EP0662121B1 - Reinigungsverfahren - Google Patents

Reinigungsverfahren Download PDF

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Publication number
EP0662121B1
EP0662121B1 EP93920792A EP93920792A EP0662121B1 EP 0662121 B1 EP0662121 B1 EP 0662121B1 EP 93920792 A EP93920792 A EP 93920792A EP 93920792 A EP93920792 A EP 93920792A EP 0662121 B1 EP0662121 B1 EP 0662121B1
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EP
European Patent Office
Prior art keywords
cleaning medium
enzyme
process according
aqueous cleaning
enzymatic
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Expired - Lifetime
Application number
EP93920792A
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English (en)
French (fr)
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EP0662121A1 (de
Inventor
Johan Haverkamp
Pieter Van Der Vlist
Marinus Maria C. G. Warmoeskerken
Simon Willemse
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.)
Unilever PLC
Unilever NV
Original Assignee
Unilever PLC
Unilever NV
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Publication date
Application filed by Unilever PLC, Unilever NV filed Critical Unilever PLC
Priority to EP93920792A priority Critical patent/EP0662121B1/de
Publication of EP0662121A1 publication Critical patent/EP0662121A1/de
Application granted granted Critical
Publication of EP0662121B1 publication Critical patent/EP0662121B1/de
Anticipated expiration legal-status Critical
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    • 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
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • 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
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/40—Specific cleaning or washing processes
    • C11D2111/46—Specific cleaning or washing processes applying energy, e.g. irradiation

Definitions

  • This invention relates to a cleaning process, and more in particular to a process for cleaning soiled articles such as fabrics, using an ultrasonic energy source.
  • the invention relates to a process whereby soiled articles are immersed in an enzymatic aqueous cleaning medium and radiated with ultrasonic energy.
  • EP-A-0,320,852 discloses a process for cleaning articles whereby soiled articles are immersed in an aqueous medium comprising lipase and radiated with ultrasonic energy.
  • numerous publications relate to ultrasonic fabric washing processes.
  • the aqueous cleaning medium usually contains one or more conventional ingredients of detergent products such as surfactants, builders and the like.
  • EP-A-258 816 discloses a ultrasonic fabric washing process wherein the wash load is treated with a cleaning medium having such a strong wetting capacity that the wash load is thoroughly wetted and deaerated.
  • EP-A-258 816 (Henkel) suggests the use of an enzymatic aqueous medium in an ultrasonic fabric washing process.
  • Suitable enzymes are in particular alkaline proteases. It is shown that the presence of an alkaline protease in the wash liquor has a beneficial effect on the cleaning performance of the detergent product in an ultrasonic washing process.
  • amylases lipases, pectinases, nucleases and/or oxydoreductases can also be used.
  • JP-A-01026779 discloses an ultrasonic fabric washing process whereby the cleaning solution contains a cellulase enzyme.
  • a process for cleaning articles whereby soiled articles are immersed in an enzymatic aqueous cleaning medium and radiated with ultrasonic energy, wherein the cleaning medium comprises an enzyme capable of hydrolysing mono-, di- or triglyceride, characterised in that the enzyme has an activity of 0.1 to 500 LU/ml and the cleaning medium further comprises surface active agents.
  • soiled articles such as fabrics are immersed in an enzymatic aqueous cleaning medium and radiated with ultrasonic energy.
  • the principles of ultrasonic washing are well known in the art and can, for instance, be derived from the earlier mentioned EP-A-258 816 (Henkel).
  • ultrasonic energy for the purpose of this application we define ultrasonic energy as usually involving frequencies of about 10 kilo Hertz (kHz) to about 100 kHz, however, higher frequencies of up to 10 mega Hertz (MHz) may also be used.
  • ultrasonic energy will be applied to the enzymatic aqueous cleaning medium for about 15 minutes or less, preferably between 0.25 to 10 minutes and more preferably between 0.5 to 5 minutes.
  • the wash load may be agitated slowly, preferably during "pulsing periods", i.e. periods in which no ultrasonic energy is applied to the wash load.
  • the enzymatic aqueous cleaning medium used in the present process comprises 0.05 to 50 g/l, preferably 0.1 to 10 g/l (most preferably up to 5 g/l) of a conventional detergent composition, which includes conventional detergent ingredients such as surface active agents, builders, etc..
  • the surface active agents may be chosen from the surfactants described in "Surface Active Agents” Vol. 1, by Schwartz & Perry, Interscience 1949, Vol. 2 by Schwartz, Perry & Berch, Interscience 1958, in the current edition of "McCutcheon's Emulsifiers and Detergents” published by Manufacturing Confectioners Company or in "Tenside-Taschenbuch", H. Stache, 2nd Edn., Carl Hauser Verlag, 1981.
  • the surfactants preferably comprise one or more nonionic and/or anionic surfactants. They may also comprise amphoteric or zwitterionic detergent compounds, but this is not normally desired owing to their relatively high cost.
  • Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having a hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids, amides or alkyl phenols with alkylene oxides, especially ethylene oxide either alone or with propylene oxide.
  • Specific nonionic detergent compounds are C 6 -C 22 alkyl phenol-ethylene oxide condensates, generally 5 to 25 EO, i.e. 5 to 25 units of ethylene oxide per molecule, and the condensation products of aliphatic C 8 -C 18 primary or secondary linear or branched alcohols with ethylene oxide, generally 5 to 10 EO.
  • suitable nonionic surfactants are alkyl polyglycosides and polyhydroxy fatty acid amide surfactants such as disclosed in WO-A-92/06154 (Procter & Gamble).
  • Suitable anionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher acyl radicals.
  • suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher C 8 -C 18 alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl C 9 -C 20 benzene sulphonates, particularly sodium linear secondary alkyl C 10 -C 15 benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
  • the preferred anionic detergent compounds are sodium C 12 -C 18 alkyl sulphates owing to their favourable compatibility with lipolytic enzymes.
  • Surface active agents may preferably be present in amounts of from 0.1% by weight of the composition, more preferably 0.5% by weight and preferably up to 70% by weight, more preferably up to 60% by weight of the composition.
  • the level of surface active agents is preferably from 5% by weight, more preferably from 10% by weight and preferably up to 60 % by weight, more preferably up to 40 % by weight, most preferably up to 35% by weight.
  • the level of surface active agents is preferably from 0.5% by weight to amounts to about 60% by weight depending upon their type and properties.
  • Preferably low-to non-foaming nonionic surfactant are used in properly built or highly built compositions in amounts to 7% by weight. Higher levels of highly detersive surfactants, i.e. up to 70% by weight, preferably 60% by weight, may be used in lower builder containing active/enzyme-based compositions.
  • the concentration of surface active agents in the wash liquor is from 0.001 to 20 g/l, preferably from 0.05 to 10 g/l, most preferably up to 5 g/l.
  • the enzymatic detergent composition used in the present invention may further contain from 5 to 60%, preferably from 20 to 50% by weight of a detergency builder.
  • This detergency builder may be any material capable of reducing the level of free calcium ions in the wash liquor and will preferably provide the composition with other beneficial properties such as an alkaline pH, the suspension of soil removed from the fabric and the suspension of the fabric-softening clay material.
  • detergency builders include precipitating builders such as the alkali metal carbonates, bicarbonates, orthophosphates, sequestering builders such as the alkali metal tripolyphosphates or nitrilotriacetates, or ion exchange builders such as the amorphous alkali metal aluminosilicates or the zeolites.
  • the characteristic feature of the process of the present invention is that an enzyme having lipolytic activity is used in the ultrasonic cleaning process.
  • any enzyme having sufficient lipolytic activity may be used in the process.
  • a lipase derived from microorganisms is used, more preferably a bacterial or fungal lipase.
  • the enzyme having lipolytic activity is selected from Thermomyces lipases or variants thereof, cutinases or variants thereof, Pseudomonas lipases or variants thereof, Fusarium lipases or variants thereof and/or Chromobacter lipases or variants thereof.
  • EP-A-214 761 (Novo/Nordisk) gives detailed description of lipases derived from organisms of the species Pseudomonas cepacia, and certain uses therefor.
  • EP-A-258 068 (Novo/Nordisk) gives detailed description of lipases derived from organisms of the genus Thermomyces (previous name Humicola) and certain uses therefor.
  • EP-A-205 208 and EP-A-206 390 (Unilever) which relate to a class of lipases defined on the basis of their immunological relationships, and describe their use in detergent compositions and textile washing.
  • the preferred lipases are those derived from P. fluorescens, P. gladioli and Chromobacter species.
  • EP-A-331 376 (Amano) describes lipases and their production by rDNA technique, and their use, including an amino acid sequence of lipase from Pseudomonas cepacia. Further lipase enzymes produced by rDNA technique are described in for example WO-A-89/09263 (Gist-Brocades) and EP-A-218 272 (Gist-Brocades).
  • WO-A-90/09446 Plant Genetics Systems discloses a cutinase enzyme from Fusarium solani pisi which is capable of hydrolysing triolein. Because there appears to be some confusion with regard to the nomenclature of these enzymes, we define an enzyme having lipolytic activity for the purposes of this patent application as any enzyme capable of hydrolysing mono-, di-, or triglycerides.
  • the present invention also provides a number of combinations of the enzyme having lipolytic activity and further, conventional constituents used in detergent systems, to provide useful advantage in the ultrasonic removal of fatty material and material adsorbed to the fatty material in soil on textile.
  • the other components of such detergent compositions can be of any of many known kinds, for example as described in GB-A-1 372 034 (Unilever), US-A-3 950 277, US-A-4 011 169 and EP-A-179 533 (Procter & Gamble), EP-A-205 208 and EP-A-206 390 (Unilever), JP-A-63-078000 (Lion), and Research Disclosure 29056 of June 1988.
  • the detergent compositions can be formulated as described in EP-A-407 225.
  • the enzyme having lipolytic activity can usefully be added to the detergent composition in the form of a granular composition, a solution or a slurry of lipolytic enzyme with carrier material (e.g. as in EP-A-258 068 and Savinase® and Lipolase® products of Novo/Nordisk).
  • carrier material e.g. as in EP-A-258 068 and Savinase® and Lipolase® products of Novo/Nordisk.
  • the amount of enzyme having lipolytic activity can be chosen within wide limits.
  • the enzymatic aqueous cleaning medium contains 0.1 to 500 LU/ml. It is especially preferred to use about 0.5 to 50 LU/ml.
  • lipase units are defined as they are in EP-A-258 068 (Novo/Nordisk), which is based on hydrolysis of tributyrin in a pH-stat.
  • 1 LU (Lipase Unit) is the amount of enzyme which liberates 1 ⁇ mol titratable butyric acid per minute at 30°C,pH 7.0 with gum arabic as an emulsifier. Similar considerations apply mutatis mutandis in the case of other enzymes, which may also be present.
  • protease is present together with the enzyme having lipolytic activity, by selecting such protease from those having pI lower than 10.
  • the protease is present in the enzymatic aqueous cleaning medium in an amount of from 0.1 to 500 GU/I.
  • a GU is a Glycerine 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.
  • EP-A-271 154 Unilever describes a number of such proteases.
  • Proteases for use together with lipolytic enzyme may include subtilisin of for example BPN' type or of some of the other types of subtilisin disclosed in the literature, some of which have already been proposed for detergents use, e.g. mutant proteases as described in for example EP-A-130 756 (Genentech), US-A-4 760 025 (Genencor), EP-A-214 435 (Henkel), WO-A-87/04661 (Amgen), WO-A-87/05050 (Genex), Thomas et al. (1986) in Nature 5, 316, and 375-376 and in J.Mol.Biol. (1987) 193, 803-813, Russel et al.
  • WO-A-92/08779 discloses liquid detergent compositions comprising a lipase and a modified bacterial serine protease, which is said to be more compatible with the lipase.
  • the proteases are modified in that the methionine adjacent to the active-site serine has been replaced by another amino acid.
  • the cleaning process of the present invention is not only suitable for cleaning fabrics, but the principle of the invention can also be applied in the cleaning of other soiled objects such as dishes and/or other table ware, or medical equipment.
  • the wash liquor contained 3 g/l of a detergent product having the following composition (in % by weight): Dodecyl Benzene Sulphonate 11.2 Ethoxylated alcohol nonionic surfactant 7 EO 4.6 Soap (pristerine 4950) 1.0 Sodium tripolyphosphate 39.5 Sodium carbonate 3.9 Sodium silicate 7.3 Sodium carboxymethyl cellulose 0.6 Fluorescer 0.2 Sodium sulphate 31.7 Water rest
  • the reflectance at 460 nm was used to monitor the cleaning action.
  • the results are shown in the Table. It is clear that the lipase effect, which is the difference between the reflectance at 460 nm after the ultrasonic wash in the presence and in the absence of lipase, increases with the lipase concentration.
  • Example 1 was repeated using the following detergent product at 2.6 g/l: Dodecyl Benzene Sulphonate 8.0 Ethoxylated alcohol nonionic surfactant 12 EO 1.8 Ethoxylated alcohol nonionic surfactant 6 EO 0.7 Ethoxylated alcohol nonionic surfactant 7 EO 2.2 Alf5 0.8 Zeolite 42.0 Acrylic/Maleic copolymer (CP5 ex BASF) 4.0 Sodium silicate 1.0 Calcium Dequest 0.3 Sodium sulphate 18.0 Water and minors 12.6
  • Example 1 was repeated using the following detergent product at 2 g/l: Dodecyl Benzene Sulphonic acid 16.0 C 12 -C 15 Ethoxylated alcohol nonionic surfactant 7 EO 7.0 Monoethanol amine 2.0 Citric acid 6.5 Sodium xylene sulphonate 6.0 Sodium hydroxide 4.1 protease 0.5 Minors and water to 100%
  • Example 1 was repeated using the following detergent product at 3 g/l: C 12 -C 15 Ethoxylated alcohol nonionic surfactant 10.5-13 EO 9.0 Sodium sulphate 36.8 Sodium carbonate 38.5 Sodium silicate 7.0 Diatomeous Earth 1.9 Sodium carboxymethyl cellulose 0.1 Fluorescer 0.1 Water and minors to 100%
  • the pH of the wash liquor was adjusted to 9.2 using a HCl solution, and further the liquor had 5 FH.
  • a US bath was used at 33 kHZ, 80 Watt, at 30°C for 30 minutes.
  • the level of H 3 labelled glycerol in the wash liquor was determined and the detergency % (i.e.
  • wash liquor comprising an enzyme having lipolytic activity. It is believed that the wash results will be even better when surface active agents are present, e.g. as regards antiredeposition.

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  • 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)
  • Cleaning By Liquid Or Steam (AREA)

Claims (9)

  1. Verfahren zum Reinigen von Gegenständen, bei dem verschmutzte Gegenstände in ein enzymatisches wässeriges Reinigungsmedium getaucht werden und mit Ultraschallenergie beschallt werden, wobei das Reinigungsmedium ein Enzym umfaßt, das Mono-, Di- oder Triglycerid hydrolysieren kann, dadurch gekennzeichnet, daß das Enzym eine Aktivität von 0,1 bis 500 LU/ml aufweist und das Reinigungsmedium weiterhin Tenside umfaßt.
  2. Verfahren nach Anspruch 1, wobei die verschmutzten Gegenstände aus Textilien, Geschirr allgemein und Haushaltsgeschirr ausgewählt sind.
  3. Verfahren nach Ansprüchen 1-2, wobei das lipolytische Aktivität aufweisende Enzym von Thermomyces, Pseudomonas, Fusarium und/oder Chromobacter oder eine Cutinase abgeleitet ist.
  4. Verfahren nach einem der vorangehenden Ansprüche, wobei das enzymatische wässerige Reinigungsmedium 0,5 bis 50 LU/ml enthält.
  5. Verfahren nach einem der vorangehenden Ansprüche, wobei das enzymatische wässerige Reinigungsmedium 0,05 bis 50 g/l, vorzugsweise 0,1 bis 5 g/l eines Waschmittels umfaßt.
  6. Verfahren nach einem der vorangehenden Ansprüche, wobei das enzymatische wässerige Reinigungsmedium 0,001 bis 20 g/l Tenside umfaßt.
  7. Verfahren nach einem der vorangehenden Ansprüche, wobei das enzymatische wässerige Reinigungsmedium weiterhin 0,1 bis 500 GU/l eines proteolytischen Enzyms umfaßt.
  8. Verfahren nach einem der vorangehenden Ansprüche, einschließlich des Schritts Entlüften des wässerigen Reinigungsmediums.
  9. Verfahren nach einem der vorangehenden Ansprüche, wobei die Ultraschallenergie 15 Minuten oder weniger auf das Reinigungsmedium angewendet wird.
EP93920792A 1992-09-25 1993-09-20 Reinigungsverfahren Expired - Lifetime EP0662121B1 (de)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP93920792A EP0662121B1 (de) 1992-09-25 1993-09-20 Reinigungsverfahren

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
EP92202964 1992-09-25
EP92202964 1992-09-25
EP93920792A EP0662121B1 (de) 1992-09-25 1993-09-20 Reinigungsverfahren
PCT/EP1993/002559 WO1994007989A1 (en) 1992-09-25 1993-09-20 Cleaning process

Publications (2)

Publication Number Publication Date
EP0662121A1 EP0662121A1 (de) 1995-07-12
EP0662121B1 true EP0662121B1 (de) 1997-05-07

Family

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Family Applications (1)

Application Number Title Priority Date Filing Date
EP93920792A Expired - Lifetime EP0662121B1 (de) 1992-09-25 1993-09-20 Reinigungsverfahren

Country Status (7)

Country Link
EP (1) EP0662121B1 (de)
JP (1) JPH08502087A (de)
AU (1) AU4818493A (de)
CA (1) CA2144063C (de)
DE (1) DE69310526T2 (de)
ES (1) ES2102677T3 (de)
WO (1) WO1994007989A1 (de)

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP3119809B2 (ja) * 1996-01-26 2000-12-25 住友電気工業株式会社 タイヤ空気圧低下検出方法および装置
DE19618725A1 (de) * 1996-05-09 1997-11-13 Weigert Chem Fab Verfahren und Kit zum Reinigen von Geschirr
KR100430166B1 (ko) 1998-11-16 2004-05-03 더 프록터 앤드 갬블 캄파니 음파 또는 초음파를 사용하는 세정 제품
BR9915733A (pt) * 1998-11-16 2001-10-02 Procter & Gamble Composições de limpeza ultra-sÈnica

Family Cites Families (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE3750450T2 (de) * 1986-08-29 1995-01-05 Novo Industri As Enzymhaltiger Reinigungsmittelzusatz.
EP0258816A2 (de) * 1986-09-04 1988-03-09 Henkel Kommanditgesellschaft auf Aktien Verbessertes Verfahren zum Waschen und Reinigen von Textilen
ATE113070T1 (de) * 1987-05-29 1994-11-15 Genencor Int Cutinase haltige reinigungsmittelzusammensetzungen.
JP2573854B2 (ja) * 1987-12-12 1997-01-22 日興バイオ技研株式会社 超精密装置の超精密洗浄方法
DE69033423T2 (de) * 1989-05-15 2000-05-25 Clorox Co Wäschewaschverfahren
GB8915658D0 (en) * 1989-07-07 1989-08-23 Unilever Plc Enzymes,their production and use

Also Published As

Publication number Publication date
ES2102677T3 (es) 1997-08-01
AU4818493A (en) 1994-04-26
EP0662121A1 (de) 1995-07-12
JPH08502087A (ja) 1996-03-05
DE69310526T2 (de) 1997-09-11
CA2144063C (en) 2003-12-09
DE69310526D1 (de) 1997-06-12
CA2144063A1 (en) 1994-04-14
WO1994007989A1 (en) 1994-04-14

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