EP0118933A1 - Stabilisierte wässrige Enzymzusammensetzung - Google Patents

Stabilisierte wässrige Enzymzusammensetzung Download PDF

Info

Publication number
EP0118933A1
EP0118933A1 EP84200157A EP84200157A EP0118933A1 EP 0118933 A1 EP0118933 A1 EP 0118933A1 EP 84200157 A EP84200157 A EP 84200157A EP 84200157 A EP84200157 A EP 84200157A EP 0118933 A1 EP0118933 A1 EP 0118933A1
Authority
EP
European Patent Office
Prior art keywords
composition
calcium
enzyme
sequestering agent
weight
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
Application number
EP84200157A
Other languages
English (en)
French (fr)
Other versions
EP0118933B1 (de
Inventor
Roland George Severson, Jr.
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Procter and Gamble Co
Original Assignee
Procter and Gamble Co
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Family has litigation
First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=23851028&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=EP0118933(A1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Application filed by Procter and Gamble Co filed Critical Procter and Gamble Co
Priority to AT84200157T priority Critical patent/ATE34767T1/de
Publication of EP0118933A1 publication Critical patent/EP0118933A1/de
Application granted granted Critical
Publication of EP0118933B1 publication Critical patent/EP0118933B1/de
Expired legal-status Critical Current

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
    • C11D3/38663—Stabilised liquid enzyme compositions

Definitions

  • the present invention relates to stabilized aqueous enzyme compositions which contain detergent components.
  • the stabilized aqueous enzyme compositions of this invention comprise: (a) from about 1% to about 75% of a non-soap detergent surfactant; (b) from about 0.01% to about 5% of an a-amylolytic enzyme, derived from Bacillus licheniformis; (c) from about 0.25% to about 40% of a sequestering agent; (d) a calcium-containing component to provide at least about 1 x 10 -4 5 millimoles of enzyme-accessible calcium ion per liter of said composition; and (e) from about 10% to about 80% water.
  • Proteolytic enzymes protease
  • amylolytic enzymes amylolytic enzymes (a-amylase) have proven to be very useful detergency adjuvants because of their ability to solubilize or otherwise degrade soils containing, respectively, protein and carbohydrate components.
  • detergency builder components The use of calcium to stabilize enzymes in aqueous media is well known, but this method of stabilization is in conflict with the incorporation of detergency builder components into liquid detergent compositions.
  • a major function of effective detergency builder components is to remove metal ions other than alkali metal ions from washing solutions by sequestration or precipitation. These undesirable metal ions, calcium and magnesium ions in particular, are generally designated water hardness.
  • the incorporation of such detergency builder components in a liquid detergent composition clearly complicates enzyme stability considerations.
  • an a-amylase can be stabilized in liquid detergent compositions containing calcium sequestering agents when said a-amylase is derived from Bacillus licheniformis (B. licheniformis) and a very low minimum level of "enzyme-accessible" calcium ion, as hereinafter defined, is provided by incorporation of a calcium-containing component in accordance with a mathematical formula involving the equilibrium constants of complexation of said calcium sequestering agents.
  • the non-soap detergent surfactant can be selected from ' nonionic, anionic, cationic, zwitterionic, amphoteric and semi-polar nonionic surfactants and mixtures thereof.
  • the surfactants preferably comprise from about 10% to about 65%, more preferably from about 20% to about 50% of the formula by weight.
  • nonionic surfactant is produced by condensing ethylene oxide with a hydrocarbon having a reactive hydrogen atom, e.g., a hydroxyl, carboxyl, amino, or amido group, in the presence of an acidic or basic catalyst.
  • Such nonionic surfactants have the general formula RA(CH 2 CH 2 O) n H wherein R represents the hydrophobic moiety, A represents the group carrying the reactive hydrogen atom and n represents the average number of ethylene oxide moieties.
  • R typically contains from about 8 to 22 carbon atoms, but can also be formed by the condensation of propylene oxide with a lower molecular weight compound.
  • n can vary from about 2 to about 24 depending on the desired physical and detergency properties.
  • the hydrophobic moiety of the nonionic compound is preferably a primary or secondary, straight or slightly branched, aliphatic alcohol having from about 8 to about 24, preferably from about 12 to about 20 carbon atoms.
  • Alkyl amine oxides and other semi-polar nonionic surfactants are hereinafter described.
  • Another class of useful nonionic surfactants are alkylpolysaccharides having a hydrophobic group containing from about 8 to about 20 carbon atoms and a polysaccharide hydrophilic group containing from about 1.5 to about 10 saccharide units.
  • Synthetic anionic surfactants can be represented by the general formula R 1 SO 3 M wherein R represents a hydrocarbon group selected from the group consisting of straight or branched alkyl radicals containing from about 8 to about 24 carbon atoms and alkyl phenyl radicals containing from about 9 to about 15 carbon atoms in the alkyl group.
  • M is a salt forming cation which typically is selected from the group consisting of sodium, potassium, ammonium, monoalkanolammonium, dialkanolammonium, trialkanolammonium, and magnesium cations and mixtures thereof.
  • Preferred synthetic anionic surfactants include the water-soluble salts of alkylbenzene sulfonic acid containing from about 9 to about 15 carbon atoms in the alkyl group and water-soluble alkyl sulfates containing from about 10 to about 18 carbon atoms.
  • Another preferred synthetic anionic surfactant is a water-soluble salt of an alkyl polyethoxylate ether sulfate wherein the alkyl group contains from about 8 to about 24, preferably from about 10 to about 18 carbon atoms and there are from about 1 to about 20, preferably from about 1 to about 12 ethoxy groups.
  • alkyl group contains from about 8 to about 24, preferably from about 10 to about 18 carbon atoms and there are from about 1 to about 20, preferably from about 1 to about 12 ethoxy groups.
  • Other suitable anionic surfactants are disclosed in U.S. Patent 4,170,565, Flesher et al, issued October 9, 1979, incorporated herein by reference.
  • Suitable cationic surfactants have the general formula wherein each R 4 is an organic group containing a straight or branched alkyl or alkenyl group optionally substituted with up to three phenyl or hydroxy groups and optionally interrupted by up to four structures selected from the group consisting of and mixtures thereof, each R 2 containing from about 8 to 22 carbon atoms, and which may additionally contain up to about 12 ethylene oxide groups, m is a number from 1 to 3, each R 3 is an alkyl or hydroxyalkyl group containing from 1 to 4 carbon atoms or a benzyl group with no more than one R 3 in a molecule being benzyl, x is a number from 0 to 11, the remainder of any carbon atoms positions being filled by hydrogens, Y is selected from the group consisting of: wherein p is from 1 to 12, wherein p is from 1 to 12, and (9) mixtures thereof and Z is an anion such as halide, methyl sulfate or hydroxide.
  • One R 3 can also be a proton.
  • the resultant tertiary amines can have characteristics similar to cationic surfactants at washing soultion pH values less than about 8.5.
  • a type of cationic surfactant generally compatible with anionic surfactants is a C8-18 alkyl tri C l-3 alkyl ammonium chloride or methyl sulfate.
  • Zwitterionic surfactants include derivatives of aliphatic quaternary ammonium, phosphonium, and sulfonium compounds in which the aliphatic moiety can be straight or branched chain and wherein one of the aliphatic substitutents contains from about 8 to 24 carbon atoms and one contains an anionic water-solubilizing group.
  • Particularly preferred zwitterionic materials are the ethoxylated ammonium sulfonates and sulfates disclosed in U.S. Patents 3,925,262, Laughlin et al, issued December 9, 1975 and 3,929,678, Laughlin et al, issued December 30, 1975, said patents being incorporated herein by reference.
  • Ampholytic surfactants include derivatives of aliphatic heterocyclic secondary and ternary amines in which the aliphatic moiety can be straight chain or branched and wherein one of the aliphatic substituents contains from about 8 to about 24 carbon atoms and at least one aliphatic substituent contains an anionic water-solubilizing group.
  • Semi-polar nonionic surfactants include water-soluble amine oxides containing 1 alkyl or hydroxy alkyl moiety of from about 8 to about 28 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxy alkyl groups, containing from 1 to about 3 carbon atoms which can optionally be joined into ring structures; water-soluble phosphine oxides containing 1 alkyl or hydroxy alkyl moiety of from about 8 to about 28 and 2 moieties selected from the group consisting of alkyl groups and hydroxy alkyl groups, containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing 1 alkyl or hydroxy alkyl moiety of from about 8 to about 28 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxy alkyl moieties of from 1 to 3 carbon atoms.
  • compositions of the invention contain from about 0.01% to about 5% by weight on a standard enzyme basis of an a-amylolytic enzyme (a-amylase) derived from B. licheniformis, preferably from about 0.05% to about 2% by weight and most preferably from about 0.1% to about 1.0% by weight.
  • a-amylase a-amylolytic enzyme
  • Commercial enzyme preparations particularly those prepared for use in detergent compositions, are rarely pure enzyme and are, in any case, generally mixed with various inert materials.
  • Commercial enzyme preparations will typically have a low calcium metal content complexed with the enzyme and as part of the inert portion of the preparation. As described hereinafter, this calcium content must be recognized for stability considerations.
  • standard enzyme basis is defined as an enzyme preparation having an activity measured in Kilo Novo a-amylase Units (KNU) of 120 KNU/gram.
  • KNU Kilo Novo a-amylase Units
  • One Kilo Novo a-amylase Unit (1 KNU) is the amount of enzyme which breaks down 5.26 grams of starch (Merck, Amylum Solubile Erg. B.
  • a-Amylases derived.from B. licheniformis have been characterized as carbohydrases and more particularly 1,4-a-D-Glucan Glucanohydrolase.
  • a-Amylases for use in detergent compositions, granule detergent compositions in particular have been generally derived from Bacillus subtilis, but a-amylase derived from B. licheniformis suitable for use in the compositions of the present invention is available from a number of sources.
  • Termamylo 120L Novo Industri A/S, Bagsvaerd, Denmark; Taka-Therm® L-340, Miles Laboratories, Elkhart, Indiana; Rohalase AT®, Rohm & Haas, West Philadelphia, PA; Maxamyl HTO, Gist Brocades, Delft, The Netherlands, are a-amylases derived from B. licheniformis and suitable for use in the compositions of the present invention.
  • Reported deposit numbers for Bacillus licheniformis capable of producing a-amylase are NCIB 8061, NCIB 8059, ATCC 6634, ATCC 6598, ATCC 11945, ATCC 8480, and ATCC 9945a.
  • British Patent Specification 1,296,839 published November 22, 1972, incorporated herein by reference, discloses methods of making a-amylases derived from B. licheniformis.
  • compositions of the invention contain from about 0.25% to about 40%, preferably from about 3% to about 30% and most preferably from about 5% to about 25% of a calcium ion sequestering agent.
  • sequestering agents act as detergency builders to improve cleaning, particularly when the washing solution will contain metal ions other than alkali metal ions. Sequestration involves the formation of a coordination complex of the sequestering agent and metallic ions in solution to reduce the interactions of calcium with other materials in the wash solution.
  • the term sequestering agent includes multidentate ligands which can act as chelating agents and can include some ion exchange materials, but not those detergency builder materials which remove calcium ions from solutions only by precipitation reactions.
  • the sequestering agents used in the compositions of this invention include polyphosphates, polyphosphonates and polycarboxylates in soluble salt or acid form.
  • Polyphosphonates comprise a large range of organic compounds having two or more - groups, wherein M is a hydrogen or a salt-forming radical.
  • Suitable phosphonates include ethane-1-hydroxy-1,1-di- phosphonates, ethanehydroxy-1,1,2-triphosphonates and their oligomeric ester chain condensates.
  • Particularly suitable polyphosphonates for use in the compositions of the invention are nitrogen-containing polyphosphonates such as ethylenediaminetetramethylene phosphonic acid and diethylenetriaminepentamethylene phosphonic acid and alkali metal, ammonium and substituted ammonium salts thereof.
  • Suitable polycarboxylates include the acid form and alkali.metal, ammonium and substituted ammonium salts of citric, ascorbic, phytic, mellitic, benzene pentacar- boxylic, oxydiacetic, carboxymethyloxysuccinic, car- boxymethyloxymalonic, cis-cyclohexanehexacarboxylic, cis-cyclopentanetetracarboxylic and oxydisuccinic acids. Also suitable are the polycarboxylate materials described in U.S. Patent 3,364,103 and polycarboxylate polymers and copolymers described in U.S. Patent 3,308,067, Diehl, issued March 7, 1967, both patents incorporated herein by reference.
  • Particularly suitable polycarboxylates are those containing nitrogen such as ethylenediaminetetraacetic acid, hydroxyethylenediaminetriacetic acid, diethylenetriaminepentaacetic acid and nitrilotriacetic acid and alklai metal, ammonium and substituted ammonium salts - thereof.
  • combinations of sequestering agents with different degrees of calcium ion sequestering power are particularly useful in the practice of this invention.
  • the combinations of citric acid and a nitrogen-containing sequestering agent selected from the group consisting of ethylenediamine tetramethylene phosphonic acid, diethylenetriamine pentamethylenephosphonic acid, nitrilotriacetic acid, ethylenediaminetetraacetic acid, hydroxyethylenediaminetriacetic acid, diethylenetriaminepentaacetic acid or mixtures and suitable salts thereof are particularly preferred.
  • Citric acid has a relatively lower equilibrium constant of complexation with calcium than the nitrogen-containing sequestering agents recited above.
  • Preferred ratios of citric acid to the nitrogen-containing sequestering agent are from about 50:1 to about 1:2 by weight and, more preferably, from about 30:1 to about 2:1 by weight.
  • the stabilized aqueous enzyme compositions of this invention comprise a calcium-containing component to provide at least about 1x10-4.5 millimoles of enzyme-accessible calcium, as hereinafter defined, per liter of said composition.
  • a calcium-containing component to provide at least about 1x10 -4 millimoles of enzyme-accessible calcium and more preferably at least about 1x10 -3 millimoles.
  • the compositions contain at least about 1x10 -2 millimoles of enzyme-accessible calcium per liter of said composition.
  • the calcium-containing component can be or can be part of other essential or optional components, for example, an anionic surfactant in the form of a calcium salt or a calcium-sequestering agent complex. More - typically, water-soluble or solubilizable calcium salts such as calcium chloride are employed. In the aqueous liquid detergent compositions of the present invention, calcium in different forms, insoluble, sequestered and enzyme-accessible, will reach an equilibrium as a function of the composition components and pH without regard to the initial nature of the calcium-containing component.
  • a upper limit of enzyme-accessible calcium in compositions of the invention can be set by practical considerations not related to enzyme stability. There is little improvement in the stability of alpha-amylase derived from B.licheniformis in compositions of the invention at enzyme-accessible calcium levels above 1x10 millimoles per liter. In the preferred compositions of the invention this level of enzyme-accessible calcium is provided by total calcium levels of no more than about from 0.1% to about 0.3% of the composition by weight. At a recommended usage of 1/2 cup of the composition in a washing machine with a 18 gallon washing solution capacity, 0.18% total calcium (from 0.5% CaCl 2 ) increases water hardness of the washing solution by about 1/2 grain per gallon (as CaC0 3 ).
  • Calcium is generally detrimental to detergency, but 1/2 grain/gal- lon is almost negligible.
  • the calcium-containing component partially depletes the sequestering capacity of the sequestering agent or agents of the composition in so far as calcium is concerned.
  • a calcium-sequestering agent complex is nevertheless capable of sequestering heavy metal ions such as iron, manganese and copper which are associated with certain staining problems. This is a result of higher complexation and formation constants of said sequestering agents with heavy metal ions relative to the constants with calcium.
  • Enzyme-accessible calcium is analagous to free or ionic calcium in aqueous solutions of less complexity than the compositions of the invention.
  • enzyme-accessible calcium is determined by the method described in the following publication:
  • alkaline earth metals other than calcium are substantially less effective for stabilizing the compositions of the invention.
  • compositions of this invention contain from about 10% to about 80% water, preferably from about 15% to about 60% water, by weight.
  • Preferred compositions have a pH of from about 6.5 to about 9.0.
  • compositions of this invention can contain components other than those disclosed as essential.
  • compositions of this invention can contain enzymes other than a-amylase derived from B.licheniformis, proteolytic enzymes in particular.
  • suitable proteolytic enzymes include many enzyme preparations adapted for use in detergent compositions and, in fact, used in detergent compositions.
  • Sources of the enzymes include commercial enzyme preparations such as Alcalasee sold by Novo Industries, A/S, Copenhagen, Denmark and Maxatasee sold by Gist-Brocades, Delft, The Netherlands.
  • Other preferred enzyme compositions include those commercially available under the tradenames Esperasee, manufactured and sold by Novo Industries, A/S, Copenhagen, Denmark and "AZ-Protease” manufactured and sold by Gist-Brocades, Delft, The Netherlands..
  • levels of enzyme accessible calcium above about lxlO -2 millimoles per liter provide excellent stability to proteolytic enzymes (proteases) incorporated in the compositions of the invention and the inclusion of a proteolytic enzyme is a preferred embodiment. There is, however, no dramatic increase in proteolytic enzyme stability over any narrow range of enzyme-accessible calcium levels as is seen with a-amylase (derived from B.licheniformis) between 1x10 -5 and 1x10 -4 .
  • compositions of this invention can contain solvents other than water.
  • Low molecular weight primary or secondary alcohol exemplified by methanol, ethanol, propanol, and isopropanol are suitable.
  • Monohydric alcohols are preferred for solubilizing the surfactant but polyols containing from 2 to about 6 carbon atoms and from 2 to about 6 hydroxy groups can be used and can provide improved enzyme stability.
  • polyols include propylene glycol, ethylene glycol, glycerine and 1,2-propanediol.
  • Ethanol is a particularly preferred alcohol.
  • the compositions contain from 0% to about 30%, preferably from about 1% to about 15%, of alcohols.
  • a short chain carboxylic acid salt can be used to stabilize enzymes, particularly proteolytic enzymes, as disclosed in U.S. Patent 4,318,818, issued March 9, 1982.
  • the short chain carboxylic acid salt preferably is a formate, e.g., formic acid and its salts.
  • the formates are surprisingly much more effective than other short chain carboxylic salts such as the acetates and the propionates.
  • the short chain carboxylic acid salt is used at a level from about 0.1% to about 10%, preferably from about 0.3% to about 3%, more preferably from about 0.5% to about 2.0% when the product pH is below about 8.5 and from about 3% to about 10%, preferably from about 4% to about 8%, when the product pH is from about 8.5 to about 10.
  • a fatty acid component is incorporated in an amount of from about 3% to about 25% by weight, preferably from about 5% to about 20% by weight.
  • the fatty acids have from 10 to 22, preferably from 12 to 18 carbon atoms in the alkyl chain.
  • Compositions containing fatty acids will have a pH of from about 6.5 to about 9.0.
  • compositions of the invention can contain such materials as fabric whiteners and brighteners, sudsing control agents, hydrotropes such as sodium toluene or xylene sulfonate, perfumes, colorants, opacifiers, anti-redeposition agents and alkalinity control or buffering agents such as monoethanolamine and triethanolamine.
  • materials such as fabric whiteners and brighteners, sudsing control agents, hydrotropes such as sodium toluene or xylene sulfonate, perfumes, colorants, opacifiers, anti-redeposition agents and alkalinity control or buffering agents such as monoethanolamine and triethanolamine.
  • the use of these materials is well known in the detergent art.
  • Materials or anions that tend to precipitate calcium should preferably be restricted to minimum levels. Examples are carbonates, sulfates, and orthophosphates.
  • the fatty acids of preferred compositions act to precipitate calcium in a washing solution, they have no such effect in the undiluted compositons of the invention if calcium levels are controlled carefully.
  • the fatty acid content of the compositions of the invention at least at pH values below 8.5, does not substantially effect the enzyme-accessible calcium level of said compositions and can be neglected when calculating the enzyme-accessible calcium level as disclosed hereinbefore.
  • Liquid detergent compositions were prepared by mixing the components listed hereinafter in the stated proportions.
  • Composition A was prepared in thirteen variations with CaCl 2 and sodium diethylenetriaminepentaacetate (DTPA) levels as indicated. The variations were stored in airtight containers for 1 week at 100°F. a-amylase activity was then measured by Technicon Industrial Method #500-77P dated September 12, 1977, as revised September 1979, (Technicon Industrial Systems, Tarry- town, N.Y. 10591), but any suitable method such as the one described in U.S. Patent 4,284,722 issued August 18, 1981, to Tamuri et al, incorporated herein by reference, will give equivalent results. a-amylase activity at the - end of the storage period was divided by activity directly after composition preparation to calculate percent retained activity.
  • DTPA sodium diethylenetriaminepentaacetate
  • Composition A - a-Amylase Stability
  • Composition B was prepared in seven variations with CaCl 2 levels as indicated. The variations were stored for 1 month at 90°F and at 70°F and evaluated for a-amylase stability in the same manner as the variations of Composition A.
  • results show the dramatic improvement in a-amylase (derived from B.licheniformis) stability in an aqueous liquid detergent composition when a calcium-containing component is incorporated that provides at least about 1x10 -4.5 millimoles of enzyme-accessible calcium.
  • the results also point out the advantage of mixtures of sequestering agents.
  • a sequestering agent with high equilibrium constant of complexation e.g., the nitrogen-containing sequestering agents disclosed hereinbefore, will tend to sequester all available calcium to the point of theoretical capacity, but can release such calcium in washing solutions to in turn sequester heavy metal ions such as copper, iron and manganese.
  • a sequestering agent with a lower equilibrium constant of complexation such as alkali metal citrates or citric acid can be incorporated in the compositions of the invention without addition of calcium-containing components at a level to satisfy theoretical capacity.
  • sequestering agents - are available to act as detergency builders effective in the presence of alkaline earth metal ions in washing solutions.
  • a-amylase derived from B.licheniformis has, in effect, an equilibrium constant of complexation with calcium somewhat greater than citrate, or more precisely, an equilibrium constant that can hold sufficient calcium for stabilization in an aqueous solution containing at least about 1x10 -4.5 millimoles of enzyme accessible calcium.
  • a-amylases derived by B.subtilis, Bane from Novo Industri and Rapidasee from Gist Brocade are incorporated in the compositions of Example I replacing the Termamyl R120L. It is not possible to add a sufficient amount of a calcium-containing component to stabilize said a-amylases derived from B.subtilis without precipitation of calcium citrate in the aqueous liquid detergent compositions.
  • Dodecyldimethyamine oxide replaces C 12 alkyltrimethylammonium chloride in the compositions of Example I. Equivalent results are obtained.
  • compositions are prepared by mixing the ingredients listed. -
  • incorporation of 0.02% calcium chloride in each composition provides an enzyme accessible calcium level of at least 1x10 -4.5 millimoles per liter.
  • Potassium pyrophosphate, potassium carboxymethyl- oxymalonate and potassium carboxymethyloxysuccinate are - each substituted for citric acid in Examples I, II and IV.
  • Composition pH is adjusted to 8.0.
  • a calcium chloride level of 0.3% by weight is sufficient to provide an enzyme-accessible calcium level greater than 1x10 4.5 millimoles and stabilize the a-amylase derived from B.licheniformis incorporated in said compositions.

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)
  • Compositions Of Macromolecular Compounds (AREA)
EP84200157A 1983-02-14 1984-02-06 Stabilisierte wässrige Enzymzusammensetzung Expired EP0118933B1 (de)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AT84200157T ATE34767T1 (de) 1983-02-14 1984-02-06 Stabilisierte waessrige enzymzusammensetzung.

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US46624383A 1983-02-14 1983-02-14
US466243 1983-02-14

Publications (2)

Publication Number Publication Date
EP0118933A1 true EP0118933A1 (de) 1984-09-19
EP0118933B1 EP0118933B1 (de) 1988-06-01

Family

ID=23851028

Family Applications (1)

Application Number Title Priority Date Filing Date
EP84200157A Expired EP0118933B1 (de) 1983-02-14 1984-02-06 Stabilisierte wässrige Enzymzusammensetzung

Country Status (9)

Country Link
EP (1) EP0118933B1 (de)
JP (1) JPS59206497A (de)
AT (1) ATE34767T1 (de)
AU (1) AU575313B2 (de)
CA (1) CA1213541A (de)
DE (1) DE3471687D1 (de)
GR (1) GR81415B (de)
IE (1) IE57055B1 (de)
MX (1) MX161307A (de)

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0199404A2 (de) * 1985-04-15 1986-10-29 The Procter & Gamble Company Flüssige Reinigungsmittel mit einer anionischen oberflächenaktiven Verbindung, einem Verstärker und einem proteolytischen Enzym
EP0268227A2 (de) * 1986-11-17 1988-05-25 Henkel Kommanditgesellschaft auf Aktien Verfahren zur Reinigung und Desinfektion von Endoskopen und Mittel zur Durchführung des Verfahrens
EP0342499A2 (de) * 1988-05-17 1989-11-23 Henkel Kommanditgesellschaft auf Aktien Verfahren zur Reinigung und Desinfektion von hitze- und korrosionsempfindlichen medizinischen Geräten, insbesondere von Endoskopen und Mittel zur Durchführung des Verfahrens
US5223166A (en) * 1986-11-17 1993-06-29 Henkel Kommanditgesellschaft Auf Aktien Preparations and processes for cleaning and disinfecting endoscopes
US5269960A (en) * 1988-09-25 1993-12-14 The Clorox Company Stable liquid aqueous enzyme detergent
US5605881A (en) * 1993-09-03 1997-02-25 Minolta Co., Ltd. Cleaning liquid for recycling copy medium for electrophotography

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP3081534B2 (ja) * 1995-12-22 2000-08-28 花王株式会社 酵素含有造粒物、その製造法及びこれを含有する組成物
DK3615041T3 (da) * 2017-04-25 2022-04-04 Nutreco Ip Assets Bv Calciumbindemiddel til brug for at forhindre dødfødsel

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2025748A1 (de) * 1969-05-29 1970-12-10 Novo Terapeutisk Laboratorium A/S, Kopenhagen Herstellung von Enzymen aus Mikroorganismen
US4111855A (en) * 1976-03-08 1978-09-05 The Procter & Gamble Company Liquid enzyme containing detergent composition
EP0028866A1 (de) * 1979-11-09 1981-05-20 THE PROCTER & GAMBLE COMPANY Eine Formate und Calciumionen enthaltende stabile, wässrige Enzymzusammensetzung
US4305837A (en) * 1980-10-30 1981-12-15 The Procter & Gamble Company Stabilized aqueous enzyme composition

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2633601A1 (de) * 1976-07-27 1978-02-02 Henkel Kgaa Fluessiges, als wasch- und reinigungsmittel verwendbares, enzymhaltiges konzentrat
US4287082A (en) * 1980-02-22 1981-09-01 The Procter & Gamble Company Homogeneous enzyme-containing liquid detergent compositions containing saturated acids
US4529525A (en) * 1982-08-30 1985-07-16 Colgate-Palmolive Co. Stabilized enzyme-containing detergent compositions

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2025748A1 (de) * 1969-05-29 1970-12-10 Novo Terapeutisk Laboratorium A/S, Kopenhagen Herstellung von Enzymen aus Mikroorganismen
US4111855A (en) * 1976-03-08 1978-09-05 The Procter & Gamble Company Liquid enzyme containing detergent composition
EP0028866A1 (de) * 1979-11-09 1981-05-20 THE PROCTER & GAMBLE COMPANY Eine Formate und Calciumionen enthaltende stabile, wässrige Enzymzusammensetzung
US4305837A (en) * 1980-10-30 1981-12-15 The Procter & Gamble Company Stabilized aqueous enzyme composition

Cited By (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0199404A2 (de) * 1985-04-15 1986-10-29 The Procter & Gamble Company Flüssige Reinigungsmittel mit einer anionischen oberflächenaktiven Verbindung, einem Verstärker und einem proteolytischen Enzym
EP0199404A3 (en) * 1985-04-15 1988-08-31 The Procter & Gamble Company Liquid detergents containing anionic surfactant, builder and proteolytic enzyme
EP0268227A2 (de) * 1986-11-17 1988-05-25 Henkel Kommanditgesellschaft auf Aktien Verfahren zur Reinigung und Desinfektion von Endoskopen und Mittel zur Durchführung des Verfahrens
JPS63135123A (ja) * 1986-11-17 1988-06-07 ヘンケル・コマンディットゲゼルシャフト・アウフ・アクチェン 内視鏡の洗浄殺菌方法および製剤
EP0268227A3 (de) * 1986-11-17 1989-12-20 Henkel Kommanditgesellschaft auf Aktien Verfahren zur Reinigung und Desinfektion von Endoskopen und Mittel zur Durchführung des Verfahrens
US5223166A (en) * 1986-11-17 1993-06-29 Henkel Kommanditgesellschaft Auf Aktien Preparations and processes for cleaning and disinfecting endoscopes
EP0342499A2 (de) * 1988-05-17 1989-11-23 Henkel Kommanditgesellschaft auf Aktien Verfahren zur Reinigung und Desinfektion von hitze- und korrosionsempfindlichen medizinischen Geräten, insbesondere von Endoskopen und Mittel zur Durchführung des Verfahrens
EP0342499A3 (en) * 1988-05-17 1990-05-09 Henkel Kommanditgesellschaft Auf Aktien Method for cleaning and disinfecting heat and corrosion sensitive medical devices, especially endoscopes, and product for carrying out the method
US5234832A (en) * 1988-05-17 1993-08-10 Henkel Kommanditgesellschaft Auf Aktien Process for cleaning and disinfecting heat and corrosion sensitive medical instruments
US5269960A (en) * 1988-09-25 1993-12-14 The Clorox Company Stable liquid aqueous enzyme detergent
US5605881A (en) * 1993-09-03 1997-02-25 Minolta Co., Ltd. Cleaning liquid for recycling copy medium for electrophotography

Also Published As

Publication number Publication date
ATE34767T1 (de) 1988-06-15
AU2453884A (en) 1984-08-23
AU575313B2 (en) 1988-07-28
IE57055B1 (en) 1992-04-08
CA1213541A (en) 1986-11-04
JPS59206497A (ja) 1984-11-22
IE840321L (en) 1984-08-14
GR81415B (de) 1984-12-11
DE3471687D1 (en) 1988-07-07
EP0118933B1 (de) 1988-06-01
MX161307A (es) 1990-09-06

Similar Documents

Publication Publication Date Title
US5591703A (en) Liquid or granular automatic diswashing detergent compositions containing builder, enzyme and low molecular weight, modified polyacrylate copolymers
US4287082A (en) Homogeneous enzyme-containing liquid detergent compositions containing saturated acids
US4305837A (en) Stabilized aqueous enzyme composition
US4318818A (en) Stabilized aqueous enzyme composition
US4537706A (en) Liquid detergents containing boric acid to stabilize enzymes
US4900475A (en) Stabilized built liquid detergent composition containing enzyme
US3557002A (en) Stabilized aqueous enzyme preparation
US5597789A (en) Liquid or granular automatic dishwashing detergent compositions containing silicate and low molecular weight modified polyacrylate coploymers
GB2168375A (en) Stabilized enzyme-containing detergent compositions
EP0703974B1 (de) Konzentriertes phosphatfreies flüssiges enzymhaltiges maschinengeschirrspülmittel
EP0028865B1 (de) Homogene, Enzym enthaltende, flüssige Reinigungsmittelzusammensetzungen, die gesättigte Fettsäuren enthalten
WO2014037344A1 (de) Wasch- oder reinigungsmittel mit verbesserter enzymleistung
EP0318279B1 (de) Zusammensetzungen für Geschirrspülmaschinen
US4842769A (en) Stabilized fabric softening built detergent composition containing enzymes
JPH02227500A (ja) 酵素系液体洗剤組成物
CA1297440C (en) Fabric softening liquid detergent
EP0118933B1 (de) Stabilisierte wässrige Enzymzusammensetzung
US4652394A (en) Built single phase liquid anionic detergent compositions containing stabilized enzymes
FI61716C (fi) Enzymer innehaollande vattenhaltig flytande detergentkomposition som uppvisar aennu baettre lagerhaollbarhet
GB2140818A (en) Stabilized built single-phase liquid detergent composition containing enzymes
EP0028866B1 (de) Eine Formate und Calciumionen enthaltende stabile, wässrige Enzymzusammensetzung
GB2178054A (en) Stabilized built liquid detergent composition containing enzymes
EP0162033A2 (de) Borsäure enthaltende flüssige Reinigungsmittel zur Stabilisierung von Enzymen
JP7138552B2 (ja) 繊維製品用の液体洗浄剤組成物
JPH05179291A (ja) 液体洗浄剤組成物

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

Designated state(s): AT BE CH DE FR GB IT LI NL SE

17P Request for examination filed

Effective date: 19850307

GRAA (expected) grant

Free format text: ORIGINAL CODE: 0009210

AK Designated contracting states

Kind code of ref document: B1

Designated state(s): AT BE CH DE FR GB IT LI NL SE

REF Corresponds to:

Ref document number: 34767

Country of ref document: AT

Date of ref document: 19880615

Kind code of ref document: T

ITF It: translation for a ep patent filed
REF Corresponds to:

Ref document number: 3471687

Country of ref document: DE

Date of ref document: 19880707

ET Fr: translation filed
PLBI Opposition filed

Free format text: ORIGINAL CODE: 0009260

26 Opposition filed

Opponent name: HENKEL KOMMANDITGESELLSCHAFT AUF AKTIEN

Effective date: 19890227

NLR1 Nl: opposition has been filed with the epo

Opponent name: HENKEL KOMMANDITGESELLSCHAFT AUF AKTIEN

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: GB

Payment date: 19910125

Year of fee payment: 8

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: SE

Payment date: 19910208

Year of fee payment: 8

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: FR

Payment date: 19910212

Year of fee payment: 8

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: AT

Payment date: 19910214

Year of fee payment: 8

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: CH

Payment date: 19910227

Year of fee payment: 8

ITTA It: last paid annual fee
PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: NL

Payment date: 19910228

Year of fee payment: 8

Ref country code: DE

Payment date: 19910228

Year of fee payment: 8

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: BE

Payment date: 19910403

Year of fee payment: 8

RDAG Patent revoked

Free format text: ORIGINAL CODE: 0009271

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: PATENT REVOKED

REG Reference to a national code

Ref country code: CH

Ref legal event code: PL

27W Patent revoked

Effective date: 19910516

GBPR Gb: patent revoked under art. 102 of the ep convention designating the uk as contracting state
NLR2 Nl: decision of opposition
BERE Be: lapsed

Owner name: THE PROCTER & GAMBLE CY

Effective date: 19920228

EUG Se: european patent has lapsed

Ref document number: 84200157.0

Effective date: 19911002