EP2640818B1 - Préparation liquide d'agents tensioactifs stabilisée et contenant des enzymes - Google Patents

Préparation liquide d'agents tensioactifs stabilisée et contenant des enzymes Download PDF

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Publication number
EP2640818B1
EP2640818B1 EP11779166.5A EP11779166A EP2640818B1 EP 2640818 B1 EP2640818 B1 EP 2640818B1 EP 11779166 A EP11779166 A EP 11779166A EP 2640818 B1 EP2640818 B1 EP 2640818B1
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Prior art keywords
acid
surfactant
enzyme
lipase
surfactant preparation
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EP2640818A1 (fr
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Timothy O'connell
Susanne Tondera
Thomas Weber
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Henkel AG and Co KGaA
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Henkel AG and Co KGaA
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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
    • C11D3/38663—Stabilised liquid enzyme compositions

Definitions

  • the invention is in the field of liquid enzyme-containing surfactant preparations, as used for example in washing, cleaning or disinfecting.
  • the invention relates to uses of enzyme stabilizers.
  • boric acid and boric acid derivatives occupy an outstanding position among enzyme stabilizers which are effective in surfactant preparations even in comparatively low concentrations.
  • boric acids or borates have the disadvantage that they form unwanted by-products with other ingredients of a surfactant preparation, in particular detergents, cleaners or disinfectant ingredients, so that they are no longer available for the desired cleaning purpose or even as such in the respective compositions Contain contamination, for example on the laundry.
  • boric acids and borates are increasingly regarded as environmentally disadvantageous.
  • boronic acid derivatives are proposed as enzyme stabilizers in the prior art.
  • the international patent application discloses WO 96/21716 A1 in that boron or boronic acid derivatives acting as protease inhibitors are suitable for stabilizing enzymes in liquid preparations, including detergents and cleaners.
  • a selection of boronic acid derivatives, including 4-formyl-phenyl-boronic acid, as stabilizers is further disclosed in the international patent application WO 96/41859 A1 , Such compounds are further disclosed in the international patent application WO 2006/045310 used for enzyme stabilization, but in solid detergent bars.
  • the present invention has for its object to provide a liquid surfactant preparation with stabilized hydrolytic enzymes.
  • the surfactant formulation should contain less boric acid than the enzyme stabilizer.
  • the invention relates to the use of a component which boric acid, propylene glycol and a phenylboronic acid derivative having the structural formula in which R is hydrogen, a hydroxyl, a C 1 -C 6 alkyl, a substituted C 1 -C 6 alkyl, a C 1 -C 6 alkenyl or a substituted C 1 -C 6 alkenyl group, in for the stabilization of a hydrolytic enzyme in a liquid surfactant composition containing at least one surfactant.
  • such a combination of boric acid, propylene glycol and a corresponding phenylboronic acid derivative advantageously keeps a hydrolytic enzyme, in particular a lipase or a protease and especially a lipase, in a liquid surfactant preparation stable, for example in a liquid washing and cleaning - or disinfectant.
  • the combination of these compounds therefore makes it possible, in preferred surfactant formulations, to be able to use the stabilizers overall at a lower concentration in order to bring about sufficient enzyme stabilization.
  • these compounds have good water solubility. Therefore, they can be easily incorporated in liquid surfactant preparations, in particular in liquid detergents, cleaners or disinfectants, or in a washing or cleaning liquor formed by such a surfactant preparation, or simply used in these. Furthermore, in preferred embodiments according to the invention, precipitation during storage is reduced or completely avoided.
  • the interaction of boric acid, propylene glycol and a corresponding phenylboronic acid derivative results in a synergistic enzyme stabilization. Among them is an improved enzyme stabilization by the combination of the compounds in comparison understood with the enzyme stabilization by one of these compounds alone and also in comparison with the sum of the individual performances of the compounds in terms of enzyme stabilization.
  • a use according to the invention is characterized in that the radical R in the phenylboronic acid derivative is a C 1 -C 6 -alkyl group and further preferred CH 3 , CH 3 CH 2 or CH 3 CH 2 CH 2 .
  • a use according to the invention is characterized in that the radical R in the phenylboronic acid derivative is hydrogen.
  • the use according to the invention is characterized in that the phenylboronic acid derivative is 4-formyl-phenylboronic acid (4-FPBA). It is given in the formula below:
  • Phenylboronic acid derivatives used according to the invention may furthermore have further chemical modifications on the phenyl ring, in particular they may contain one or more methyl, amino, nitro, chloro, fluoro, bromo, hydroxyl, formyl, ethyl, acetyl, t-butyl, anisyl, benzyl, trifluoroacetyl, N-hydroxysuccinimide, t-butyloxycarbonyl, benzoyl, 4-methylbenzyl, thioanizyl, thiocresyl, benzyloxymethyl, 4-nitrophenyl, benzyloxycarbonyl, 2 Nitrobenzoyl, 2-nitrophenylsulphenyl, 4-toluenesulphonyl, pentafluorophenyl, diphenylmethyl, 2-chlorobenzyloxycarbonyl, 2,4,5-trichlorophenyl, 2-bromobenzyloxycarbonyl, 9-
  • All compounds provided in the context of the present invention as part of the hydrolytic enzyme stabilizing component may be present in all protonated or deprotonated forms in the surfactant preparation. Furthermore, all such compounds, in particular their deprotonated forms, may be associated with cations.
  • Preferred cations in this regard are monovalent or polyvalent, in particular divalent, cations, in particular Na ions (Na + ), K ions (K + ), Li ions (Li + ), Ca ions (Ca 2+ ), Mg ions (Mg 2+ ), Mn ions (Mn 2+ ) and Zn ions (Zn 2+ ). Particularly preferred are Na ions (Na + ).
  • the hydrolytic enzyme stabilizing component may consist exclusively of said compounds so that the hydrolytic enzyme stabilizing component is the combination of boric acid, propylene glycol and corresponding phenylboronic acid derivative.
  • the hydrolytic enzyme stabilizing component may comprise further compounds such that the combination of boric acid, propylene glycol and corresponding phenylboronic acid derivative is part of the hydrolytic enzyme stabilizing component.
  • the boric acid is contained in an amount of 0.09 to 3.5, and preferably from 0.1 to 2.49 wt .-%.
  • Propylene glycol is used in a surfactant preparation according to the invention in an amount of 0.000001 to 10 wt .-% and increasingly preferably from 0.01 to 9.5 wt .-%, from 1 to 9 wt .-%, from 1.5 to 8.5% by weight and from 2 to 8% by weight.
  • the phenylboronic acid derivative is present in a surfactant preparation used in the invention in an amount of from 0.001 to 0.08 weight percent, and more preferably from 0.003 to 0.06 weight percent, from 0.005 to 0.05 weight percent, from 0.007 to 0.03 wt .-% and from 0.009 to 0.01 wt .-%.
  • a hydrolytic enzyme is a hydrolase (EC 3.XXX) and thus an enzyme that hydrolytically cleaves esters, ethers, peptides, glycosides, acid anhydrides or CC bonds in a reversible reaction.
  • the hydrolytic enzyme therefore catalyzes the hydrolytic cleavage of substances according to AB + H 2 O ⁇ AH + B-OH.
  • Hydrolases constitute the third major class of EC classification of enzymes.
  • the EC numbers (“Enzyme Commission numbers”) form a numerical classification system for enzymes. Each EC number consists of four numbers separated by periods, with the first digit designating one of the six main enzyme classes and hydrolases corresponding to EC 3.XXX corresponding to the third major class. Their representatives are proteases, peptidases, nucleases, phosphatases, glycosidases and esterases.
  • the hydrolytic enzyme is preferably contained in the liquid surfactant preparation in an amount of 1 x 10 -8 to 5% by weight, based on active protein.
  • the hydrolytic enzyme is from 0.001 to 5% by weight, more preferably from 0.01 to 5% by weight, still more preferably from 0.05 to 4% by weight and most preferably from 0.075 to 3.5% by weight .-% in the liquid surfactant preparation.
  • the hydrolytic enzyme may be further covalently or non-covalently bound to a carrier and / or embedded in encapsulating substances, for example to additionally protect it against premature inactivation.
  • the protein concentration in the surfactant preparation can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ).
  • BCA method bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid
  • the biuret method Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 .
  • a surfactant preparation used according to the invention is characterized in that the hydrolytic enzyme is a protease, amylase, cellulase, glycosidase, hemicellulase, mannanase, xylanase, xyloglucanase, xanthanase, pectinase, ⁇ -glucosidase, carrageenase or a lipase or a mixture containing at least two of these enzymes. More preferably, the hydrolytic enzyme is a lipase or a protease.
  • the hydrolytic enzyme is more preferably a serine protease, more preferably a subtilase, and most preferably a subtilisin. Most preferably, the hydrolytic enzyme is a lipase. It has been found that lipases are stabilized particularly well by the hydrolytic enzyme-stabilizing component in a surfactant preparation used according to the invention. For in particular for detergents, cleaners or disinfectants, the storage stability of the enzymes and in particular also of lipases is a general problem. The same applies to the proteases mentioned. Proteases are also stabilized particularly well by the component stabilizing the hydrolytic enzyme in a surfactant preparation used according to the invention.
  • proteases are the subtilisins BPN 'from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY and the subtilases, but no longer the subtilisins in the strict sense attributable enzymes Thermitase, proteinase K and the proteases TW3 and TW7.
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from the company Novozymes A / S, Bagsvaerd, Denmark.
  • subtilisins 147 and 309 are sold under the trade names Esperase®, and Savinase® by the company Novozymes. From the protease from Bacillus lentus DSM 5483 derived under the name BLAP® protease variants derived.
  • proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® from the company Novozymes, which are sold under the trade names, Purafect®, Purafect® OxP, Purafect® Prime, Excellase® and Properase® from Danisco / Genencor, sold under the tradename Protosol® by Advanced Biochemicals Ltd., Thane, India, under the tradename Wuxi® by Wuxi Snyder Bioproducts Ltd.
  • proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications WO 08/086916 and WO 07/131656 , Further advantageous proteases are disclosed in the patent applications WO 91/02792 . WO 08/007319 . WO 93/18140 . WO 01/44452 . GB 1243784 . WO 96/34946 .
  • WO 02/029024 and WO 03/057246 Other useful proteases are those that are found in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus sphaericus are naturally present.
  • amylases are the ⁇ -amylases from Bacillus licheniformis, from Bacillus amyloliquefaciens or from Bacillus stearothermophilus and, in particular, also their improved developments for use in detergents or cleaners.
  • the enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl® and from the company Danisco / Genencor under the name Purastar®ST.
  • this ⁇ -amylase is available from the company Novozymes under the trade name Duramyl® and Termamyl®ultra, from the company Danisco / Genencor under the name Purastar®OxAm and from the company Daiwa Seiko Inc., Tokyo, Japan, as Keistase®.
  • the Bacillus amyloliquefaciens ⁇ -amylase is sold by the company Novozymes under the name BAN®, and variants derived from the Bacillus stearothermophilus ⁇ -amylase under the names BSG® and Novamyl®, also from the company Novozymes. Furthermore, for this purpose, the ⁇ -amylase from Bacillus sp.
  • a 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948).
  • CCTase cyclodextrin glucanotransferase
  • DSM 9948 Bacillus agaradherens
  • WO 03/054177 and WO07 / 079938 are disclosed.
  • fusion products of all the molecules mentioned can be used.
  • the further developments of the ⁇ -amylase from Aspergillus niger and A. oryzae available under the trade name Fungamyl® from the company Novozymes are suitable.
  • amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus® are, for example, the amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus®, the latter also from the company Novozymes.
  • variants of these enzymes obtainable by point mutations can be used according to the invention.
  • cellulases examples include doglucanases, EG
  • EG fungal, endoglucanase
  • EG fungal, endoglucanase
  • Novozymes examples of cellulases
  • Endolase® and Carezyme® are based on the 50 kD EG or 43 kD EG from Humicola insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®.
  • cellulases available from the company AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®, which are based, at least in part, on the 20 kD-EG of melanocarpus.
  • Other cellulases from AB Enzymes are Econase® and Ecopulp®.
  • Other suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, those derived from Bacillus sp. CBS 670.93 is available from the company Danisco / Genencor under the trade name Puradax®.
  • Other usable Commercial products of the company Danisco / Genencor are "Genencor detergent cellulase L" and lndiAge®Neutra.
  • hydrolytic enzymes are those which are grouped under the term glycosidases (E.C. 3.2.1.X). These include, in particular, arabinases, fucosidases, galactosidases, galactanases, arabico-galactan galactosidases, mannanases (also referred to as mannosidases or mannases), glucuronosidases, agarase, carrageenases, pullulanases, ⁇ -glucosidases, xyloglucanases (xylanases), xanthanases and pectin-degrading enzymes (pectinases).
  • Preferred glycosidases are also summarized by the term hemicellulases.
  • Hemicellulases include, in particular, mannanases, xyloglucanases (xylanases), ⁇ -glucosidases and carrageenases, and also pectinases, pullulanases and ⁇ -glucanases.
  • Pectinases are pectin-degrading enzymes, wherein the hydrolytic pectin degrading enzymes belong in particular to the enzyme classes EC 3.1.1.11, EC 3.2.1.15, EC 3.2.1.67 and EC 3.2.1.82.
  • pectinases in the context of the present invention are also counted enzymes with the designations pectate lyase, pectin esterase, pectin methoxylase, pectin methoxylase, pectin methyl esterase, pectase, pectin methyl esterase, pectin esterase, pectin-pectin hydrolase, pectin-polymerase, endopolygalacturonase, pectolase, pectin hydrolase, pectin-polygalacturonase, endo-polygalacturonase, poly - ⁇ -1,4-galacturonide glycanohydrolase, endogalacturonase, endo-D-galacturonase, galacturan 1,4- ⁇ -galacturonidase, exopolygalacturonase, poly (galacturonate) hydrolase, exo-D-galacturona
  • enzymes suitable for this purpose are, for example, under the name Gamanase®, Pektinex AR® or Pectaway® from the company Novozymes, under the name Rohapec® B1L from the company AB Enzymes and under the name Pyrolase® from Diversa Corp., San Diego , CA, USA available.
  • the ⁇ -glucanase obtained from Bacillus subtilis is available under the name Cereflo® from the company Novozymes.
  • Particularly preferred glycosidases or hemicellulases according to the invention are mannanases which are sold, for example, under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Danisco / Genencor.
  • lipases or cutinases are the lipases originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or developed therefrom, in particular those with the amino acid exchange D96L. They are sold, for example, by the company Novozymes under the trade names Lipolase®, Lipolase®Ultra, LipoPrime®, Lipozyme® and Lipex®. Another advantageous lipase is available under the trade name Lipoclean® from the company Novozymes.
  • the cutinases can be used, originally from Fusarium solani pisi and Humicola insolens have been isolated.
  • lipases are from the company Amano under the names Lipase CE®, Lipase P®, Lipase B®, and Lipase CES®, lipase AKG®, Bacillis sp. Lipase®, Lipase AP®, Lipase M-AP® and Lipase AML®. From the company Danisco / Genencor, for example, the lipases or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii.
  • Lipase® and Lipomax® are prepared by Gist-Brocades (now Danisco / Genencor), and Lipase MY-30®, Lipase OF®, by Meito Sangyo KK of Japan and Lipase PL® distributed enzymes, further the product Lumafast® from the company Danisco / Genencor.
  • the enzymes to be used in the context of the present invention can be derived, for example, originally from microorganisms, such as the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or produced by suitable biotechnological methods by suitable microorganisms, for example by transgenic expression hosts, for example the genera Escherichia, Bacillus, or by filamentous fungi. It is emphasized that they may in particular also be technical enzyme preparations of the respective enzyme, i. Accompanying substances may be present. Therefore, the enzymes can be formulated and used together with accompanying substances, for example from the fermentation or with other stabilizers.
  • An enzyme stabilization according to the invention is when the presence of the hydrolytic enzyme stabilizing component causes a surfactant preparation comprising hydrolytic enzyme and hydrolytic enzyme stabilizing component (surfactant preparation according to the invention) after storage has a higher enzymatic activity of the hydrolytic enzyme compared to a Control preparation which differs from the surfactant preparation according to the invention only by the absence of the hydrolytic enzyme stabilizing component (control).
  • the boric acid is in an amount of 0.1 to 2.49 wt%
  • the propylene glycol in an amount of 2 to 8 wt%
  • the phenylboronic acid derivative in an amount of 0.009 to 0 , 01 wt .-% included.
  • the surfactant preparation according to the invention therefore has a higher residual activity of the hydrolytic enzyme compared to the control, wherein the preparation used according to the invention and the control have the same initial enzymatic activity at the start of storage, both preparations are treated in the same manner, in particular concerning the conditions storage and determination of enzyme activity.
  • storage is for at least 1 week, 2 weeks, 3 weeks, 4 weeks, and most preferably for 7 weeks. More preferably, the storage is carried out at a temperature of 20 ° C, 25 ° C or 30 ° C.
  • the enzyme activity can in this regard - matched to the respective type of enzyme - done in the usual way. Methods for determining activity are familiar to the expert in the field of enzyme technology and are routinely used by him. Methods for determining the protease activity are disclosed, for example, in Surfactants, Vol. 7 (1970), pp. 125-132 .
  • the proteolytic activity can be further determined by the release of the chromophore para-nitroaniline (pNA) from the substrate suc-L-Ala-L-Ala-L-Pro-L-Phe-p-nitroanilide (suc-AAPF-pNA). The protease cleaves the substrate and releases pNA.
  • pNA chromophore para-nitroaniline
  • the release of pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of enzymatic activity (see Del Mar et al., 1979).
  • the measurement is carried out at a temperature of 25 ° C, at pH 8.6 and a wavelength of 410 nm.
  • the measuring time is 5 min. at a measuring interval of 20s to 60s.
  • the protease activity is preferably indicated in PE (protease units).
  • the lipase activity is determined in the usual way, preferably as described in US Pat Michael C. Schotz and Arlene S. Garfinkel, "A simple lipase assay using trichloroacetic acid” (Journal of Lipid Research, Vol. 13, pp. 824-826, November 1972 ).
  • the activity determination described here is based on that enzyme samples are incubated with a serum-activated solution, the radioactively labeled glycerol trioleate ([2- 3 H] glycerol trioleate) as the substrate for the lipase (See p. 824, last paragraph of the left column, and Page 825, first paragraph of the left column in the above publication).
  • TCA trichloroacetic acid
  • the radioactivity in the supernatant is determined, whereby the activity of the enzyme is determined by means of a standard curve.
  • the presence of enzyme stabilization is determined using a lipase-containing liquid surfactant formulation which is stored for 7 weeks at a temperature of 30 ° C and whose residual lipolytic activity is determined as described above. Most preferably, the presence of enzyme stabilization is determined as described in the example.
  • a surfactant preparation is to be understood as meaning any type of composition which comprises at least one surfactant.
  • a composition contains a surfactant as described below.
  • liquid or flowable administration forms can serve as liquid surfactant preparations.
  • Flowable in the context of the present application are preparations which are pourable and can have viscosities of up to several tens of thousands of mPas. The viscosity can be measured by conventional standard methods (for example, Brookfield LVT-II at 20 rpm and 20 ° C., spindle 3) and is preferably in the range from 5 to 10000 mPas. Preferred agents have viscosities of 10 to 8000 mPas, with values between 120 to 3000 mPas being particularly preferred.
  • a liquid surfactant preparation in the context of the present invention can therefore also be gelatinous or paste-like, it can be in the form of a homogeneous solution or suspension, and can be sprayed or packaged in other conventional dosage forms, for example.
  • a liquid surfactant preparation used according to the invention can be used as such or after dilution with water, in particular for the cleaning of textiles and / or hard surfaces.
  • Such dilution can be readily made by diluting a measured amount of the surfactant preparation in a further amount of water in certain weight ratios of surfactant preparation: water and optionally shaking this dilution to ensure uniform distribution of the surfactant formulation in the water.
  • Possible weight or volume ratios of the dilutions are from 1: 0 surfactant preparation: water to 1: 10,000 or 1: 20000 surfactant preparation: water, preferably from 1:10 to 1: 2000 surfactant preparation: water.
  • a surfactant preparation in the sense of the present invention can therefore also be the washing or cleaning liquor itself.
  • the washing or cleaning liquor is understood to mean the use solution containing the washing or cleaning agent which acts on textiles or fabrics (wash liquor) or hard surfaces (cleaning liquor) and thus comes into contact with the soiling present on textiles or fabrics or hard surfaces ,
  • the washing or cleaning liquor arises when the washing or cleaning process begins and the washing or cleaning agent is diluted, for example, in a washing machine or other suitable container with water.
  • the surfactant preparation is a washing, cleaning or disinfecting agent.
  • the detergents include all conceivable types of detergents, in particular detergents for textiles, carpets or natural fibers. They can be provided for manual and / or machine application.
  • the detergents also include washing aids, which are added to the actual detergent in the manual or machine textile washing, in order to achieve a further effect.
  • Detergents include all agents for cleaning and / or disinfecting hard surfaces also found in all of the above dosage forms, manual and automatic dishwashing detergents, carpet cleaners, abrasives, glass cleaners, toilet scavengers, etc.
  • Textile pre- and post-treatment are finally on the one hand such means with which the garment is brought into contact before the actual laundry, for example, for solving stubborn dirt, on the other hand, those in one of the actual textile laundry downstream step the laundry further desirable Give properties such as a comfortable grip, crease resistance or low static charge.
  • the fabric softeners are among the latter expected.
  • Disinfectants are, for example, hand disinfectants, surface disinfectants and instrument disinfectants, which may also occur in the mentioned dosage forms.
  • a disinfectant preferably causes a germ reduction by a factor of at least 10 4 , that is to say that of originally 10,000 proliferating germs (so-called colony-forming units - CFU) survived no more than a single, with viruses in this regard are not considered as germs, since they have no cytoplasm and have no own metabolism.
  • Preferred disinfectants cause a germ reduction by a factor of at least 10 5 .
  • surfactant (s) it is possible to use anionic, nonionic, zwitterionic and / or amphoteric surfactants. From an application point of view, preference is given to mixtures of anionic and nonionic surfactants.
  • the total surfactant content of the liquid surfactant preparation is preferably below 60% by weight, and more preferably below 45% by weight, based on the total liquid surfactant formulation.
  • Suitable nonionic surfactants include alkoxylated fatty alcohols, alkoxylated fatty acid alkyl esters, fatty acid amides, alkoxylated fatty acid amides, polyhydroxy fatty acid amides, alkylphenol polyglycol ethers, amine oxides, alkyl polyglucosides, and mixtures thereof.
  • the nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, in particular primary, alcohols having preferably 8 to 18 carbon atoms and on average 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position or linear and methyl-branched radicals in the mixture can contain, as they are usually present in Oxoalkoholresten.
  • alcohol ethoxylates with linear radicals of alcohols of native origin having 12 to 18 carbon atoms, for example of coconut, palm, tallow or oleyl alcohol, and on average 2 to 8 EO per mole of alcohol are preferred.
  • the preferred ethoxylated alcohols include, for example, C 12-14 alcohols with 3 EO, 4 EO or 7 EO, C 9-11 alcohols with 7 EO, C 13-15 alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C 12-18 -alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C 12-14 -alcohol with 3 EO and C 12-18 -alcohol with 7 EO.
  • the degrees of ethoxylation given represent statistical means which, for a particular product, may be an integer or a fractional number.
  • Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE).
  • fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohol with 14 EO, 25 EO, 30 EO or 40 EO.
  • Nonionic surfactants containing EO and PO groups together in the molecule can also be used according to the invention. Also suitable are also a mixture of a (more) branched ethoxylated fatty alcohol and an unbranched ethoxylated fatty alcohol, such as a mixture of a C 16-18 fatty alcohol with 7 EO and 2-propylheptanol with 7 EO.
  • the Surfactant preparation a C 12-18 fatty alcohol with 7 EO or a C 13-15 -oxo-alcohol with 7 EO as nonionic surfactant.
  • the content of nonionic surfactants is preferably 3 to 40 wt .-%, preferably 5 to 30 wt .-% and in particular 7 to 20 wt .-%, each based on the total surfactant.
  • the surfactant preparation may also contain anionic surfactants.
  • the anionic surfactant used is preferably sulfonates, sulfates, soaps, alkyl phosphates, anionic silicone surfactants and mixtures thereof.
  • the surfactants of the sulfonate type are preferably C 9-13 -alkylbenzenesulfonates, olefinsulfonates, ie mixtures of alkene and hydroxyalkanesulfonates and disulfonates, as are obtained, for example, from C 12-18 -monoolefins having terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acid hydrolysis of the sulfonation products into consideration.
  • esters of ⁇ -sulfo fatty acids for example the ⁇ -sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.
  • Alk (en) ylsulfates are the alkali metal salts and in particular the sodium salts of the sulfuric monoesters of C 12 -C 18 fatty alcohols, for example coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C 10 -C 20 oxo alcohols and those half-esters of secondary alcohols of these chain lengths are preferred.
  • the C 12 -C 16 alkyl sulfates and C 12 -C 15 alkyl sulfates and C 14 -C 15 alkyl sulfates are preferred.
  • 2,3-alkyl sulfates are also suitable anionic surfactants.
  • EO ethylene oxide
  • Fatty alcohols with 1 to 4 EO are suitable.
  • anionic surfactants are soaps.
  • Suitable are saturated and unsaturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, (hydrogenated) erucic acid and behenic acid and, in particular, soap mixtures derived from natural fatty acids, for example coconut, palm kernel, olive oil or tallow fatty acids.
  • the anionic surfactants including the soaps may be in the form of their sodium, potassium or magnesium or ammonium salts.
  • the anionic surfactants are in the form of their sodium salts.
  • Further preferred counterions for the anionic surfactants are also the protonated forms of choline, triethylamine or methylethylamine.
  • the content of a surfactant preparation of anionic surfactants can be from 1 to 40% by weight, preferably from 5 to 30% by weight and very particularly preferably from 10 to 25% by weight, based in each case on the total surfactant preparation.
  • the surfactant preparation is characterized by further comprising at least one other ingredient selected from the group consisting of builder, nonaqueous solvent, acid, water soluble salt, thickener, disinfecting ingredient, and combinations thereof.
  • the improved cleaning performance and / or disinfection is based on a synergistic interaction of at least two ingredients.
  • the hydrolytic enzyme preferably a lipase or a protease, in particular a lipase
  • Such synergy can be achieved with one of the water-soluble salts described below and / or with one of the thickening agents described below and / or with one of the disinfecting ingredients described below.
  • Builders which may be present in the surfactant preparation include, in particular, silicates, aluminum silicates (in particular zeolites), carbonates, salts of organic di- and polycarboxylic acids and mixtures of these substances.
  • Organic builders which may be present in the surfactant preparation are, for example, the polycarboxylic acids which can be used in the form of their sodium salts, polycarboxylic acids meaning those carboxylic acids which carry more than one acid function. These are, for example, citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids, aminocarboxylic acids, nitrilotriacetic acid (NTA), methylglycinediacetic acid (MGDA) and derivatives thereof and mixtures thereof.
  • Preferred salts are the salts of polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, tartaric acid, sugar acids and mixtures thereof.
  • polymeric polycarboxylates are suitable. These are, for example, the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example, those having a molecular weight of 600 to 750,000 g / mol.
  • Suitable polymers are in particular polyacrylates, which preferably have a molecular weight of from 1,000 to 15,000 g / mol. Because of their superior solubility, the short-chain polyacrylates, which have molecular weights of from 1,000 to 10,000 g / mol, and particularly preferably from 1,000 to 5,000 g / mol, may again be preferred from this group.
  • copolymeric polycarboxylates in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid.
  • the polymers may also contain allylsulfonic acids, such as allyloxybenzenesulfonic acid and methallylsulfonic acid, as a monomer.
  • soluble builders such as, for example, citric acid, or acrylic polymers having a molar mass of from 1,000 to 5,000 g / mol, preferably in the liquid surfactant preparation.
  • the molecular weights stated for polymeric polycarboxylates are weight-average molecular weights M w of the particular acid form, which were determined in principle by means of gel permeation chromatography (GPC), a UV detector being used. The measurement was carried out against an external polyacrylic acid standard, which provides realistic molecular weight values due to its structural relationship with the polymers investigated. These data differ significantly from the molecular weight data, in which polystyrene sulfonic acids are used as standard. The molar masses measured against polystyrenesulfonic acids are generally significantly higher than the molecular weights specified in this document.
  • organic builder substances may be present in amounts of up to 40% by weight, in particular up to 25% by weight and preferably from 1% by weight to 8% by weight. Amounts close to the stated upper limit are preferably used in paste-form or liquid, in particular water-containing, surfactant preparations.
  • the surfactant formulations used in the invention are liquid and preferably contain water as the main solvent.
  • non-aqueous solvents may be added to the surfactant preparation. Suitable non-aqueous solvents include mono- or polyhydric alcohols, alkanolamines or glycol ethers, provided that they are miscible with water in the specified concentration range.
  • the solvents are selected from ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, glycerol, diglycol, propyldiglycol, butyldiglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, Propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol monomethyl ether, Dipropylene glycol monoethyl ether, di-isopropylene glycol monomethyl ether, diisopropylene glycol monoethyl ether, methoxytriglycol, ethoxytriglycol
  • the surfactant formulation contain a polyol as a nonaqueous solvent.
  • the polyol may in particular comprise glycerol, 1,2-propanediol, 1,3-propanediol, ethylene glycol, diethylene glycol and / or dipropylene glycol.
  • the surfactant formulation contains a mixture of a polyol and a monohydric alcohol.
  • Non-aqueous solvents may be used in the surfactant preparation in amounts of between 0.5 and 15% by weight, but preferably below 12% by weight.
  • the surfactant formulation to establish a desired, not by the mixture of the remaining components resulting in self-evident pH, the surfactant formulations systemic and environmentally acceptable acids, especially citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and / or adipic acid, but also, mineral acids, in particular sulfuric acid, or bases, in particular ammonium or alkali metal hydroxides.
  • pH regulators are present in the surfactant preparations in amounts of preferably not more than 20% by weight, in particular from 1.2% by weight to 17% by weight.
  • a surfactant preparation according to the invention may further contain one or more water-soluble salts which serve, for example, for adjusting the viscosity.
  • These may be inorganic and / or organic salts.
  • Useful inorganic salts are preferably selected from the group consisting of colorless water-soluble halides, sulfates, sulfites, carbonates, bicarbonates, nitrates, nitrites, phosphates and / or oxides of the alkali metals, alkaline earth metals, aluminum and / or transition metals; Furthermore, ammonium salts can be used.
  • the inorganic salt is selected from the group comprising sodium chloride, potassium chloride, sodium sulfate, potassium sulfate and mixtures thereof.
  • Useful organic salts are, for example, colorless water-soluble alkali metal, alkaline earth metal, ammonium, aluminum and / or transition metal salts of the carboxylic acids.
  • the salts are selected from the group comprising formate, acetate, propionate, citrate, malate, tartrate, succinate, malonate, oxalate, lactate and mixtures thereof.
  • a surfactant preparation used according to the invention may contain one or more thickeners.
  • the thickener is selected from the group comprising xanthan, guar, carrageenan, agar-agar, gellan, pectin, locust bean gum and mixtures thereof. These compounds are effective thickeners even in the presence of inorganic salts.
  • the surfactant preparation contains xanthan as a thickening agent, since xanthan effectively thickened even in the presence of high salt concentrations and a macroscopic separation of the continuous Phase prevented.
  • the thickener stabilizes the continuous, low surfactant phase and prevents macroscopic phase separation.
  • acrylic and methacrylic (co) polymers include, for example, the high molecular weight homopolymers of acrylic acid crosslinked with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol or propylene (INCI name according to "International Dictionary of Cosmetic Ingredients” of "The Cosmetic, Toiletry and Fragrance Association (CTFA) ": carbomer), also referred to as carboxyvinyl polymers.
  • CFA Cosmetic, Toiletry and Fragrance Association
  • Such polyacrylic acids are available, inter alia, under the trade names Polygel® and Carbopol®.
  • acrylic acid copolymers are suitable: (i) copolymers of two or more monomers from the group of acrylic acid, methacrylic acid and their simple, preferably formed with C 1-4 alkanols, esters (INCI acrylates copolymer), for example, among the Trade names Aculyn®, Acusol® or Tego® Polymer are available; (ii) crosslinked high molecular weight acrylic acid copolymers, such as those crosslinked with an allyl ether of sucrose or pentaerythritol copolymers of C 10-30 alkyl acrylates with one or more monomers from the group of acrylic acid, methacrylic acid and their simple, preferably with C 1 4- alkanols, esters (INCI acrylates / C 10-30 alkyl acrylate crosspolymer) and are available, for example, under the trade name Carbopol®.
  • Other suitable polymers are (meth) acrylic acid (co) polymers of the Sokalan® type.
  • the surfactant preparation used according to the invention contains a (meth) acrylic acid (co) polymer in combination with a further thickener, preferably xanthan.
  • the surfactant preparation can contain from 0.05 to 1.5% by weight and preferably from 0.1 to 1% by weight, based in each case on the total surfactant preparation, of thickening agent.
  • the amount of thickener used depends on the type of thickener and the desired degree of thickening.
  • ingredients which have an antimicrobial or antiviral activity are understood to be a disinfectant ingredient.
  • the germicidal effect is dependent on the content of the disinfecting ingredient in the surfactant preparation, wherein the germicidal effect decreases with decreasing content of disinfecting ingredient or increasing dilution of the surfactant preparation.
  • a preferred disinfecting ingredient is ethanol or propanol. These monohydric alcohols are commonly used in disinfectants and detergents because of their solvent properties and their germicidal activity.
  • the term "propanol” encompasses both the 1-propanol (n-propanol) and the 2-propanol ("isopropanol”).
  • Ethanol and / or propanol is, for example, in a total amount of from 10 to 65% by weight, preferably 25 to 55 wt .-% in the surfactant preparation.
  • Another preferred disinfecting ingredient is tea tree oil.
  • the tea tree oil is obtained by steam distillation from the leaves and branch tips of these trees and is a mixture of about 100 substances; its main constituents include (+) - terpinene-4-ol, ⁇ -terpinene, terpinolene, terpineol, pinene, myrcene, phellandrene, p-cymene, limonene and 1,8-cineole.
  • Tea tree oil is contained, for example, in an amount of 0.05 to 10% by weight, preferably 0.1 to 5.0% by weight, in the virucidal treatment solution.
  • Another preferred disinfecting ingredient is lactic acid.
  • the lactic acid or 2-hydroxypropionic acid is a fermentation product produced by various microorganisms. She is weakly active in antibiotics. Lactic acid is contained in the surfactant preparation, for example, in amounts of up to 10% by weight, preferably 0.2 to 5.0% by weight.
  • disinfectant ingredients are, for example, active compounds from the groups of alcohols, aldehydes, antimicrobial acids or their salts, carboxylic esters, acid amides, phenols, phenol derivatives, diphenyls, diphenylalkanes, urea derivatives, oxygen, nitrogen acetals and formals, benzamidines, isothiazoles and derivatives thereof such as isothiazolines and isothiazolinones, phthalimide derivatives, pyridine derivatives, antimicrobial surface active compounds, guanidines, antimicrobial amphoteric compounds, quinolines, 1,2-dibromo-2,4-dicyanobutane, iodo-2-propynyl-butyl-carbamate, iodine, iodophores and peroxides.
  • active compounds from the groups of alcohols, aldehydes, antimicrobial acids or their salts, carboxylic esters, acid amides, phenols,
  • preferred active ingredients are selected from the group comprising 1,3-butanediol, phenoxyethanol, 1,2-propylene glycol, glycerol, undecylenic acid, citric acid, lactic acid, benzoic acid, salicylic acid, thymol, 2-benzyl-4-chlorophenol, 2,2 '.
  • Preferred quaternary surface active compounds contain an ammonium, sulfonium, phosphonium, iodonium or arsonium group. Furthermore, it is also possible to use disinfecting essential oils which at the same time provide scenting of the virucidal treatment solution.
  • particularly preferred active compounds are selected from the group comprising salicylic acid, quaternary surfactants, in particular benzalkonium chloride, peroxo compounds, in particular hydrogen peroxide, alkali metal hypochlorite and mixtures thereof.
  • Such another disinfecting ingredient is, for example, in an amount of 0.01 to 1 wt .-%, preferably 0.02 to 0.8 wt .-%, in particular 0.05 to 0.5 wt .-%, particularly preferably 0 , 1 to 0.3 wt .-%, most preferably 0.2 wt .-% in the surfactant preparation.
  • Liquid surfactant preparations used in the form of conventional solvent-containing solutions are usually prepared by simply mixing the ingredients, which can be added in bulk or as a solution in an automatic mixer.
  • Surfactant formulations used according to the invention may contain only the hydrolytic enzyme as described. Alternatively, they may also contain other hydrolytic enzymes or other enzymes in a concentration useful for the effectiveness of the surfactant formulation.
  • a further subject of the invention thus represent uses of surfactant preparations, which further comprise one or more further enzymes, it being possible in principle to use all enzymes established for this purpose in the prior art.
  • enzymes which can be used as further enzymes are all enzymes which can exhibit catalytic activity in a surfactant preparation according to the invention, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, .beta.-glucosidase, pectinase, carrageenase, perhydrolase, Oxidase, oxidoreductase or a lipase, and mixtures thereof.
  • each further enzyme is from 0.0001 to 1% and more preferably from 0.0005 to 0.5%, from 0.001 to 0.1% and particularly preferably from 0.001 to 0.06% by weight, contained in surfactant preparations according to the invention, based on active protein.
  • the enzymes show synergistic cleaning performance against certain stains or stains, ie the enzymes contained in the surfactant preparation support each other in their cleaning performance.
  • the hydrolytic enzyme stabilizing component may further comprise at least one further enzyme stabilizer.
  • the compounds which are provided as part of the component stabilizing the hydrolytic enzyme ie boric acid, propylene glycol or a corresponding phenylboronic acid derivative, can be replaced by a further enzyme stabilizer.
  • such a further enzyme stabilizer is or comprises a polyol, in particular glycerol or 1,2-ethylene glycol, a sugar or sugar alcohol, a boric acid derivative, in particular aromatic boric acid esters, as described, for example, in the international patent applications WO 92/119709 and WO 92/19708 discloses an antioxidant, glyceric acid, calcium ions or calcium compounds, lactate or a Lactate derivative, sulfonylurea, imidazolium salt, 3,4-dichloroisocoumarin, 4- (2-aminoethyl) benzenesulfonyl fluoride hydrochloride, 4-amidinophenylmethanesulfonyl fluoride hydrochloride, antipaindihydrochloride, benzamidine hydrochloride, exhaled aspartate, trifluoroacetate, leupeptin, chymostatin or a peptide of formula B2-B1 -B0-R, where R is
  • hydrolytic enzyme stabilizing component and the further enzyme stabilizer preferably results in a synergistic enzyme stabilization.
  • the further enzyme stabilizer is preferably in a concentration of 0.000001 to 10 wt .-% and increasingly preferably from 0.00001 to 5.5 wt .-%, from 0.000035 to 4.5 wt .-%, of 0, 00007 to 3.5 wt .-% and from 0.0001 to 2.5 wt .-% in the surfactant preparation.
  • these components provide beneficial stabilization of the hydrolytic enzyme in a liquid surfactant formulation.
  • the phenylboronic acid derivative is 4-formyl-phenyl-boronic acid (4-FPBA).
  • the hydrolytic enzyme is a lipase or a protease, in particular a lipase.
  • a method in which the components described herein for stabilizing a hydrolytic enzyme in a liquid surfactant preparation are used in a temperature range between 10 ° C and 60 ° C, in particular between 10 ° C and 50 ° C, between 10 ° C and 40 ° C, between 10 ° C and 30 ° C, and more preferably between 15 ° C and 30 ° C.
  • Thermostable hydrolytic enzymes could be used even at temperatures even higher than 60 ° C such as 70 ° C or 75 ° C.
  • a surfactant formulation based on a toilet detergent advantageously has an acidic pH, for example, a pH between pH 2 and pH 5.
  • a surfactant preparation which is based on a laundry detergent or other hard surface cleaning agent advantageously has a slightly acidic, neutral or alkaline pH, for example a pH between pH6 and pH11 or between pH7 and pH10.
  • a surfactant formulation based on a hand dishwashing detergent has a pH between pH 6.5 and pH 8. Consequently, it is advantageous to carry out a corresponding process even at these respective pH values.
  • the detergent base formulation used was a propylene glycol-containing liquid detergent of the following composition (all figures in percentages by weight): 0.3-0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0, 3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut fatty acids, 0.5 % HEDP (1-hydroxyethane- (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinylpyrrolidone), 4-8% propylene glycol, 0-0.05% optical brightener, 0-0.001% dye, Rest demineralized water.
  • composition 0.3-0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0, 3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic
  • the storage was carried out for different lengths of time as indicated in Table 1 in airtight containers at 30 ° C. After storage, the respective residual lipolytic activity was determined as described in Michael C. Schotz and Arlene S. Garfinkel, "A simple lipase assay using trichloroacetic acid" (Journal of Lipid Research, Vol. 13, pp. 824-826, November 1972 ).
  • the samples were incubated with a serum-activated solution containing radioactively labeled glycerol trioleate ([2- 3 H] glycerol trioleate) as substrate for the lipase.
  • TCA trichloroacetic acid
  • hydrolytic enzyme-stabilizing component brings about a marked improvement in enzyme stability compared to the control preparations without such a component. This opens up the possibility of being able to use less boric acid as an enzyme stabilizer in liquid surfactant preparations.

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Claims (7)

  1. Utilisation d'un composant comprenant de l'acide borique, de propylène glycol et d'un dérivé d'acide phénylborique doté de la structure chimique
    Figure imgb0005
     dans laquelle R représente de l'hydrogène, un groupe hydroxyle, un groupe alkyle en C1-C6, un groupe alkyle en C1-C6 substitué, un groupe alcényle en C1-C6 ou un groupe alcényle en C1-C6 substitué, pour stabiliser une enzyme hydrolytique dans une préparation liquide de tensioactifs contenant au moins un tensioactif, caractérisée en ce que le propylène glycol est présent dans une quantité allant de 0,000001 à 10 % en poids, le dérivé d'acide phénylborique est présent dans une quantité allant de 0,001 à 0,08 % en poids et l'acide borique est présent dans une quantité allant de 0,09 à 3,5 % en poids.
  2. Utilisation selon la revendication 1, caractérisé en ce que le résidu R dans le dérivé d'acide phénylborique est un groupe alkyle en C1-C6 ou de l'hydrogène.
  3. Utilisation selon la revendication 1 ou 2, caractérisée en ce que le dérivé d'acide phénylborique est de l'acide 4-formyl-phényl-borique.
  4. Utilisation selon l'une des revendications 1 à 3, caractérisé en ce que l'enzyme hydrolytique est présente dans une quantité allant de 1 x 10-8 à 5 % en poids rapporté à la protéine active.
  5. Utilisation selon l'une des revendications 1 à 4, caractérisée en ce que l'enzyme hydrolytique est une protéase, une amylase, une cellulase, une glycosidase, une hémicellulase, une mannanase, une xylanase, une xyloglucanase, une xanthanase, une pectinase, une β-glucosidase, une carraghénase ou une lipase ou un mélange, qui comprend au moins deux de ces enzymes, en particulier une lipase.
  6. Utilisation selon l'une des revendications 1 à 5, caractérisée en ce que la composition liquide de tensioactifs est un agent de lavage, de nettoyage ou de désinfection.
  7. Utilisation selon l'une des revendications 1 à 6, caractérisé en ce que la préparation liquide de tensioactifs comprend de plus au moins un autre ingrédient, sélectionné dans le groupe comprenant un adjuvant (builder), un agent solvant non-aqueux, de l'acide, un sel soluble dans l'eau, un agent épaississant, un composant désinfectant, ainsi que des combinaisons de ceux-ci.
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EP2640818A1 (fr) 2013-09-25
WO2012065839A1 (fr) 2012-05-24
US20130252315A1 (en) 2013-09-26

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