EP0271153A2 - Enzymatic detergent composition - Google Patents
Enzymatic detergent composition 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
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:
Landscapes
- 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
Description
- The present invention relates to an enzymatic detergent composition comprising as detergent active material solely a nonionic synthetic detergent, and a mixture of lipolytic and proteolytic enzymes.
- Proteolytic 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.
- Insofar the compatibility of proteolytic and lipolytic enzymes with synthetic detergents is concerned, it is well known that 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.
- However, since 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.
- We have now surprisingly found that when using such compositions comprising a special class of lipases, hereinafter more specifically defined, this expected loss of lipolytic activity does not occur, but that, the activity of these lipases remains almost unaffected by the presence of the proteases in these compositions.
- 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 No 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.
- All 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. available under the trade name Amano-CES, lipase ex Pseudomonas cepacia, 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.
- A Lipase Unit (LU) is that amount of lipase which produces 1µmol of titratable fatty acid per minute in a pH stat. under the following conditions: temperature 30°C; pH = 9.0; substrate is an emulsion of 3.3 wt.% of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca²⁺ and 20 mmol/l NaCl in 5 mmol/l Tris-buffer.
- Naturally, mixtures of the above lipases can be used. The 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.
- The proteases used according to the present invention are the well-known detergent proteases and mixtures thereof. Typical examples are the subtilisin type proteases, such as Alcalase, Esperase, Savinase, all available from Novo Industri A/S, Maxatase and Maxacal, both available from Gist Brocades N.Y., Kazuzase ex Showa Denko. (= API-21 = AP-1)
- In general, 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).
- In general, 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. Thus, 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.
- The 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.
- The compositions of the present invention can be formulated in any desired form, such as powders, bars, pastes, liquids, etc.
- The invention will now further be illustrated by way of Examples.
- 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 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.
-
- 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.
-
-
Claims (2)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB8629535 | 1986-12-10 | ||
GB868629535A GB8629535D0 (en) | 1986-12-10 | 1986-12-10 | Enzymatic detergent composition |
Publications (3)
Publication Number | Publication Date |
---|---|
EP0271153A2 true EP0271153A2 (en) | 1988-06-15 |
EP0271153A3 EP0271153A3 (en) | 1988-08-10 |
EP0271153B1 EP0271153B1 (en) | 1990-03-14 |
Family
ID=10608785
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP87202385A Expired - Lifetime EP0271153B1 (en) | 1986-12-10 | 1987-12-02 | Enzymatic detergent composition |
Country Status (9)
Country | Link |
---|---|
EP (1) | EP0271153B1 (en) |
JP (1) | JPH0696717B2 (en) |
AU (1) | AU605806B2 (en) |
BR (1) | BR8706682A (en) |
CA (1) | CA1288368C (en) |
DE (1) | DE3761910D1 (en) |
ES (1) | ES2014465B3 (en) |
GB (1) | GB8629535D0 (en) |
ZA (1) | ZA879296B (en) |
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 (en) * | 1988-11-08 | 1990-05-16 | Unilever Plc | Enzyme-containing detergent compositions |
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 (en) * | 1989-07-07 | 1991-01-09 | Unilever Plc | Enzymes and enzymatic detergent compositions |
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 (en) * | 1999-11-10 | 2001-05-31 | Eppendorf Geraetebau Netheler | Use of non-ionic surfactants to carry out enzymatic reactions |
CN110804506A (en) * | 2019-11-13 | 2020-02-18 | 领先生物农业股份有限公司 | Microbial wool detergent and using method thereof |
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 (en) * | 1990-07-30 | 1992-03-24 | Solvay Enzyme Prod Inc | Detergent compound containing alkaline lipase |
EP2529998B1 (en) | 2009-12-28 | 2016-03-30 | Toyota Jidosha Kabushiki Kaisha | Hood structure of vehicle |
Citations (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE1930636A1 (en) * | 1968-06-24 | 1970-07-09 | Albright & Wilson | cleaning supplies |
DE1767413A1 (en) * | 1967-08-14 | 1971-09-09 | Henkel & Cie Gmbh | Surfactant combinations which can be used as laundry detergents and detergents or auxiliary washing agents containing them |
EP0130064A1 (en) * | 1983-06-23 | 1985-01-02 | Novo Nordisk A/S | Improvements in and relating to an enzymatic detergent additive, a detergent, and a washing method |
EP0205208A2 (en) * | 1985-06-11 | 1986-12-17 | Unilever N.V. | Enzymatic detergent composition |
EP0206390A2 (en) * | 1985-06-11 | 1986-12-30 | Unilever N.V. | Enzymatic detergent composition |
EP0214761A2 (en) * | 1985-08-07 | 1987-03-18 | Novo Nordisk A/S | An enzymatic detergent additive, a detergent, and a washing method |
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 EP EP87202385A patent/EP0271153B1/en not_active Expired - Lifetime
- 1987-12-02 ES ES87202385T patent/ES2014465B3/en not_active Expired - Lifetime
- 1987-12-02 DE DE8787202385T patent/DE3761910D1/en not_active Expired - Fee Related
- 1987-12-08 CA CA000553755A patent/CA1288368C/en not_active Expired - Fee Related
- 1987-12-08 AU AU82226/87A patent/AU605806B2/en not_active Ceased
- 1987-12-09 BR BR8706682A patent/BR8706682A/en not_active IP Right Cessation
- 1987-12-09 JP JP62311792A patent/JPH0696717B2/en not_active Expired - Lifetime
- 1987-12-10 ZA ZA879296A patent/ZA879296B/en unknown
Patent Citations (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE1767413A1 (en) * | 1967-08-14 | 1971-09-09 | Henkel & Cie Gmbh | Surfactant combinations which can be used as laundry detergents and detergents or auxiliary washing agents containing them |
DE1930636A1 (en) * | 1968-06-24 | 1970-07-09 | Albright & Wilson | cleaning supplies |
EP0130064A1 (en) * | 1983-06-23 | 1985-01-02 | Novo Nordisk A/S | Improvements in and relating to an enzymatic detergent additive, a detergent, and a washing method |
EP0205208A2 (en) * | 1985-06-11 | 1986-12-17 | Unilever N.V. | Enzymatic detergent composition |
EP0206390A2 (en) * | 1985-06-11 | 1986-12-30 | Unilever N.V. | Enzymatic detergent composition |
EP0214761A2 (en) * | 1985-08-07 | 1987-03-18 | Novo Nordisk A/S | An enzymatic detergent additive, a detergent, and a washing method |
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 |
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 |
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 (en) * | 1988-11-08 | 1990-10-31 | Unilever Plc | Enzyme-containing detergent compositions |
EP0368589A2 (en) * | 1988-11-08 | 1990-05-16 | Unilever Plc | Enzyme-containing detergent compositions |
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 (en) * | 1989-07-07 | 1991-01-09 | Unilever Plc | Enzymes and enzymatic detergent compositions |
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 (en) * | 1999-11-10 | 2001-05-31 | Eppendorf Geraetebau Netheler | Use of non-ionic surfactants to carry out enzymatic reactions |
CN110804506A (en) * | 2019-11-13 | 2020-02-18 | 领先生物农业股份有限公司 | Microbial wool detergent and using method thereof |
CN110804506B (en) * | 2019-11-13 | 2021-06-01 | 领先生物农业股份有限公司 | Microbial wool detergent and using method thereof |
Also Published As
Publication number | Publication date |
---|---|
GB8629535D0 (en) | 1987-01-21 |
JPH0696717B2 (en) | 1994-11-30 |
AU8222687A (en) | 1988-06-16 |
CA1288368C (en) | 1991-09-03 |
DE3761910D1 (en) | 1990-04-19 |
AU605806B2 (en) | 1991-01-24 |
JPS63161084A (en) | 1988-07-04 |
BR8706682A (en) | 1988-07-19 |
ZA879296B (en) | 1989-08-30 |
EP0271153A3 (en) | 1988-08-10 |
EP0271153B1 (en) | 1990-03-14 |
ES2014465B3 (en) | 1990-07-16 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
EP0206390B1 (en) | Enzymatic detergent composition | |
US4824599A (en) | Enzymatic detergent composition | |
EP0271153B1 (en) | Enzymatic detergent composition | |
EP0205208B1 (en) | Enzymatic detergent composition | |
EP0381262B1 (en) | Enzymatic liquid detergent composition | |
EP0271152B1 (en) | Enzymatic detergent and bleaching composition | |
US5089163A (en) | Enzymatic liquid detergent composition | |
US5484555A (en) | Method for creating a pH jump system | |
EP0271155B1 (en) | Enzymatic dishwashing and rinsing process | |
US4511490A (en) | Cooperative enzymes comprising alkaline or mixtures of alkaline and neutral proteases without stabilizers | |
EP0271156B1 (en) | Enzymatic dishwashing composition | |
AU616780B2 (en) | Enzymatic dishwashing composition | |
US4861509A (en) | Enzymatic detergent and bleaching composition |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PUAI | Public reference made under article 153(3) epc to a published international application that has entered the european phase |
Free format text: ORIGINAL CODE: 0009012 |
|
AK | Designated contracting states |
Kind code of ref document: A2 Designated state(s): CH DE ES FR GB IT LI NL SE |
|
PUAL | Search report despatched |
Free format text: ORIGINAL CODE: 0009013 |
|
AK | Designated contracting states |
Kind code of ref document: A3 Designated state(s): CH DE ES FR GB IT LI NL SE |
|
17P | Request for examination filed |
Effective date: 19880711 |
|
17Q | First examination report despatched |
Effective date: 19890302 |
|
GRAA | (expected) grant |
Free format text: ORIGINAL CODE: 0009210 |
|
AK | Designated contracting states |
Kind code of ref document: B1 Designated state(s): CH DE ES FR GB IT LI NL SE |
|
REF | Corresponds to: |
Ref document number: 3761910 Country of ref document: DE Date of ref document: 19900419 |
|
ITF | It: translation for a ep patent filed |
Owner name: JACOBACCI & PERANI S.P.A. |
|
ET | Fr: translation filed | ||
PLBE | No opposition filed within time limit |
Free format text: ORIGINAL CODE: 0009261 |
|
STAA | Information on the status of an ep patent application or granted ep patent |
Free format text: STATUS: NO OPPOSITION FILED WITHIN TIME LIMIT |
|
26N | No opposition filed | ||
ITTA | It: last paid annual fee | ||
EAL | Se: european patent in force in sweden |
Ref document number: 87202385.8 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: SE Payment date: 19951121 Year of fee payment: 9 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: CH Payment date: 19951201 Year of fee payment: 9 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: NL Payment date: 19951220 Year of fee payment: 9 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: SE Effective date: 19961203 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: LI Effective date: 19961231 Ref country code: CH Effective date: 19961231 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: NL Effective date: 19970701 |
|
REG | Reference to a national code |
Ref country code: CH Ref legal event code: PL |
|
NLV4 | Nl: lapsed or anulled due to non-payment of the annual fee |
Effective date: 19970701 |
|
EUG | Se: european patent has lapsed |
Ref document number: 87202385.8 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: ES Payment date: 20011218 Year of fee payment: 15 |
|
REG | Reference to a national code |
Ref country code: GB Ref legal event code: IF02 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: FR Payment date: 20021119 Year of fee payment: 16 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: GB Payment date: 20021127 Year of fee payment: 16 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: ES Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20021203 |
|
PGFP | Annual fee paid to national office [announced via postgrant information from national office to epo] |
Ref country code: DE Payment date: 20021230 Year of fee payment: 16 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: GB Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20031202 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: DE Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20040701 |
|
GBPC | Gb: european patent ceased through non-payment of renewal fee |
Effective date: 20031202 |
|
REG | Reference to a national code |
Ref country code: ES Ref legal event code: FD2A Effective date: 20021203 |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: FR Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES Effective date: 20040831 |
|
REG | Reference to a national code |
Ref country code: FR Ref legal event code: ST |
|
PG25 | Lapsed in a contracting state [announced via postgrant information from national office to epo] |
Ref country code: IT Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES;WARNING: LAPSES OF ITALIAN PATENTS WITH EFFECTIVE DATE BEFORE 2007 MAY HAVE OCCURRED AT ANY TIME BEFORE 2007. THE CORRECT EFFECTIVE DATE MAY BE DIFFERENT FROM THE ONE RECORDED. Effective date: 20051202 |