AU609433B2 - Enzymatic dishwashing composition - Google Patents
Enzymatic dishwashing composition Download PDFInfo
- Publication number
- AU609433B2 AU609433B2 AU82225/87A AU8222587A AU609433B2 AU 609433 B2 AU609433 B2 AU 609433B2 AU 82225/87 A AU82225/87 A AU 82225/87A AU 8222587 A AU8222587 A AU 8222587A AU 609433 B2 AU609433 B2 AU 609433B2
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- AU
- Australia
- Prior art keywords
- lipase
- pseudomonas
- lipases
- 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.)
- Ceased
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- 239000000203 mixture Substances 0.000 title claims description 28
- 238000004851 dishwashing Methods 0.000 title claims description 19
- 230000002255 enzymatic effect Effects 0.000 title claims description 5
- 239000004367 Lipase Substances 0.000 claims description 44
- 108090001060 Lipase Proteins 0.000 claims description 43
- 102000004882 Lipase Human genes 0.000 claims description 43
- 235000019421 lipase Nutrition 0.000 claims description 43
- 108091005804 Peptidases Proteins 0.000 claims description 12
- 239000004365 Protease Substances 0.000 claims description 12
- 102000035195 Peptidases Human genes 0.000 claims description 10
- 230000037029 cross reaction Effects 0.000 claims description 4
- 230000001900 immune effect Effects 0.000 claims description 4
- 239000003599 detergent Substances 0.000 claims description 3
- 230000000694 effects Effects 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
- 241000145542 Pseudomonas marginata Species 0.000 claims description 2
- 241000204735 Pseudomonas nitroreducens Species 0.000 claims description 2
- 239000004094 surface-active agent Substances 0.000 claims description 2
- 230000001580 bacterial effect Effects 0.000 claims 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 12
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 229940088598 enzyme Drugs 0.000 description 10
- 239000000427 antigen Substances 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 102000002322 Egg Proteins Human genes 0.000 description 6
- 108010000912 Egg Proteins Proteins 0.000 description 6
- 235000013345 egg yolk Nutrition 0.000 description 6
- 210000002969 egg yolk Anatomy 0.000 description 6
- 239000002671 adjuvant Substances 0.000 description 5
- 239000002585 base Substances 0.000 description 5
- 238000000034 method Methods 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 4
- 229910052783 alkali metal Inorganic materials 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 239000011521 glass Substances 0.000 description 4
- 239000002736 nonionic surfactant Substances 0.000 description 4
- 108010065511 Amylases Proteins 0.000 description 3
- 102000013142 Amylases Human genes 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical group NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 108010056079 Subtilisins Proteins 0.000 description 3
- 102000005158 Subtilisins Human genes 0.000 description 3
- 150000001340 alkali metals Chemical class 0.000 description 3
- 235000019418 amylase Nutrition 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000007844 bleaching agent Substances 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 239000000839 emulsion Substances 0.000 description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 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
- -1 alkali metal citrates Chemical class 0.000 description 2
- 229940025131 amylases Drugs 0.000 description 2
- 238000005187 foaming Methods 0.000 description 2
- PMYUVOOOQDGQNW-UHFFFAOYSA-N hexasodium;trioxido(trioxidosilyloxy)silane Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[O-][Si]([O-])([O-])O[Si]([O-])([O-])[O-] PMYUVOOOQDGQNW-UHFFFAOYSA-N 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 238000002791 soaking Methods 0.000 description 2
- 235000017550 sodium carbonate Nutrition 0.000 description 2
- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 235000019832 sodium triphosphate Nutrition 0.000 description 2
- 239000002689 soil Substances 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 244000215068 Acacia senegal Species 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
- 229920000084 Gum arabic Polymers 0.000 description 1
- 241001397173 Kali <angiosperm> Species 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
- 108010059820 Polygalacturonase Proteins 0.000 description 1
- 229920000388 Polyphosphate Polymers 0.000 description 1
- 241000589774 Pseudomonas sp. Species 0.000 description 1
- YCFMRQKSKDFOKI-UHFFFAOYSA-L S(=O)(=O)([O-])[O-].[Na+].C1C(C)O1.[Na+] Chemical compound S(=O)(=O)([O-])[O-].[Na+].C1C(C)O1.[Na+] YCFMRQKSKDFOKI-UHFFFAOYSA-L 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 239000000205 acacia gum Substances 0.000 description 1
- 235000010489 acacia gum Nutrition 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 230000007797 corrosion Effects 0.000 description 1
- MWKFXSUHUHTGQN-UHFFFAOYSA-N decan-1-ol Chemical compound CCCCCCCCCCO MWKFXSUHUHTGQN-UHFFFAOYSA-N 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 108010093305 exopolygalacturonase Proteins 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 230000002070 germicidal 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
- 239000003112 inhibitor Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 108020004410 pectinesterase Proteins 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
- 125000000864 peroxy group Chemical group O(O*)* 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920005646 polycarboxylate Polymers 0.000 description 1
- 229920000867 polyelectrolyte Polymers 0.000 description 1
- 239000001205 polyphosphate Substances 0.000 description 1
- 235000011176 polyphosphates Nutrition 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 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
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate 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
- 239000000758 substrate Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000005494 tarnishing Methods 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
- 238000005303 weighing Methods 0.000 description 1
- 239000010457 zeolite Substances 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
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)
- Enzymes And Modification Thereof (AREA)
Description
1 111 1 .4111~
AUSTRALIA
PATENTS ACT 1952 Form COMPLETE SPECIFICATION
(ORIGINAL)
FOR OFFICE USE 609433 Short Title: Int. Cl: Application Number: Lodged: t Complete Specification-Lodged: Accepted: Lapsed: SPublished: S Priority: Related Art: t C TO BE COMPLETED BY APPLICANT Name of Applicant: Address of Applicant: UNILEVER PLC UNILEVER HOUSE
BLACKFRIARS
LONDON EC4
ENGLAND
C C
'C
Actual Inventor: Address for Service: CLEMENT HACK CO., 601 St. Kilda Road, Melbourne, Victoria 3004, Australia.
Complete Specification for the invention entitled: ENZYMATIC DISHWASHING COMPOSITION The following statement is a full description of this invention including the best method of performing it known to me:- MAIL OFFICE ONEff HUNDRED DOLLARS TWENTY DOLLARS TEN DOLLARS c 7096(R) 1A 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 compositio s, 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.
Sc Although lipases as a general class of enzymes have also been suggested, no specific proposals relating to the use of specific lipases in dishwashing compositions Sc have been made as far as we know.
v In dishwashing, the removal of egg-yolk, particularly dried-up or baked-on egg-yolk from the surface of the S" 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 proteases and a special class of lipases in dishwashing compositions provide for a satisfactory removal of eggyolk from the dishware. This removal is significantly superior to the removal, obtained with either the proteases or the lipases, and the combination of these two types of enzymes in fact produces a synergistic cleaning effect in this respect.
The proteases which can be used in the present inventioni 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 proteases are Alcalase, .r
L
SC 7096(R) 2 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 amount of enzyme cc which under standard incubation conditions produces an cc amount of terminal NH 2 -groups equivalent to 1 m' icrogramme/ml glycin.
The class of lipases to be used according to the c present invention embraces those lipases which show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Scc* Chromobacter viscosum var. lipolyticum NRRL-B 3673.
20 This lipase has been described in Dutch Patent Specification 154,269 of Toyo Jozo KK, and the 2 5 microorganism is available to the public at the United States Department of Agriculture, Agricultural Research Service, Northern Utilization and Development Division c 25 at Peoria, Illinois, under the number NRRL-B 3673. This lipase will hereinafter be referred to as "Toyo Jozo" lipase. Th- lipases of the present invention should show a positive immunological cross reaction with the Toyo Jozo lipase antibody, using the standard and well- 30 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 volume of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an i C 7096(R) 3 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 r t The serum containing the required antibody is prepared by centrifugation of clotted blood, taken on day 67.
a 1t C The titre of the anti-Toyo Jozo-lipase antiserum is Cr 15 determined by the inspection of precipitation of serial cc dilutions of antigen and antiserum according to the Ouchterlony procedure. A 25 dilution of antiserum was the dilution that still gave a visible precipitation S0oo with an antigen concentration of 0.1 mg/ml.
0I o 0 All lipases showing a positive immunological cross reaction with Toyo Jozo lipase antibody as hereabove described are lipases according to the present invention. Typical examples thereof are the lipase ex o 25 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 v r. lipolyticum i FERM P 1338, the lipase ex Pseudomonas sp., available under the trade name Amano-CES, the 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 Chromobacter viscosum lipases from US Biochemical Corp., U.S.A. and Diosynth Co., The Netherlands, and lipases ex Pseudomonas gladioli.
C 7096(R) 4 The 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 1umol of titratable fatty acid per minute in a pH stat. under the following conditions: temperature 30OC; pH 9.0; substrate is an emulsion of e, 3.3 wt of olive oil and 3.3 gum arabic, in the ,C presence of 13 mmol/l Ca 2 and 20 mmol/l NaCl in 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 wellknown adsorption methods, such as phenylsepharose as adsorption techniques.
4 The dishwashing compositions of the present invention may furthermore comprise the usual ingredients of CC0 dishwashing compositions. Thus, they may comprise a small amount, in the order of 0.5 5 by weight of a detergent surfactant, 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 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, -i I i i 1 i C 7096(R) -silicates; furthermore, alkali metal polycarboxylates and -polyhydroxysulphonates. Additional examples include alkali metal citrates, -nitrilotriacetates, -carboxymethyloxysuccinates, zeolites etc.
Polyelectrolytes such as polymaleates and polyacrylates are also suitable examples.
Furthermore, peroxy-type bleaching agents may be included such as alkalimetal perborates, -percarbonates, -persulphates as well as organic Srperacids and salts thereof. Bleach precursors such as c tetraacetylethylenediamine may also be included e c t c c together with a peroxy type bleaching agents such as sodium perborate.
Sc Buffers, perfumes, dyes, germicides, solvents, foam Cc depressors, clays such as hectorites, corrosion inhibitors anti-tarnishing agents etc. may also be r included if required.
Other enzymes such as amylases, cellulases, pectinases, pectin-esterases or oxidases may also be included. The compositions may be formulated in any desired form, such as powders, bars, cakes, blocks, pastes and cc 25 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: 9/1 pentasodium triphosphate 1.16 sodium carbonate 0 aq. 0.27 sodium disilicate 0.33 sodium sulphate 0 aq. 0.561 C 7096(R) 6 Comparisons were carried out with this formulation without enzymes, with Toyo Jozo lipase (0.25 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 soiled with 51.5 1.8 mg baked-on egg yolk per glass plate. These were soaked in 1 liter water of 27 0 GH containing the above amounts of the dishwashing composition for a period of one hour at pH 10.0. After soaking the residual egg-yolk present on the plates was determined ti 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 C4e original amount of soil. The tests were repeated three times independently. The following results were obtained: a DW (in 20 no enzymes 96.4 95.5 95.2 c 0 only lipase 97.1 96.0 I 95.3 only Savinase 56.7 47.2 I 51.7 lipase Savinase: 22.3 20.5 I 22.9 At 35 and 45°C 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 no enzymes 97 only lipase only Savinase 52 lipase Savinase: a.~P -I C 7096(R) Example 3 Glasses were cleaned in a Kenmore Sears dishwashing machine, using the normal wash programme at followed by a hot dry. The water hardness was 14.4 0
FH.
The dishwashing composition was dosed in an amount of g, and had the following formulation: by weight 24 sodium tripolyphosphate soda ash sodium disilicate *4 4 4~ Cs S I L Or.
4 54, *c 4 .5 45 C C' linear C 10 alcohol, condensed with 6 moles of ethylene oxide and 24 moles of propylene oxide sodium sulphate 27.8 Amylase (4.8 MU/mg) protease (SavinaseG) (1544 GU/mg) Toyo Jozo lipase 15 LU/ml.
20 The soiling was 6 g 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 washes score Base powder 3 0.5 Base powder lipase 15 1.7 Base powder Savinase 15 2.3 Base powder lipase Savinase 15 0.3 severe spot formation occurred.
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 prcteolytic activity of 0.1-50 Glycine Units per milligram, characterised in that it 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 S' 10 viscosum var. lipolyticum NRRL B 3673.
2. A composition according to claim 1, characterised in that the lipase is producible by Pseudomonas fluorescens, Pseudomonas fragi, Pseudomonas nitroreducens var. lipolyticum, Pseudomonas cepacia, Pseudomonas gladioli and Chromobacter viscosum. tt t DATED THIS 8TH DAY OF DECEMBER 1987 SUNILEVER PLC By its Patent Attorneys: CLEMENT HACK CO. Fellows Institute of Patent Attorneys of Australia. i
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB868629537A GB8629537D0 (en) | 1986-12-10 | 1986-12-10 | Enzymatic dishwashing composition |
| GB8629537 | 1986-12-10 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU8222587A AU8222587A (en) | 1988-06-16 |
| AU609433B2 true AU609433B2 (en) | 1991-05-02 |
Family
ID=10608787
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU82225/87A Ceased AU609433B2 (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 |
|---|---|---|---|---|
| JPH0697997B2 (en) * | 1985-08-09 | 1994-12-07 | ギスト ブロカデス ナ−ムロ−ゼ フエンノ−トチヤツプ | New enzymatic detergent additive |
| 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 | Cleaning composition for automatic dishwashers |
| US4959179A (en) * | 1989-01-30 | 1990-09-25 | Lever Brothers Company | Stabilized enzymes liquid detergent composition containing lipase and protease |
| US5089163A (en) * | 1989-01-30 | 1992-02-18 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic liquid detergent composition |
| 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 |
| AU694268B2 (en) * | 1994-09-06 | 1998-07-16 | S.C. Johnson & Son, Inc. | A cleaning composition comprising lipase and amylase enzymes |
| BRPI0808513A2 (en) | 2007-03-09 | 2014-08-19 | Danisco Us Inc Genencor Div | ALPHA-AMILASE VARIANTS OF ALKALIFYL BACILLUS SPECIES, COMPOSITIONS UNDERSTANDING ALPHA-AMYLASE VARIANTS AND METHODS OF USE |
| BRPI0913378A2 (en) | 2008-06-06 | 2015-09-01 | Danisco Us Inc | Glucose production from starch using bacillus subtilis alpha-amylase |
| MX364987B (en) | 2008-06-06 | 2019-05-17 | Danisco Us Inc | Variant alpha-amylases from bacillus subtilis and methods of use, thereof. |
| CA2726631A1 (en) | 2008-06-06 | 2009-12-10 | Danisco Us Inc. | Saccharification enzyme composition and method of saccharification thereof |
| WO2010036515A1 (en) | 2008-09-25 | 2010-04-01 | Danisco Us Inc. | Alpha-amylase blends and methods for using said blends |
| CA2778471A1 (en) | 2009-10-23 | 2011-04-28 | Danisco Us Inc. | Methods for reducing blue saccharide |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0205208A2 (en) * | 1985-06-11 | 1986-12-17 | Unilever N.V. | Enzymatic detergent composition |
| US4707291A (en) * | 1985-06-11 | 1987-11-17 | Lever Brothers Company | Enzymatic detergent composition |
Family Cites Families (6)
| 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 |
| 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 EP EP87202396A patent/EP0271156B1/en not_active Expired - Lifetime
- 1987-12-02 DE DE8787202396T patent/DE3763814D1/en not_active Expired - Fee Related
- 1987-12-02 ES ES87202396T patent/ES2017711B3/en not_active Expired - Lifetime
- 1987-12-08 CA CA000553757A patent/CA1288369C/en not_active Expired - Fee Related
- 1987-12-08 JP JP62310793A patent/JPH0647679B2/en not_active Expired - Lifetime
- 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
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0205208A2 (en) * | 1985-06-11 | 1986-12-17 | Unilever N.V. | Enzymatic detergent composition |
| US4707291A (en) * | 1985-06-11 | 1987-11-17 | Lever Brothers Company | Enzymatic detergent composition |
Also Published As
| Publication number | Publication date |
|---|---|
| DE3763814D1 (en) | 1990-08-23 |
| EP0271156A2 (en) | 1988-06-15 |
| GB8629537D0 (en) | 1987-01-21 |
| AU8222587A (en) | 1988-06-16 |
| ES2017711B3 (en) | 1991-03-01 |
| JPH0647679B2 (en) | 1994-06-22 |
| JPS63159498A (en) | 1988-07-02 |
| BR8706684A (en) | 1988-07-19 |
| EP0271156B1 (en) | 1990-07-18 |
| ZA879299B (en) | 1989-08-30 |
| EP0271156A3 (en) | 1988-08-03 |
| CA1288369C (en) | 1991-09-03 |
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