CA1288369C - Enzymatic dishwashing composition - Google Patents
Enzymatic dishwashing compositionInfo
- Publication number
- CA1288369C CA1288369C CA000553757A CA553757A CA1288369C CA 1288369 C CA1288369 C CA 1288369C CA 000553757 A CA000553757 A CA 000553757A CA 553757 A CA553757 A CA 553757A CA 1288369 C CA1288369 C CA 1288369C
- Authority
- CA
- Canada
- Prior art keywords
- lipase
- lipases
- pseudomonas
- dishwashing composition
- proteases
- 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.)
- Expired - Fee Related
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
Abstract
ABSTRACT OF THE DISCLOSURE
The present invention relates to an enzymatic dishwashing composition comprising proteases and lipases. The lipases belong to a special class, i.e.
those which show a positive immunological cross-reaction with the antibody of the lipase, produced by Chromobacter viscosum var. lipolyticum NRRL B 3683.
The use of the proteases and the lipases together provides for a synergistic cleaning effect of the dishwashing composition.
The present invention relates to an enzymatic dishwashing composition comprising proteases and lipases. The lipases belong to a special class, i.e.
those which show a positive immunological cross-reaction with the antibody of the lipase, produced by Chromobacter viscosum var. lipolyticum NRRL B 3683.
The use of the proteases and the lipases together provides for a synergistic cleaning effect of the dishwashing composition.
Description
C 7096 ( R ) ENZYMATIC DISHWASHING COMPOSITION
The present invention relates to an enzymatic dishwashing composition comprising proteases and a special class of lipases.
The use of enzymes in dishwashing compositions, both for manual as well as mechanical dishwashing is generally well-known in the art. For that purpose, in particular amylases and/or proteases have been proposed.
Although lipase~ as a general class of enzymes have also been suggested, no specific proposals relating to the use of specific lipases in dishwashing compositions have been made as far as we know.
In dishwashing, the removal of egg-yolk, particularly dried~up or baked-on egg-yolk from the surface of the dishware is often a problem, and the satisfactory removal of this type of soil often requires special measures or special dishwashing compositions.
We have now surprisingly found that the inclusion of proteaseg and a special cla~s of lipases in di hwashing compositions provide for a satisfactory removal of egg-yolk from the dishware. This removal ~s signi~icantlysuperior to the removal, obtained with either the proteases or the lipa~es, and the combination of the4e two types o enzymes in fact produces a syner~istic cleaning effect in this re~pect.
The protea3es which can be used in the present invention can be any type of protease known for inclusion in detergent compositions. Most commercially available proteases are of the subtilisin type, and suitable examples of such proteaqes are Alcalase, ~ de-.~tes -~r~Gle ~a~k ~ 3~i9 C 7096(R) . . ~
Esperase and Savinase, sold by NOVO Industri; Maxatase and Maxacal, sold by Gist Brocades; Optimase sold by Kali Chemie; Kazusase, sold by Showa Denka. Preferred are the so-called high alkaline proteases such as Savinase. Mixtures of various proteases can also be used. In general, the dishwashing compositions of the invention contain the proteases in such an amount, that the final composition has a proteolytic activity of 0.1 - 50, usually 1 - 40 and preferably 5 -30 GU/mg. A
GU is a glycin unit, which is the a~ount oi~nzyme which under standard incubation conditions produces an amount of terminal NH2-groups equivalent to 1 microgramme/ml glycin.
The class of lipases to be used according to the present invention embraces those lipases which show a positive immunoIogical 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 at the United States Department of Agriculture, Aqricultural Research Service, Northern Utilization and Development Division at Peoria, Illinois, under the number NRRL-B 3673. This lipase will hereinafter be referred to as "~oyo Jo20"
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 toOuchterlony (Acta. Med. Scan., 133, page~ 76-79 (1950)).
The preparation o~ the antiserum i~ carried out as fol~ows:
Equal volume of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an ~..2883~9 C 7096(R) . ~
emulsion is obtained. Two female rabbits are injected with 2 ml samples of the emulsion accordiny to the followiny 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, ta~en on day 67.
The titre of the anti-Toyo Jozo-lipase antiserum i9 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 Toyo Jozo lipase antibody as hereabove deRcribed are lipases according to the present invention. Typical examples thereof are the lipase ex Pseudomona~ fluorescens IAM 1057 (available under the trade name Amano-P), the lipase ex Pseudomonas fragi FERM P 1339 tavailable under the trade name Amano-s lipaqe ex Pseudomonas n troreducens var. ~
FERM P 1338, the lipase ex P~eudomonas sp., available under the trade name Amano-CES, the lipase ex Pseudomonas cepacia, lipase~ ex Chromobacter viscosum, .
e.g. Chromobacter viscosum var. lipolyticum NRRL B-3673, commercially available from Toyo Jozo Co., Ta~ata, Japan: and ~urther Chromobacter viscosum lipases from US Biochemical Corp., U.S.A. and Diosynth Co., The Netherlands, and lipases ex Pseudomonas ~adioli.
~ .. 2883~i9 C 7096(R) ~he lipases of the present invention are included in the dishwashing composition in such an amount that the final dishwashing 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 l/umol of titratable fatty acid per minute in a pH stat. under the following conditions:
temperature 30C; 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 phenylsepharose adsorption techniques.
~0 ; The dishwashing compositions of the present invention may furthermore comprise the usual ingredients of dishwashing compositions. Thus, they may comprise a ~mall amount, in the order of 0.5 - S ~ by weight of a detergent ~urfactant, e.g. anionic or nonionic surfactants, such as a low or non-foaming nonionic surfactant. Such low or non-foaming nonionic surfactants are well-known in the art, and suitable examples can be found in M. Schick "Nonionic 30 Surfactants" Vol. 1, (1967).
Furthermore, they may comprise organic and/or inorganic builder materials, usually in amounts of from 10 - 80 %~
for most practical purposes from 20 - 60 ~ by weight.
Such builder materials include alkali metal polyphosphates, -pyrophosphates, -hexametaphosphates, -orthophosphates, -carbonates, -bicarbonates, -borates, ~.288~9 C 7096(R) -qilicates; furthermore, alkali metal polycarboxylates and -polyhydroxysulphonates. Additional examples include alkali metal citrates, -nitrilotriacetates, -carboxymethyloxysuccinates, zeolites etc.
Polyelectrolytes such as polymaleate~ and palyacrylates are also suitable examples.
Furthermcre, peroxy type bleaching agents may be included such as alkalimetal perborates, -percarbonates, -persulphates as well as organic peracids and salts thereof. Bleach"precursors ~uch as tetraacetylethylenediamine may also be included together with a peroxy type bleaching agents such as sodium perbora';e.
Buffers, perfumes, dyes, germicides, solvents, foam depreQsors, clays such as hectorites, corrosion inhibitors anti-tarnishing agents etc. may also be included if required.
Other enzymes such as amylases, cellulases, pectina~es, pectin-esterases or oxidases may also be included. The compositions may be formulated in any desired form, such as powders, bars, cakes, block~, pastes and liquids. The invention will further be illustrated by way of Example.
Example 1 Tests were carried out with an aqueous solution containing the following base formulation:
pentasodium tripho~phate 1.16 sodium carbonate O aq. 0.27 sodium disilicate 0~33 sodium sulphate O aq. 0.561 9 c 7096 ( R ) Comparisons were carried out with this formulation without enzymes, with Toyo Jo20 lipase (0.25 g/l~, with Savinase 6.0 CM (0.023 g/l) or with a mixture of these enzymes.
A set of 8 glass plates (4 x 4 cm) were ~oiled with 51.5 + 1.8 mg baked-on egg yolk per glass plate. These were soaked in 1 liter water of 27GH containing the above amounts of the dishwashing composition for a period of one hour at pH 10Ø After ~oaking the residual egg-yolk present on the plate~ was determined by weighing and measuring the weight difference of the soiled plates before and after soaking.
The difference (DW) is expressed as a percentage of the original amount of soil. The tests were repeated three times independently. The following results were obtained:
DW (in %) no enzymes : 96.4 1 95.5 1 95.2 only lipase : 97.1 ¦ 96.0 ¦ 35.3 1. ~ only~fSavinase : 56.7 1 47.2 ¦ 51.7 lipase + Savinase: 22.3 1 20.5 1 22.9 At 35 and 45C similar results were obtained. Replacing Savinase by Alcalase also produced similar results.
Example 2 Repeating Example 1, but using the Amano-P lipase, gave the following results:
DW (in g) no enzymes : 97 only lipase : 95 only Savinase : 52 lipase ~ Savinase: 20 ~ ~er~ S t^rQd~ ek ~. ~8~3~9 c 7096(R) Example 3 Glasses were cleaned in a Kenmore Sears dishwashing machine, using the normal wa~h programme at 60C
followed by a hot dry. The water hardness was 14.4FH.
The dishwashing composition was dosed in an amount of 30 g, and had the following formulation:
~ by weight sodium tripolyphoqphate 24 soda ash 20 qodium disilicate 11 linear C10 alcohol, condensed with 6 moles of ethylene oxide 2.5 and 24 moles of propylene oxide sodium sulphate 27.8 Amylase (4.3 MU/mg) 0.5 protease (Savinase ~ (1544 G~/mg) 1.0 Toyo Jozo lipase 15 LU/ml.
The soiling was 6 9 egg-yolk.
The glasses were washed consecutively several times, and the film formation was thereafter assessed using a scale of 0 - 5, 0 being no film at all and 5 being very severe film formation~ These experiments were also carried out with the same formulation, but without lipase or without Savinase or without lipase and Savinase.
.. .. .. .
The following results were obtained:
Number of Film consecutive _shes score Base powder 3 0.5 *
Base powder ~ lipase15 1.7 35 Base powder + Savinase15 2.3 Base powder ~ lipase + Savinase 15 0.3 * severe spot formation occurred.
~ ~lenc~tes ~ cl e n~ r k
The present invention relates to an enzymatic dishwashing composition comprising proteases and a special class of lipases.
The use of enzymes in dishwashing compositions, both for manual as well as mechanical dishwashing is generally well-known in the art. For that purpose, in particular amylases and/or proteases have been proposed.
Although lipase~ as a general class of enzymes have also been suggested, no specific proposals relating to the use of specific lipases in dishwashing compositions have been made as far as we know.
In dishwashing, the removal of egg-yolk, particularly dried~up or baked-on egg-yolk from the surface of the dishware is often a problem, and the satisfactory removal of this type of soil often requires special measures or special dishwashing compositions.
We have now surprisingly found that the inclusion of proteaseg and a special cla~s of lipases in di hwashing compositions provide for a satisfactory removal of egg-yolk from the dishware. This removal ~s signi~icantlysuperior to the removal, obtained with either the proteases or the lipa~es, and the combination of the4e two types o enzymes in fact produces a syner~istic cleaning effect in this re~pect.
The protea3es which can be used in the present invention can be any type of protease known for inclusion in detergent compositions. Most commercially available proteases are of the subtilisin type, and suitable examples of such proteaqes are Alcalase, ~ de-.~tes -~r~Gle ~a~k ~ 3~i9 C 7096(R) . . ~
Esperase and Savinase, sold by NOVO Industri; Maxatase and Maxacal, sold by Gist Brocades; Optimase sold by Kali Chemie; Kazusase, sold by Showa Denka. Preferred are the so-called high alkaline proteases such as Savinase. Mixtures of various proteases can also be used. In general, the dishwashing compositions of the invention contain the proteases in such an amount, that the final composition has a proteolytic activity of 0.1 - 50, usually 1 - 40 and preferably 5 -30 GU/mg. A
GU is a glycin unit, which is the a~ount oi~nzyme which under standard incubation conditions produces an amount of terminal NH2-groups equivalent to 1 microgramme/ml glycin.
The class of lipases to be used according to the present invention embraces those lipases which show a positive immunoIogical 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 at the United States Department of Agriculture, Aqricultural Research Service, Northern Utilization and Development Division at Peoria, Illinois, under the number NRRL-B 3673. This lipase will hereinafter be referred to as "~oyo Jo20"
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 toOuchterlony (Acta. Med. Scan., 133, page~ 76-79 (1950)).
The preparation o~ the antiserum i~ carried out as fol~ows:
Equal volume of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an ~..2883~9 C 7096(R) . ~
emulsion is obtained. Two female rabbits are injected with 2 ml samples of the emulsion accordiny to the followiny 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, ta~en on day 67.
The titre of the anti-Toyo Jozo-lipase antiserum i9 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 Toyo Jozo lipase antibody as hereabove deRcribed are lipases according to the present invention. Typical examples thereof are the lipase ex Pseudomona~ fluorescens IAM 1057 (available under the trade name Amano-P), the lipase ex Pseudomonas fragi FERM P 1339 tavailable under the trade name Amano-s lipaqe ex Pseudomonas n troreducens var. ~
FERM P 1338, the lipase ex P~eudomonas sp., available under the trade name Amano-CES, the lipase ex Pseudomonas cepacia, lipase~ ex Chromobacter viscosum, .
e.g. Chromobacter viscosum var. lipolyticum NRRL B-3673, commercially available from Toyo Jozo Co., Ta~ata, Japan: and ~urther Chromobacter viscosum lipases from US Biochemical Corp., U.S.A. and Diosynth Co., The Netherlands, and lipases ex Pseudomonas ~adioli.
~ .. 2883~i9 C 7096(R) ~he lipases of the present invention are included in the dishwashing composition in such an amount that the final dishwashing 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 l/umol of titratable fatty acid per minute in a pH stat. under the following conditions:
temperature 30C; 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 phenylsepharose adsorption techniques.
~0 ; The dishwashing compositions of the present invention may furthermore comprise the usual ingredients of dishwashing compositions. Thus, they may comprise a ~mall amount, in the order of 0.5 - S ~ by weight of a detergent ~urfactant, e.g. anionic or nonionic surfactants, such as a low or non-foaming nonionic surfactant. Such low or non-foaming nonionic surfactants are well-known in the art, and suitable examples can be found in M. Schick "Nonionic 30 Surfactants" Vol. 1, (1967).
Furthermore, they may comprise organic and/or inorganic builder materials, usually in amounts of from 10 - 80 %~
for most practical purposes from 20 - 60 ~ by weight.
Such builder materials include alkali metal polyphosphates, -pyrophosphates, -hexametaphosphates, -orthophosphates, -carbonates, -bicarbonates, -borates, ~.288~9 C 7096(R) -qilicates; furthermore, alkali metal polycarboxylates and -polyhydroxysulphonates. Additional examples include alkali metal citrates, -nitrilotriacetates, -carboxymethyloxysuccinates, zeolites etc.
Polyelectrolytes such as polymaleate~ and palyacrylates are also suitable examples.
Furthermcre, peroxy type bleaching agents may be included such as alkalimetal perborates, -percarbonates, -persulphates as well as organic peracids and salts thereof. Bleach"precursors ~uch as tetraacetylethylenediamine may also be included together with a peroxy type bleaching agents such as sodium perbora';e.
Buffers, perfumes, dyes, germicides, solvents, foam depreQsors, clays such as hectorites, corrosion inhibitors anti-tarnishing agents etc. may also be included if required.
Other enzymes such as amylases, cellulases, pectina~es, pectin-esterases or oxidases may also be included. The compositions may be formulated in any desired form, such as powders, bars, cakes, block~, pastes and liquids. The invention will further be illustrated by way of Example.
Example 1 Tests were carried out with an aqueous solution containing the following base formulation:
pentasodium tripho~phate 1.16 sodium carbonate O aq. 0.27 sodium disilicate 0~33 sodium sulphate O aq. 0.561 9 c 7096 ( R ) Comparisons were carried out with this formulation without enzymes, with Toyo Jo20 lipase (0.25 g/l~, with Savinase 6.0 CM (0.023 g/l) or with a mixture of these enzymes.
A set of 8 glass plates (4 x 4 cm) were ~oiled with 51.5 + 1.8 mg baked-on egg yolk per glass plate. These were soaked in 1 liter water of 27GH containing the above amounts of the dishwashing composition for a period of one hour at pH 10Ø After ~oaking the residual egg-yolk present on the plate~ was determined by weighing and measuring the weight difference of the soiled plates before and after soaking.
The difference (DW) is expressed as a percentage of the original amount of soil. The tests were repeated three times independently. The following results were obtained:
DW (in %) no enzymes : 96.4 1 95.5 1 95.2 only lipase : 97.1 ¦ 96.0 ¦ 35.3 1. ~ only~fSavinase : 56.7 1 47.2 ¦ 51.7 lipase + Savinase: 22.3 1 20.5 1 22.9 At 35 and 45C similar results were obtained. Replacing Savinase by Alcalase also produced similar results.
Example 2 Repeating Example 1, but using the Amano-P lipase, gave the following results:
DW (in g) no enzymes : 97 only lipase : 95 only Savinase : 52 lipase ~ Savinase: 20 ~ ~er~ S t^rQd~ ek ~. ~8~3~9 c 7096(R) Example 3 Glasses were cleaned in a Kenmore Sears dishwashing machine, using the normal wa~h programme at 60C
followed by a hot dry. The water hardness was 14.4FH.
The dishwashing composition was dosed in an amount of 30 g, and had the following formulation:
~ by weight sodium tripolyphoqphate 24 soda ash 20 qodium disilicate 11 linear C10 alcohol, condensed with 6 moles of ethylene oxide 2.5 and 24 moles of propylene oxide sodium sulphate 27.8 Amylase (4.3 MU/mg) 0.5 protease (Savinase ~ (1544 G~/mg) 1.0 Toyo Jozo lipase 15 LU/ml.
The soiling was 6 9 egg-yolk.
The glasses were washed consecutively several times, and the film formation was thereafter assessed using a scale of 0 - 5, 0 being no film at all and 5 being very severe film formation~ These experiments were also carried out with the same formulation, but without lipase or without Savinase or without lipase and Savinase.
.. .. .. .
The following results were obtained:
Number of Film consecutive _shes score Base powder 3 0.5 *
Base powder ~ lipase15 1.7 35 Base powder + Savinase15 2.3 Base powder ~ lipase + Savinase 15 0.3 * severe spot formation occurred.
~ ~lenc~tes ~ cl e n~ r k
Claims (2)
1. An enzymatic dishwashing composition comprising from 0.5-5% by weight of a detergent surfactant, from 10-80% by weight of a builder, and proteases in an amount such that the composition has a proteolytic activity of 0.1-50 Glycine Units per milligram, wherein the dishwashing composition further comprises from 0.005-100 LU/mg of a bacterial lipase which shows a positive immunological cross-reaction with the antibody of the lipase, produced by Chromobacter viscosum var. lipolyticum NRRL B 3673.
2. A composition according to claim 1, wherein the lipase is producible by Pseudomonas fluorescens, Pseudomonas fragi, Pseudomonas nitroreducens var. lipolyticum, Pseudomonas cepacia, Pseudomonas gladioli and Chromobacter viscosum.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB8629537 | 1986-12-10 | ||
| GB868629537A GB8629537D0 (en) | 1986-12-10 | 1986-12-10 | Enzymatic dishwashing composition |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1288369C true CA1288369C (en) | 1991-09-03 |
Family
ID=10608787
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000553757A Expired - Fee Related CA1288369C (en) | 1986-12-10 | 1987-12-08 | Enzymatic dishwashing composition |
Country Status (9)
| Country | Link |
|---|---|
| EP (1) | EP0271156B1 (en) |
| JP (1) | JPH0647679B2 (en) |
| AU (1) | AU609433B2 (en) |
| BR (1) | BR8706684A (en) |
| CA (1) | CA1288369C (en) |
| DE (1) | DE3763814D1 (en) |
| ES (1) | ES2017711B3 (en) |
| GB (1) | GB8629537D0 (en) |
| ZA (1) | ZA879299B (en) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3684398D1 (en) * | 1985-08-09 | 1992-04-23 | Gist Brocades Nv | LIPOLYTIC ENZYMES AND THEIR USE IN DETERGENTS. |
| BE1001436A3 (en) * | 1988-02-22 | 1989-10-31 | Synfina Sa | New lipase and detergent compositions containing. |
| GB8813687D0 (en) * | 1988-06-09 | 1988-07-13 | Unilever Plc | Enzymatic dishwashing & rinsing composition |
| JPH0277499A (en) * | 1988-09-14 | 1990-03-16 | Lion Corp | Detergent composition for use in automatic dishwasher |
| US5089163A (en) * | 1989-01-30 | 1992-02-18 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic liquid detergent composition |
| US4959179A (en) * | 1989-01-30 | 1990-09-25 | Lever Brothers Company | Stabilized enzymes liquid detergent composition containing lipase and protease |
| JPH0699714B2 (en) * | 1990-07-11 | 1994-12-07 | 花王株式会社 | Detergent composition for automatic dishwasher |
| JP2986595B2 (en) * | 1991-11-08 | 1999-12-06 | ダイセル化学工業株式会社 | New lipase |
| CA2088230A1 (en) * | 1992-02-03 | 1993-08-04 | James Gordon | Detergent composition |
| WO1996007723A1 (en) * | 1994-09-06 | 1996-03-14 | S.C. Johnson & Son, Inc. | A cleaning composition comprising lipase and amylase enzymes |
| WO2008112459A2 (en) | 2007-03-09 | 2008-09-18 | Danisco Us Inc., Genencor Division | Alkaliphilic bacillus species a-amylase variants, compositions comprising a-amylase variants, and methods of use |
| CA2726631A1 (en) | 2008-06-06 | 2009-12-10 | Danisco Us Inc. | Saccharification enzyme composition and method of saccharification thereof |
| EP2698434A1 (en) | 2008-06-06 | 2014-02-19 | Danisco US Inc. | Uses of an alpha-amylase from Bacillus subtilis |
| US9090887B2 (en) | 2008-06-06 | 2015-07-28 | Danisco Us Inc. | Variant alpha-amylases from Bacillus subtilis and methods of use, thereof |
| BRPI0920891B1 (en) | 2008-09-25 | 2023-01-10 | Danisco Us Inc | ALPHA-AMYLASE MIXTURE AND METHOD FOR PRODUCING A FERMENTABLE SUGAR |
| US20120202265A1 (en) | 2009-10-23 | 2012-08-09 | Vivek Sharma | Methods for reducing blue saccharide |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE1619087A1 (en) * | 1967-08-14 | 1969-10-02 | Henkel & Cie Gmbh | Surfactant combinations which can be used as laundry detergents and detergents or auxiliary washing agents containing them |
| GB1273545A (en) * | 1968-06-24 | 1972-05-10 | Albright & Wilson | Multi-enzyme cleaning compositions |
| DK289083A (en) * | 1983-06-23 | 1984-12-24 | Novo Industri As | LIPASE, PROCEDURE FOR PREPARING THEREOF AND ITS APPLICATION |
| GB8514708D0 (en) * | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
| GB8514707D0 (en) * | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
| DK154572C (en) * | 1985-08-07 | 1989-04-24 | Novo Industri As | ENZYMATIC DETERGENT ADDITIVE, DETERGENT AND METHOD FOR WASHING TEXTILES |
| JPS6434560A (en) * | 1987-07-30 | 1989-02-06 | Seiko Epson Corp | Die structure |
| JPS6434559A (en) * | 1987-07-30 | 1989-02-06 | Seiko Epson Corp | Structure for taking out cavity |
-
1986
- 1986-12-10 GB GB868629537A patent/GB8629537D0/en active Pending
-
1987
- 1987-12-02 ES ES87202396T patent/ES2017711B3/en not_active Expired - Lifetime
- 1987-12-02 EP EP87202396A patent/EP0271156B1/en not_active Expired - Lifetime
- 1987-12-02 DE DE8787202396T patent/DE3763814D1/en not_active Expired - Fee Related
- 1987-12-08 JP JP62310793A patent/JPH0647679B2/en not_active Expired - Lifetime
- 1987-12-08 CA CA000553757A patent/CA1288369C/en not_active Expired - Fee Related
- 1987-12-08 AU AU82225/87A patent/AU609433B2/en not_active Ceased
- 1987-12-09 BR BR8706684A patent/BR8706684A/en not_active IP Right Cessation
- 1987-12-10 ZA ZA879299A patent/ZA879299B/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| DE3763814D1 (en) | 1990-08-23 |
| ES2017711B3 (en) | 1991-03-01 |
| GB8629537D0 (en) | 1987-01-21 |
| EP0271156A2 (en) | 1988-06-15 |
| JPH0647679B2 (en) | 1994-06-22 |
| AU8222587A (en) | 1988-06-16 |
| EP0271156B1 (en) | 1990-07-18 |
| EP0271156A3 (en) | 1988-08-03 |
| BR8706684A (en) | 1988-07-19 |
| AU609433B2 (en) | 1991-05-02 |
| JPS63159498A (en) | 1988-07-02 |
| ZA879299B (en) | 1989-08-30 |
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