GB2247025A - Enzymatic dishwashing and rinsing composition - Google Patents
Enzymatic dishwashing and rinsing composition Download PDFInfo
- Publication number
- GB2247025A GB2247025A GB9017733A GB9017733A GB2247025A GB 2247025 A GB2247025 A GB 2247025A GB 9017733 A GB9017733 A GB 9017733A GB 9017733 A GB9017733 A GB 9017733A GB 2247025 A GB2247025 A GB 2247025A
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- GB
- United Kingdom
- Prior art keywords
- composition
- dishwashing
- amount
- rinsing composition
- detergent
- Prior art date
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- Withdrawn
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- 239000000203 mixture Substances 0.000 title claims abstract description 40
- 238000004851 dishwashing Methods 0.000 title claims abstract description 20
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 6
- 108091005804 Peptidases Proteins 0.000 claims abstract description 13
- 239000004365 Protease Substances 0.000 claims description 11
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 102000035195 Peptidases Human genes 0.000 abstract description 12
- 239000002689 soil Substances 0.000 abstract description 10
- 108010000912 Egg Proteins Proteins 0.000 abstract description 8
- 102000002322 Egg Proteins Human genes 0.000 abstract description 8
- 235000013345 egg yolk Nutrition 0.000 abstract description 8
- 210000002969 egg yolk Anatomy 0.000 abstract description 8
- 102100037611 Lysophospholipase Human genes 0.000 abstract description 3
- 108010058864 Phospholipases A2 Proteins 0.000 abstract description 2
- 102100031415 Hepatic triacylglycerol lipase Human genes 0.000 abstract 1
- 108010013563 Lipoprotein Lipase Proteins 0.000 abstract 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 11
- 108090000790 Enzymes Proteins 0.000 description 11
- 229940088598 enzyme Drugs 0.000 description 11
- 239000003599 detergent Substances 0.000 description 8
- 150000003904 phospholipids Chemical class 0.000 description 8
- 235000019419 proteases Nutrition 0.000 description 8
- 239000007844 bleaching agent Substances 0.000 description 7
- 101000585299 Tropidechis carinatus Acidic phospholipase A2 2 Proteins 0.000 description 6
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 5
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 5
- 102000015439 Phospholipases Human genes 0.000 description 5
- 108010064785 Phospholipases Proteins 0.000 description 5
- 229940067606 lecithin Drugs 0.000 description 5
- 235000010445 lecithin Nutrition 0.000 description 5
- 239000000787 lecithin Substances 0.000 description 5
- 229910019142 PO4 Inorganic materials 0.000 description 4
- 239000003795 chemical substances by application Substances 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 239000011521 glass Substances 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 4
- 239000010452 phosphate Substances 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 239000004094 surface-active agent Substances 0.000 description 4
- 102000013142 Amylases Human genes 0.000 description 3
- 108010065511 Amylases Proteins 0.000 description 3
- 108010056079 Subtilisins Proteins 0.000 description 3
- 102000005158 Subtilisins Human genes 0.000 description 3
- 229910052783 alkali metal Inorganic materials 0.000 description 3
- 150000001340 alkali metals Chemical class 0.000 description 3
- 235000019418 amylase Nutrition 0.000 description 3
- 229940025131 amylases Drugs 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 description 2
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 2
- 239000004150 EU approved colour Substances 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- 239000004367 Lipase Substances 0.000 description 2
- -1 N-acetyl casein Chemical compound 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- 229910001424 calcium ion Inorganic materials 0.000 description 2
- 239000000460 chlorine Substances 0.000 description 2
- 229910052801 chlorine Inorganic materials 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 239000000945 filler Substances 0.000 description 2
- 238000005187 foaming Methods 0.000 description 2
- 239000003752 hydrotrope Substances 0.000 description 2
- 235000019421 lipase Nutrition 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 229940006093 opthalmologic coloring agent diagnostic Drugs 0.000 description 2
- 239000002304 perfume Substances 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 230000000007 visual effect Effects 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- CIOXZGOUEYHNBF-UHFFFAOYSA-N (carboxymethoxy)succinic acid Chemical class OC(=O)COC(C(O)=O)CC(O)=O CIOXZGOUEYHNBF-UHFFFAOYSA-N 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108020002496 Lysophospholipase Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- BGRWYDHXPHLNKA-UHFFFAOYSA-N Tetraacetylethylenediamine Chemical compound CC(=O)N(C(C)=O)CCN(C(C)=O)C(C)=O BGRWYDHXPHLNKA-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 229910052910 alkali metal silicate Inorganic materials 0.000 description 1
- 150000001447 alkali salts Chemical class 0.000 description 1
- 229910052784 alkaline earth metal Inorganic materials 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- QRUDEWIWKLJBPS-UHFFFAOYSA-N benzotriazole Chemical compound C1=CC=C2N[N][N]C2=C1 QRUDEWIWKLJBPS-UHFFFAOYSA-N 0.000 description 1
- 150000001642 boronic acid derivatives Chemical class 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 150000004649 carbonic acid derivatives Chemical class 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- OEYIOHPDSNJKLS-UHFFFAOYSA-N choline Chemical group C[N+](C)(C)CCO OEYIOHPDSNJKLS-UHFFFAOYSA-N 0.000 description 1
- 229960001231 choline Drugs 0.000 description 1
- 150000001860 citric acid derivatives Chemical class 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 150000002148 esters Chemical group 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 235000021588 free fatty acids Nutrition 0.000 description 1
- 230000002070 germicidal effect Effects 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 150000002327 glycerophospholipids Chemical class 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 108010052522 livetin Proteins 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical class OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 125000000864 peroxy group Chemical group O(O*)* 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920000867 polyelectrolyte Polymers 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 150000004760 silicates Chemical class 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 230000009974 thixotropic effect Effects 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- 235000013311 vegetables Nutrition 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
-
- 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
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
An enzymatic dishwashing or rinsing composition comprises phospholipase A1 and/or A2. In combination with proteolytic enzymes the composition is effective in removing egg yolk soil and consequently reducing spotting on glassware.
Description
ENZYMATIC DISHWASHING AND RINSING COMPOSITION
FIELD OF INVENTION
The present invention relates to an enzymatic dishwashing or rinsing composition comprising lipolytic enzymes.
BACKGROUND OF INVENTION
Enzymatic dishwashing compositions have been proposed in the art. As enzymes, mainly amylases and/or proteases have been proposed for inclusion in dishwashing compositions (e.g. US 4 162 987, Maguire et al). Lipases have also been suggested (e.g. EP 271 155, Unilever), but have received far less attention than the amylases and/or proteases. Dishwashing compositions, in particular machine dishwashing compositions which are used in the main wash step of a machine dishwashing operation have, in general, a satisfactory cleaning performance. However, frequently the articles cleaned with such products still do not have a satisfactory visual appearance after rinsing and drying, showing film or spots.Some main wash liquor is usually carried over from the main wash step to the rinse step, causing some deposition of soil and resulting in insoluble calcium salts on the articles to be rinsed.
This results in visible film or spots on the articles when they are dry. In particular with glass articles, this causes an unsightly visual appearance, and most particularly when egg soil is present in the wash.
SUMMARY OF INVENTION
We have now found that the addition of phospholipase
A and/or A2 to a main wash dishwashing composition or to a rinse composition significantly improves the cleaning of certain soils and reduces the formation of film or spots on the articles cleaned or rinsed with such a composition.
DESCRIPTION OF INVENTION
Phospholipids occurs generally in animal and vegetable foods. They are important constituents of all cell membranes. For example, in egg yolk the phospholipid level is 18% of the total dry weight. Phospholipids are of the general formula (I):
wherein X represents hydrogen, choline (to give lecithin), ethanolamine or serine, for example, and R1 and R2 are alkyl groups which may be the same or different.
Tests have shown that if glasses are washed in the presence of the phospholipid lecithin, there is a significantly greater degree of spot formation in comparison to other fats, proteins, etc. Although we do not wish to be bound by any theory, it is possible that the phospholipid adsorbs onto glass surfaces, thereby modifying the drainage behaviour of water films.
Furthermore, phospholipids may influence the removal of composite soils, such as egg yolk, because of their tendency to form complexes with proteins (usually phosphoglycoproteins, eg livetin in egg yolk) and more apolar lipids such as triglycerides.
Four classes of phospolipases (classified as Al, A2,
C and D) are known (E Dennis, The Phospholipases, Chapter 9, The Enzymes, Vol XVI, Academic Press, 1983). The enzymes all use phospholipids as a substrate, but catalyse the hydrolysis of different ester moieties in the substrate molecule. Phospholipase-Al, and -A2 yield lysophospholipids which can in turn be further hydrolysed by lysophospholipases.
The most common class of phospholipase is
Phospholipase-A2, commercially available as Lecitase (ex
Novo Industri) and isolated from porcine pancreas glands.
Lecitase has an activity of 10,000 IU/ml, wherein 1 IU is defined as the amount of enzyme producing 1 microequivalent of free fatty acid per minute on an egg yolk emulsion substrate at 6mM calcium over 5-10 minutes at 400C, pH 8.0 (G de Haas et al, Biochim Biophys Acta 159, 105 (1968)). Molecular weight is approximately 14,000 and the enzyme has a high stability by virtue of its disulphide bridges.
Lecitase hydrolyses glycerophospholipids to yield a fatty acid and lysoglycerophospholipid.
Both of the reaction products are surface active and, accordingly, will assist in the removal of egg yolk and the prevention of spot formation. Thus, soil breakdown products themselves act in the removal of soils.
However, it has been found that the above described phospholipases require free calcium ions for enzyme activity at a sufficient level to break down phospholipids. In conventional machine dishwashing compositions the level of free Ca ions is generally very low because the compositions are usually built (pCa > 4-5).
Accordingly, such a class of phospholipase is generally thought impractical for machine compositions.
However, it has been found that PLA-2 may yield significant appearance benefits in dishwashing, when lecithin containing soils are present. In order to be of use in a built dishwashing system when egg yolk is present, it has been found that it is necessary to utilise a combination of PLA-2 and protease.
The phospholipase used in the system according to the invention may be as described above. It is preferred to use from 5-200 U/g of final detergent composition. This will be roughly 2000-1500 U/standard wash.
The protease can be the subtilisin variety sold as
Savinase (TM of Novo-Nordisk A/S) or Maxacal (TM of Gist
Brocades/IBIS) or as Opticlean (ex MKC) or AP122 (ex Showa
Denko), which has pI approximately 10. Other useful examples of protease include Maxatase, Esperase, Alcalase (Trade Marks), proteinase K and subtilisin BPN'.
Protease can for example be used in an amount ranging from about the order of 0.0002 to about the order of 0.05
Anson units per gram of the detergent composition.
Expressed in other units, the protease can also be included in the compositions in amounts of the order of from about 0.1 to 100 GU/mg detergent formulation.
Preferably, the amount ranges from 1 to 50 and particularly preferably from 5 to 20 GU/mg, although the upper level of protease is not critical to the invention.
A GU is a Glycine Unit, defined as the proteolytic enzyme activity which, under standard conditions, during a 15-minute-incubation at 40 deg C, with N-acetyl casein as substrate, produces an amount of NH2-group equivalent to 1 micromole of glycine.
The enzymes may be added in the form of a granular preparation or a slurry. The compositions may contain either crude or purified enzyme.
The composition of the invention may furthermore comprise the usual ingredients of dishwashing compositions, i.e. it may contain one or more alkali salts commonly used in dishwashing compositions. Thus, it may contain organic and/or inorganic builders such as the alkali metal ortho-, pyro- and tripolyphosphates and hexametaphosphates, zeolites, silicates, carbonates, borates, citrates, carboxymethyloxysuccinates, nitrilotriacetates, polymeric polyelectrolytes such as polyacrylates, polymaleates, and other known organic and inorganic builder compounds, together with combinations thereof.
Usually, the amount of builders in the composition varies from 10-90% by weight, generally from 20-70% by weight.
The composition may also contain a detergent-active compound. If a detergent-active compound is included, it is usually in an amount of from 0.5-10%, usually 1-5%.
Any well-known type of detergent-active compound may be used, such as soaps, synthetic anionic, nonionic, or amphoteric detergent surfactants and mixtures thereof.
Preferably, a nonionic detergent surfactant is used, especially a low-foaming one. Suitable examples of such nonionic detergent surfactants can easily be found in
M Schick, "Nonionic Surfactants" (1967).
The composition may furthermore contain other useful additives such as bleaching agents, bleaching agent activators, hydrotropes, fillers, perfumes, colouring agents, germicides, soil-suspending agents, drainage-promoting agents, threshold agents, aminopolyphosphonic acids and alkali metal or alkaline earth metal salts thereof, clays such as hectorites, anti-corrosion agents such as fatty acids and benztriazole. Other enzymes such as amylases and lipases may also be included.
As bleaching agents the peroxygen type bleaching agents, preferably with a bleach precursor such as TAED are suitable for inclusion in the machine dishwashing compositions. Chlorine based agents may not be used unless suitably separated from the enzymes by, eg encapsulation.
The composition of the present invention may be formulated as a powder, as a pourable aqueous or non-aqueous liquid or gel, as a tablet or cake, or in any other conventional form.
A typical example of a conventional powder machine dishwashing composition usually contains a phosphate or non-phosphate builder in an amount of from 20-60% by weight an alkali metal silicate in an amount of from 40-80% by weight or an alkali metal disilicate in an amount of from 5-308 by weight, a peroxy type bleaching agent in an amount of from 1-15% by weight, a low-foaming nonionic detergent surfactant in an amount of from 0.5-5% by weight, and minor ingredients such as perfumes, colouring agents, hydrotropes, fillers, etc.
A typical example of a conventional liquid machine dishwashing composition usually contains a phosphate or non-phosphate builder in an amount of from 1-30 wtt, a bleach in an amount equivalent to from 0.5 to 5 wtt available chlorine and a thixotropic thickener in an amount of from 0.5 to 5 wtt, the balance being water.
Minor ingredients as above may also be present.
Final rinse products may be produced containing phospholipase. Rinse aids are described in, eg,
EP 0 070 587 and EP 0 197 434.
The invention will be further described with reference to the following non-limiting Examples.
Example 1
In a test system, a 50:50 mix of a base composition of disilicate and citrate was used in a commercial dishwashing machine.
Detergent composition dose : 30 g
Water hardness : 16 OFH Main wash temperature : 65 OC 'Test soil : 0.15 g lecithin
The glasses were appraised by counting the average number of spots.
PLA-2 (ml at 11,000 U/ml) Number Spots > 60
0.025 30
0.05 30
0.1 10
0.3 10
0.5 10
It is seen that addition of PLA-2 causes a significant reduction in the number of spots caused by lecithin-based soil.
Example 2
When egg yolk is present, the combination of protease and PLA-2 is essential. In a machine experiment, using a base composition of a 50:50 mixture of disilicate and citrate the following results were obtained:
Number
Protease PLA-2 of Spots
80-100 0.2g Esp - 80-100 0.2g Esp 1100 U 60
(37 U/g) 0.2g Esp 2200 U < 10 0.2g Esp 4400 U < 10
Claims (2)
- Claims 1. An enzymatic dishwashing composition comprising from 10-80% by weight of a builder, characterised in that it further contains from 5-50 IU/g of composition of phospolipase A1 and/or A2.
- 2. A composition as claimed in claim 1 which further contains 1-50 GU/mg of composition of protease.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9017733A GB2247025A (en) | 1990-08-13 | 1990-08-13 | Enzymatic dishwashing and rinsing composition |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9017733A GB2247025A (en) | 1990-08-13 | 1990-08-13 | Enzymatic dishwashing and rinsing composition |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| GB9017733D0 GB9017733D0 (en) | 1990-09-26 |
| GB2247025A true GB2247025A (en) | 1992-02-19 |
Family
ID=10680589
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| GB9017733A Withdrawn GB2247025A (en) | 1990-08-13 | 1990-08-13 | Enzymatic dishwashing and rinsing composition |
Country Status (1)
| Country | Link |
|---|---|
| GB (1) | GB2247025A (en) |
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1997043376A1 (en) * | 1996-05-15 | 1997-11-20 | The Procter & Gamble Company | Detergent compositions comprising lipolytic enzymes |
| WO1998006810A1 (en) * | 1996-08-16 | 1998-02-19 | The Procter & Gamble Company | Detergent compositions comprising antibody controlled lipolytic activity |
| WO1999001531A1 (en) * | 1997-07-02 | 1999-01-14 | The Procter & Gamble Company | Dishwashing compositions comprising a phospholipase and an amylase |
| WO1999003962A1 (en) * | 1997-07-18 | 1999-01-28 | The Procter & Gamble Company | Detergent compositions comprising a phospholipase |
| WO2004097012A2 (en) | 2003-04-28 | 2004-11-11 | Novozymes A/S | Phospholipase and method of producing it |
| EP2113563A2 (en) | 1998-11-27 | 2009-11-04 | Novozymes A/S | Lipolytic enzyme variants |
| EP2119773A1 (en) | 2000-06-26 | 2009-11-18 | Novozymes A/S | Lipolytic enzymes from strains of fusarium and acremonium |
| EP2199386A1 (en) | 1993-10-08 | 2010-06-23 | Novozymes A/S | Amylase variants |
| WO2017220422A1 (en) * | 2016-06-23 | 2017-12-28 | Novozymes A/S | Use of enzymes, composition and method for removing soil |
| EP3511403A1 (en) * | 2016-05-09 | 2019-07-17 | The Procter & Gamble Company | Detergent composition |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0139329A2 (en) * | 1983-10-20 | 1985-05-02 | Unilever N.V. | Dishwashing compositions |
| EP0271155A2 (en) * | 1986-12-10 | 1988-06-15 | Unilever N.V. | Enzymatic dishwashing and rinsing process |
| EP0346137A1 (en) * | 1988-06-09 | 1989-12-13 | Unilever Plc | Enzymatic dishwashing composition |
-
1990
- 1990-08-13 GB GB9017733A patent/GB2247025A/en not_active Withdrawn
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0139329A2 (en) * | 1983-10-20 | 1985-05-02 | Unilever N.V. | Dishwashing compositions |
| EP0271155A2 (en) * | 1986-12-10 | 1988-06-15 | Unilever N.V. | Enzymatic dishwashing and rinsing process |
| EP0346137A1 (en) * | 1988-06-09 | 1989-12-13 | Unilever Plc | Enzymatic dishwashing composition |
Cited By (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2199386A1 (en) | 1993-10-08 | 2010-06-23 | Novozymes A/S | Amylase variants |
| WO1997043376A1 (en) * | 1996-05-15 | 1997-11-20 | The Procter & Gamble Company | Detergent compositions comprising lipolytic enzymes |
| WO1998006810A1 (en) * | 1996-08-16 | 1998-02-19 | The Procter & Gamble Company | Detergent compositions comprising antibody controlled lipolytic activity |
| WO1998007817A1 (en) * | 1996-08-16 | 1998-02-26 | The Procter & Gamble Company | Detergent compositions comprising antibody controlled lipolytic activity |
| WO1999001531A1 (en) * | 1997-07-02 | 1999-01-14 | The Procter & Gamble Company | Dishwashing compositions comprising a phospholipase and an amylase |
| WO1999003962A1 (en) * | 1997-07-18 | 1999-01-28 | The Procter & Gamble Company | Detergent compositions comprising a phospholipase |
| EP2290059A1 (en) | 1998-11-27 | 2011-03-02 | Novozymes A/S | Lipolytic enzyme variants |
| EP2302043A2 (en) | 1998-11-27 | 2011-03-30 | Novozymes A/S | Lipolytic enzyme variants |
| EP2113563A2 (en) | 1998-11-27 | 2009-11-04 | Novozymes A/S | Lipolytic enzyme variants |
| EP2236602A1 (en) | 1998-11-27 | 2010-10-06 | Novozymes A/S | Lipolytic enzyme variants |
| EP2287298A1 (en) | 1998-11-27 | 2011-02-23 | Novozymes A/S | Lipolytic enzyme variants |
| EP2287297A1 (en) | 1998-11-27 | 2011-02-23 | Novozymes A/S | Lipolytic enzyme variants |
| EP2716753A1 (en) | 1998-11-27 | 2014-04-09 | Novozymes A/S | Lipolytic enzyme variants |
| EP2290058A1 (en) | 1998-11-27 | 2011-03-02 | Novozymes A/S | Lipolytic enzyme variants |
| EP2298873A1 (en) | 1998-11-27 | 2011-03-23 | Novozymes A/S | Lipolytic enzyme variants |
| EP2302044A1 (en) | 1998-11-27 | 2011-03-30 | Novozymes A/S | Lipolytic enzyme variants |
| EP2119773A1 (en) | 2000-06-26 | 2009-11-18 | Novozymes A/S | Lipolytic enzymes from strains of fusarium and acremonium |
| WO2004097012A2 (en) | 2003-04-28 | 2004-11-11 | Novozymes A/S | Phospholipase and method of producing it |
| EP3511403A1 (en) * | 2016-05-09 | 2019-07-17 | The Procter & Gamble Company | Detergent composition |
| EP3372662B1 (en) * | 2016-05-09 | 2020-07-22 | The Procter & Gamble Company | Detergent composition |
| US10858616B2 (en) | 2016-05-09 | 2020-12-08 | The Procter & Gamble Company | Detergent composition |
| WO2017220422A1 (en) * | 2016-06-23 | 2017-12-28 | Novozymes A/S | Use of enzymes, composition and method for removing soil |
| CN109563449A (en) * | 2016-06-23 | 2019-04-02 | 诺维信公司 | Uses, compositions and methods for soil removal of enzymes |
| US11001787B2 (en) | 2016-06-23 | 2021-05-11 | Novozymes A/S | Use of enzymes, composition and method for removing soil |
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| Publication number | Publication date |
|---|---|
| GB9017733D0 (en) | 1990-09-26 |
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