1990-08-21 | Miles Inc. | Detergent formulations containing alkaline lipase derived from Pseudomonas plantarii |
US5658871A (en) * | 1989-07-07 | 1997-08-19 | Lever Brothers Company, Division Of Conopco, Inc. | Microbial lipase muteins and detergent compositions comprising same |
EP0407225A1 (de) * | 1989-07-07 | 1991-01-09 | Unilever Plc | Enzyme und enzymhaltiges Reinigungsmittel |
WO1991000910A1 (en) * | 1989-07-07 | 1991-01-24 | Unilever Plc | Enzymes and enzymatic detergent compositions |
WO1994007985A1 (en) * | 1992-09-25 | 1994-04-14 | The Procter & Gamble Company | Detergent composition comprising lime soap dispersant and lipase enzymes |
WO1994007984A1 (en) * | 1992-09-25 | 1994-04-14 | The Procter & Gamble Company | Detergent composition comprising lime soap dispersant and lipase enzymes |
US5772786A (en) * | 1993-08-13 | 1998-06-30 | The Procter & Gamble Company | Detergent composition comprising lime soap dispersant and lipase enzymes |
DE19954181A1 (de) * | 1999-11-10 | 2001-05-31 | Eppendorf Geraetebau Netheler | Verwendung nichtionogener Tenside zur Durchführung enzymatischer Reaktionen |
CN110804506A (zh) * | 2019-11-13 | 2020-02-18 | 领先生物农业股份有限公司 | 一种微生物毛洗涤剂及其使用方法 |
CN110804506B (zh) * | 2019-11-13 | 2021-06-01 | 领先生物农业股份有限公司 | 一种微生物毛洗涤剂及其使用方法 |
Also Published As
Publication number | Publication date |
---|---|
EP0271153B1 (de) | 1990-03-14 |
AU605806B2 (en) | 1991-01-24 |
ES2014465B3 (es) | 1990-07-16 |
ZA879296B (en) | 1989-08-30 |
BR8706682A (pt) | 1988-07-19 |
JPS63161084A (ja) | 1988-07-04 |
EP0271153A3 (en) | 1988-08-10 |
CA1288368C (en) | 1991-09-03 |
AU8222687A (en) | 1988-06-16 |
GB8629535D0 (en) | 1987-01-21 |
DE3761910D1 (de) | 1990-04-19 |
JPH0696717B2 (ja) | 1994-11-30 |
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