WO2010069812A2

WO2010069812A2 - Disinfection of viruses on textiles and hard surfaces

Info

Publication number: WO2010069812A2
Application number: PCT/EP2009/066583
Authority: WO
Inventors: Michael Heinzel; Dirk Bockmühl; Andrea Kyas; Timothy O'connell
Original assignee: Henkel Ag & Co. Kgaa
Priority date: 2008-12-18
Filing date: 2009-12-08
Publication date: 2010-06-24
Also published as: WO2010069812A3; DE102008062772A1

Abstract

Textiles and/or hard surfaces can be disinfected by bringing them into contact with a viricidal treatment solution which comprises at least one hydrolytic enzyme.

Description

Disinfecting viruses on textiles and hard surfaces

The invention is directed to a method for disinfecting textiles and / or hard surfaces by a virucidal treatment solution comprising at least one hydrolytic enzyme.

When washing textiles or cleaning hard surfaces such as bathroom tiles or crockery you expect not only a visually flawless cleanliness, but increasingly also an improved hygiene effect or disinfection of the funds used for cleaning. With disinfectants, a satisfactory hygiene effect is necessary anyway. With regard to the disinfection of textiles or hard surfaces, which is to be achieved in particular by a washing, cleaning or disinfecting agent, a distinction is usually made between the activity against germs and the effectiveness against viruses, whereby germs usually independently reproducible germs (so-called colony forming units). CFU), ie especially bacteria and fungi. The disinfection of viruses on textiles or hard surfaces is not satisfactory in contrast to the disinfection of germs.

It is known from the prior art that detergents or cleaners contain enzymes which improve the cleaning performance of the compositions. Typical enzymes in detergents or cleaners are proteases, amylases, cellulases, lipases, but also other hydrolytic enzymes.

It is also known that enzymes are capable of inactivating viruses. This applies in particular to RNases, DNases, transcriptases or amino acid lyases. Some of these enzymes are hydrolytic enzymes such as RNases or DNases. However, the said antiviral enzymes are mainly used in the therapy of viral infections. Furthermore, the use of hydrolytic enzymes in virus analysis or plant protection is known. For example, proteases are used in the preparative analysis of viral envelope proteins. Neither RNases, DNases, nor other hydrolytic enzymes are yet provided for the antiviral disinfection of textiles or hard surfaces.

For inactivating viruses on hard surfaces, the enzyme-based disinfectant Enzodine ™ is known (see Kessler & Richards, Symbollon Corp., Sudbury, 1993). This comprises as enzyme a peroxidase which has a corresponding virucidal activity. However, this composition contains no hydrolytic enzyme, in particular no protease, Amylase, cellulase, glycosidase, hemicellulase, mannanase, xylanase, pectinase, β-glucosidase, carrageenase or lipase.

Thus, it is not known from the prior art that a hydrolytic enzyme has a virucidal activity, i. has an activity against a virus when the hydrolytic enzyme is brought into contact with textiles or hard surfaces as part of a treatment solution.

Surprisingly, it has now been found that textiles or hard surfaces are disinfected in an improved manner when treated with a virucidal solution containing at least one hydrolytic enzyme. In particular, the hydrolytic enzyme improves the virus activity of a solution containing this enzyme.

The invention thus relates to a process for the disinfection of textiles and / or hard surfaces, which is characterized in that the textile and / or the hard surface is brought into contact with a virucidal treatment solution comprising at least one hydrolytic enzyme. An inventive method therefore causes at least a proportionate disinfection of the textile or the hard surface.

Disinfection in the context of the present invention is understood to be effective against at least one virus species (virus activity). A virucidal treatment solution is therefore a liquid composition which has viral activity against at least one virus species.

Viral efficacy is understood to mean any reduction in virus titer and, associated therewith, the infectivity of a virus, infectivity being the ability of a virus to infect a host. Viral activity is therefore advantageously achieved by damage to the virus or viruses, in particular with regard to the ability to adhere to a host cell and / or to introducing the genetic material into a host cell and / or to replicate the genetic material in a host cell. According to the invention, the hydrolytic enzyme contained in the virucidal treatment solution has viral activity and therefore contributes to the viral efficacy of the virucidal treatment solution.

The determination of the viral efficacy of the hydrolytic enzyme as well as the virucidal treatment solution can according to the established and accepted methodology of the DVV / RKI guideline (guideline of the German Association for the Control of Viral Diseases and the Robert Koch Institute for testing chemical disinfectants for efficacy against viruses in human medicine, version of 15 June 2005, Bundesgesundheitsblatt (Bundesgesundheitsblatt 48, (2005) 1420-1426), to the disclosure of which expressly referenced or whose disclosure is expressly incorporated into the present application. This method is used to test chemical disinfectants for effectiveness against viruses, but it is also applicable if, for example, the virus effectiveness of a substance to be determined, for example, that of the contained in the virucidal treatment solution hydrolytic enzyme. The methodology is equally applicable to mixtures and preparations as described below. In this case, the substance mixture or the preparation is used instead of the hydrolytic enzyme.

It is an in vitro suspension test in which the decrease (reduction) of the virus titer in the presence of the hydrolytic enzyme as an active ingredient is determined in comparison with an active ingredient-free water solution and expressed as the logarithm of this reduction factor (RF). The virus titer is a measure of a concentration of a virus. It is determined by diluting the sample continuously and diluting it with a detection test for the particular virus to be determined by inoculating the dilutions on cell cultures whose cells are permissive to the virus in question. The most extensive dilution at which a positive test reaction is still detectable is given as titre. In the present case, therefore, a test batch with a hydrolytic enzyme is compared with a parallel batch without this hydrolytic enzyme. The hydrolytic enzyme is used in a concentration of 100 ppm ("parts per million", 1 ppm = 10 "^6" = 0.0001%) The exposure time in the present invention is 15 or 30 minutes Values greater than one are indicative of viral activity, since in this case the decrease in virus titer in the assay is greater than the decrease in virus titer in the water Thus, viral efficacy is already present when there is a reduction in viral titer over the water feed, and it is not necessary to have complete viral efficacy, ie complete inactivation of all viruses of a virus species, in the sense that no virus titer is present Preferably virus efficacy is always assumed to be the case after the tested egg niger time under the respective test conditions, a reduction of Virustiters by at least 50%, and increasingly preferably by at least 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99% and most preferably by 99.99% (corresponds to at least 4 Iog10 levels). A preferred virus activity is indicated in particular by RF values of increasingly preferably 1, 5, 2, 2.5, 3, 3.5 and particularly preferably 4 or more.

The aforementioned DVV / RKI guideline stipulates that the temperature during the exposure time is 2O ⁰ C +/- 0.5 ⁰ C. However, the guideline also explicitly allows lower temperatures to be selected may be provided that the virus is inactivated at lower temperatures. Consequently, in the context of determining the virus activity in the context of the present application, it is also possible to select higher temperatures during the reaction time, provided that it is intended to use the hydrolytic enzyme or the virucidal treatment solution containing it at a higher temperature according to the invention.

Viruses (singular: virus) are understood to mean intracellular but even noncellular parasites that can infect cells of living beings. Viruses contain the genetic program (genetic material) in the form of at least one nucleic acid (deoxyribonucleic acid (DNA) or ribonucleic acid (RNA)) and, optionally, further auxiliary components for their propagation and propagation. However, they do not have their own metabolism, because they have no cytoplasm, which could be a medium for metabolic processes, and they lack both ribosomes and mitochondria. Therefore, they alone can not produce proteins, convert energy or replicate themselves. They are therefore dependent on the metabolism of the host cell. This makes them intracellular parasites. In essence, a virus is thus a nucleic acid on which the information for controlling the metabolism of a host cell is contained, in particular for replication of the virus nucleic acid and for further equipment of the virus particles (virions). Therefore, for the purposes of the present patent application, a virus can be both a single virus or a virus particle and a specific type of virus, which then naturally contains several or many individual viruses or virus particles of the same type (for example the same family, the same genus, the same Species or the same serotype).

Viruses come in two forms. In the first appearance as nucleic acid in the cells of the host, this nucleic acid contains the information for its replication by the host cell and for the production of the second manifestation, the virus particle (virion). The virion is secreted to spread the virus from the host cells. Virions are about 15 to 400 nm sized particles consisting of nucleic acids and a protein shell (capsid). Virions are significantly smaller than bacteria. In addition, some virions are surrounded by a membrane called the virus envelope or have other additional constituents. For example, in some types of viruses, the virions have a lipoprotein envelope. Such viruses, which have a lipoprotein envelope in addition to the capsid temporarily until the beginning of the replication phase, are enveloped viruses, viruses without such a casing are non-enveloped viruses. Virions are suitable for spreading the viruses. They invade (infect) all or part (at least their nucleic acid) into the host cells and the virus nucleic acid then programs their metabolism to increase the viral nucleic acid and to produce the other virion components. 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 (English Enzyme Commission numbers) form a numerical classification system for enzymes. Each EC number consists of four numbers separated by periods, the first digit designating one of the six major enzyme classes and hydrolases corresponding to the third major class with E.C. 3.X.X.X. Their representatives are proteases, peptidases, nucleases, phosphatases, glycosidases and esterases, with nucleases, in particular DNases and RNases, not being regarded as hydrolytic enzymes in the context of the present invention.

Usually, the viruses are in the form of the virion on textiles and hard surfaces. Therefore, according to the present invention, it is particularly and advantageously possible to inactivate even a virus present in the form of a virion on the textile or hard surface with a hydrolytic enzyme. However, nucleases, in particular DNases or RNases, are unsuitable for this purpose since they attack the genetic material of the viruses, which is not freely accessible in the virion but is packed in in some cases extremely complex structures. Therefore, virions on textiles or hard surfaces are not suitable for RNases or DNases or only insufficiently addressable with regard to a method according to the invention. In addition, such enzymes are relatively expensive. Overall, therefore, nucleases are not suitable for comparatively large-scale applications, as required by methods of the invention, and are therefore not considered to be hydrolytic enzymes in the context of the present invention.

Hydrolases preferred according to the invention are described below as preferred embodiments.

Textiles include all types of fabric, even of different composition, for example of cotton, wool, silk, other natural fibers, polyester and blended fabrics of any kind. Preferred textiles are linen. This is understood to mean the entirety of the washable textiles. Hard surfaces include, for example, surfaces of metal, glass, porcelain, ceramics, tiles, stone, plastic, wood or painted surfaces. Too hard surfaces include, in particular, bathroom tiles, tiles, surfaces of shower cubicles or other ceramic items in sanitary facilities. Hard surfaces also include any kind of tableware, countertops, floor coverings or table tops. Even carpets and leather are attributed according to the invention hard surfaces. A virucidal treatment solution can be, for example, an aqueous-based liquid, in particular water, a mixture with one or more solvents, which are usually present in liquid detergents or cleaners, or an alcohol-based liquid, in particular ethanol or isopropanol act, with water being preferred. Such a liquid may comprise as constituent only the hydrolytic enzyme and then constitutes a virucidal treatment solution according to the invention due to the viral activity of the hydrolytic enzyme. The hydrolytic enzyme may also be part of a liquid composition comprising, besides the hydrolytic enzyme, other ingredients and a virucidal Treatment solution within the meaning of the invention.

The concentration of the hydrolytic enzyme in the virucidal treatment solution is preferably in a range of 0.000005-0.1 g dry enzyme per 100 g treatment solution, and more preferably 0.0005-0.1 g dry enzyme per 100 g treatment solution and 0.005-0, 05 g dry enzyme per 100 g treatment solution. In this regard, the weight of the virucidal treatment solution is determined so that the data are based on weight of enzyme and weight of virucidal treatment solution.

The concentration of the enzyme in the virucidal treatment solution can be determined by known methods, for example, the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (AG Gornall, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766).

In a further embodiment of the invention, a method according to the invention is characterized in that the virucidal treatment solution further comprises at least one further disinfecting ingredient. In addition to ingredients having a virus activity, a disinfectant ingredient also includes those ingredients which, in addition or alternatively, have antimicrobial activity, ie kill germs. The germicidal effect is dependent on the content of the disinfecting ingredient in the virucidal treatment solution, wherein the germicidal effect decreases with decreasing content of disinfecting ingredient or increasing dilution of the virucidal treatment solution.

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" includes both the 1-propanol (n-propanol) and the 2-propanol ("isopropanol"). ethanol and / or propanol, for example, in an amount of 10 to 65 wt .-%, preferably 25 to 55 wt .-% in the virucidal treatment solution. Another preferred disinfecting ingredient is tea tree oil. These are the essential oil of the Australian Tea Tree (Melaleuca alternifolia), a native of New South Wales and Queensland evergreen shrub of the genus Myrtenheiden (Melaleuca), and other tea tree species from different genera (eg Baeckea, Kunzea and Leptospermum) in the family of myrtle family (Myrtaceae). 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, α-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 virucidal treatment solution, for example, in amounts of up to 10% by weight, preferably 0.2 to 5.0% by weight.

Further 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. Among these, 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 '. -Methylenebis (6-bromo-4-chlorophenol), 2,4,4'-trichloro-2'-hydroxydiphenyl ether, N- (4-chlorophenyl) -N- (3,4-dichlorophenyl) -urea, N , N '- (1, 10-decanediyldi-1-pyridinyl-4-ylidene) bis (1-octanamine) dihydrochloride, N, N'-bis (4-chlorophenyl) -3,12-diimino-2 , 4,11,13-tetraazatetradecandiimidamide, quaternary surface active compounds, guanidines. Preferred quaternary surface active compounds contain an ammonium, sulfonium, phosphonium, iodonium or arsonium group. Furthermore, disinfectant essential oils can be used, which at the same time provide for a scenting of the virucidal treatment solution. However, 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 .-%, more preferably 0.1 to 0.3 wt .-%, most preferably 0.2 wt .-% in the virucidal treatment solution.

In a further embodiment of the invention, the virucidal treatment solution further comprises a surfactant preparation. In the context of the present invention, the term "surfactant preparation" is understood to mean any composition which comprises at least one surfactant, preferably at least one of the surfactants mentioned below. In a preferred embodiment, the surfactant preparation is in particular a diluted or undiluted washing, cleaning, textile pretreatment or aftertreatment agent or disinfectant. These are also understood below by the term "surfactant preparation." As a result, the treated textile or the treated hard surface undergoes, in addition to a disinfection of viruses, at the same time a cleaning of soiling and / or a disinfection of germs.

Such surfactant preparations can be used as such or after dilution with water in the context of the inventive method. Such surfactant formulations are useful for the cleaning and / or disinfection of textiles or hard surfaces, optionally with a soil deposited thereon. If it is a liquid surfactant preparation, it can be used as such according to the invention and constitutes a surfactant preparation in the sense of the invention. However, a corresponding preparation can also be diluted in order to then prepare the surfactant preparation in the sense of the invention. Such a surfactant formulation can be readily prepared by diluting a measured amount of the surfactant formulation in a further amount of water in certain weight ratios of surfactant formulation: 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. Furthermore, it is also possible to dissolve an originally solid surfactant preparation, that is to say for example a pulverulent preparation or one in tablet form, in a liquid and preferably in water in order then to prepare a surfactant preparation in the sense of the invention.

Detergents which may be used here are all solid, liquid or flowable, gelatinous, custom-packaged or individually portionable, powdered, granulated, tabletted, pasty, sprayable or in other conventional dosage forms formulated for machine or manual textile washing. 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. The cleaning agents are all, also in all mentioned Detergents occurring means for cleaning hard surfaces, manual and automatic dishwashing detergents, carpet cleaners, scouring agents, glass cleaners, toilet scenters, etc. counted. 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. Amongst others, the fabric softeners are calculated. Disinfectants are, for example, hand disinfectants, surface disinfectants and instrument disinfectants, which may also occur in all of the above 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 . Also, disinfectants with an already existing germ-reducing effect can therefore be improved as part of a method according to the invention in their viral efficacy. "Flowable" in the sense of the present application are compositions which are pourable and may have viscosities up to several 10,000 mPas., The viscosity (measured using standard methods, for example, Brookfield viscometer LVT-II at 20 U / min and 2O ⁰ C, Spindle 3) and is preferably in the range of 5 to 10,000 mPas Preferred agents have viscosities of 10 to 8000 mPas, values between 120 and 3000 mPas being particularly preferred.

Suitable surfactants are, in particular, anionic surfactants, nonionic surfactants and mixtures thereof, but also cationic, zwitterionic and amphoteric surfactants.

Suitable nonionic surfactants are in particular alkyl glycosides and ethoxylation and / or propoxylation of alkyl glycosides or linear or branched alcohols each having 12 to 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10 alkyl ether groups. Furthermore, corresponding ethoxylation and / or propoxylation of N-alkyl-amines, vicinal diols, fatty acid esters and fatty acid amides, which correspond to said long-chain alcohol derivatives with respect to the alkyl moiety, and of alkylphenols having 5 to 12 carbon atoms in the alkyl radical.

The nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, especially primary alcohols having preferably 8 to 18 carbon atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical is linear or preferably 2-position may be methyl-branched or may contain linear and methyl-branched radicals in the mixture, as they are usually present in Oxoalkoholresten. In particular, however, alcohol ethoxylates with linear radicals of alcohols of natural 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 -C ₁₄ -alkyl with 3 EO or 4 EO, C ₉ -C ₁₁ -AlkOhOIe with 7 EO and 2-propylheptanol with 7 EO, C ₁₃ -C ₁₅ -AlkOhOIe with 3 EO, 5 EO, 7 EO or 8 EO, C ₁₂ -C ₁₈ -alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C ₁₂ -C ₁₄ -alcohol with 3 EO and C ₁₂ -C 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 rank ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples of these are (TaIg) fatty alcohols with 14 EO, 16 EO, 20 EO, 25 EO, 30 EO or 40 EO. Especially in surfactant formulations for use in mechanical processes usually extremely low-foam compounds are used. These include preferably C ₁₂ -C ₁₈ -alkylpolyethylenglykol-polypropylene glycol ethers with in each case at to 8 mol ethylene oxide and propylene oxide units in the molecule. However, it is also possible to use other known low-foam nonionic surfactants, for example C ₁₂ -C ₁₈ -alkyl polyethylene glycol-polybutylene glycol ethers having in each case up to 8 mol of ethylene oxide and butylene oxide units in the molecule, and also end-capped alkylpolyalkylene glycol mixed ethers. Also particularly preferred are the hydroxyl-containing alkoxylated alcohols, as described in European Patent Application EP 0 300 305, so-called hydroxy mixed ethers. The nonionic surfactants also include alkyl glycosides of the general formula RO (G) _x in which R is a primary straight-chain or methyl-branched, in particular 2-methyl-branched aliphatic radical having 8 to 22, preferably 12 to 18 carbon atoms and G represents a glycose unit having 5 or 6 C atoms, preferably glucose. The degree of oligomerization x, which indicates the distribution of monoglycosides and oligoglycosides, is an arbitrary number - which, as a variable to be determined analytically, may also be fractionated, is between 1 and 10; preferably x is 1, 2 to 1, 4. Also suitable are polyhydroxy fatty acid amides of the formula (III) in which R ¹ CO is an aliphatic acyl radical having 6 to 22 carbon atoms, R ^{2 is} hydrogen, an alkyl or hydroxyalkyl radical having 1 to 4 carbon atoms and [Z] is a linear or branched polyhydroxyalkyl radical having 3 to 10 carbon atoms and 3 to 10 hydroxyl groups:

R ²

R ¹ -CO-N- [Z] (III) The polyhydroxy fatty acid amides are preferably derived from reducing sugars having 5 or 6 carbon atoms, in particular from glucose. The group of polyhydroxy fatty acid amides also includes compounds of the formula (IV)

R ⁴ -OR ⁵

(IV)

R ³ -CO-N- [Z]

in the R ^{3 is} a linear or branched alkyl or alkenyl radical having 7 to 12 carbon atoms, R ^{4 is} a linear, branched or cyclic alkylene radical or an arylene radical having 2 to 8 carbon atoms and R ^{5 is} a linear, branched or cyclic alkyl radical or a Aryl radical or an oxy-alkyl radical having 1 to 8 carbon atoms, wherein dC ₄ alkyl or phenyl radicals are preferred, and [Z] is a linear polyhydroxyalkyl radical whose alkyl chain is substituted with at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated derivatives this rest stands. [Z] is also obtained here preferably by reductive amination of a sugar such as glucose, fructose, maltose, lactose, galactose, mannose or xylose. The N-alkoxy- or N-aryloxy-substituted compounds can then be converted into the desired polyhydroxy fatty acid amides, for example by reaction with fatty acid methyl esters in the presence of an alkoxide as catalyst. Another class of preferred nonionic surfactants used either as the sole nonionic surfactant or in combination with other nonionic surfactants, in particular together with alkoxylated fatty alcohols and / or alkyl glycosides, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably from 1 to 4 carbon atoms in the alkyl chain, especially fatty acid methyl ester. Nonionic surfactants of the amine oxide type, for example N-cocoalkyl-N, N-dimethylamine oxide and N-tallowalkyl-N, N-dihydroxyethylamine oxide, and the fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably not more than that of the ethoxylated fatty alcohols, especially not more than half thereof. Other suitable surfactants are so-called gemini surfactants. These are generally understood as meaning those compounds which have two hydrophilic groups per molecule. These groups are usually separated by a so-called "spacer". This spacer is typically a carbon chain that should be long enough for the hydrophilic groups to be spaced sufficiently apart for them to act independently of each other. Such surfactants are generally characterized by an unusually low critical micelle concentration and the ability to greatly reduce the surface tension of the water. In exceptional cases, the term gemini surfactants not only such "dimer", but also corresponding to "trimeric" surfactants understood. Examples of suitable gemini surfactants are sulfated hydroxy mixed ethers or dimer alcohol bis- and trimer tris-sulfates and ether sulfates. End-capped dimeric and trimeric mixed ethers are characterized in particular by their bi- and multi-functionality. Thus, the end-capped surfactants mentioned have good wetting properties and are low foaming, so that they are particularly suitable for use in machine washing or cleaning processes. However, it is also possible to use gemini-polyhydroxy fatty acid amides or poly-polyhydroxy fatty acid amides. Also suitable are the sulfuric acid monoesters of the straight-chain or branched C ₇ -C ₂ -substituted alcohols ethoxylated with from 1 to 6 mol of ethylene oxide, such as 2-methyl-branched C ₉ -C ₁₁ -alcohols having on average 3.5 mol of ethylene oxide (EO) or C ₁₂ C ₁₈ fatty alcohols with 1 to 4 EO. The preferred anionic surfactants also include the salts of alkylsulfosuccinic acid, which are also referred to as sulfosuccinates or as sulfosuccinic acid esters, and the monoesters and / or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and in particular ethoxylated fatty alcohols. Preferred sulfosuccinates contain C ₈ - to C ₁₈ - fatty alcohol residues or mixtures of these. Particularly preferred sulfosuccinates contain a fatty alcohol residue derived from ethoxylated fatty alcohols, which by themselves are nonionic surfactants. Sulfosuccinates, whose fatty alcohol residues are derived from ethoxylated fatty alcohols with a narrow homolog distribution, are again particularly preferred. Likewise, it is also possible to use alk (en) ylsuccinic acid having preferably 8 to 18 carbon atoms in the alk (en) yl chain or salts thereof. Suitable further anionic surfactants are fatty acid derivatives of amino acids, for example N-methyltaurine (Tauride) and / or N-methylglycine (sarcosides). Particularly preferred are the sarcosides or the sarcosinates and here especially sarcosinates of higher and optionally monounsaturated or polyunsaturated fatty acids such as oleyl sarcosinate. As further anionic surfactants are particularly soaps into consideration. Particularly suitable are saturated 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 or tallow fatty acids. Together with these soaps or as a substitute for soaps, it is also possible to use the known alkenylsuccinic acid salts.

The anionic surfactants, including soaps, may be in the form of their sodium, potassium or ammonium salts and as soluble salts of organic bases, such as mono-, di- or triethanolamine. The anionic surfactants are preferably present in the form of their sodium or potassium salts, in particular in the form of the sodium salts.

Surfactants are present in the surfactant preparation preferably in proportions of from 5% by weight to 50% by weight, in particular from 8% by weight to 30% by weight. In a further preferred embodiment, the surfactant preparation comprises at least one further ingredient, preferably one selected from the group consisting of builder, peroxygen compound, bleach activator, alcohol, acid, grayness inhibitor, optical brightener, foam inhibitor, water-soluble salt, polymeric thickener, volatile alkali and or base, hydrophilizing agent and combinations thereof.

In particular, a combination of the hydrolytic enzyme as the first component with one or more other ingredients of the virucidal treatment solution as the second component proves to be advantageous, since such a treatment solution brings about further improved viral efficacy by resulting synergies. This means that the treatment solution has an improved viral efficacy compared to a treatment solution containing either only one of the two components, or even compared to the expected viral efficacy of a treatment solution with both components due to the mere addition of the individual contributions of these two components to viral efficacy , In particular by the combination of the hydrolytic enzyme with one of the above-described further disinfecting ingredients and / or with one of the surfactants described above and / or with one of the builders described below and / or with one of the peroxygen compounds described below and / or with one of those described below Alcohol is achieved such a synergy.

A surfactant preparation according to the invention may further contain at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The water-soluble organic builder substances include polycarboxylic acids, in particular citric acid and sugar acids, monomeric and polymeric aminopolycarboxylic acids, in particular methylglycinediacetic acid, nitrilotriacetic acid and ethylenediaminetetraacetic acid and polyaspartic acid, polyphosphonic acids, in particular aminotris (methylenephosphonic acid), ethylenediaminetetrakis (methylenephosphonic acid) and 1-hydroxyethane-1,1-diphosphonic acid, polymeric hydroxy compounds such as dextrin and polymeric (poly) carboxylic acids, in particular the polycarboxylates obtainable by oxidation of polysaccharides or dextrins, polymeric acrylic acids, methacrylic acids, maleic acids and mixed polymers of these, which may also contain small amounts of polymerizable substances without carboxylic acid functionality in copolymerized form. The molecular weight of the homopolymers of unsaturated carboxylic acids is generally between 3,000 and 200,000, of the copolymers between 2,000 and 200,000, preferably 30,000 to 120,000, each based on the free acid. A particularly preferred acrylic acid-maleic acid copolymer has a molecular weight of from 30,000 to 100,000. Commercially available products are, for example, Sokalan® CP 5, CP 10 and PA 30 from BASF. Suitable, although less preferred compounds of this class are copolymers of acrylic acid or methacrylic acid with vinyl ethers, such as vinylmethyl ethers, vinyl esters, ethylene len, propylene and styrene, in which the proportion of acid is at least 50 wt .-%. It is also possible to use terpolymers which contain two unsaturated acids and / or salts thereof as monomers and also vinyl alcohol and / or an esterified vinyl alcohol or a carbohydrate as the third monomer as water-soluble organic builder substances. The first acidic monomer or its salt is derived from a monoethylenically unsaturated C ₃ -C ₈ -carboxylic acid and preferably from a C ₃ -C ₄ -monocarboxylic acid, in particular from (meth) acrylic acid. The second acidic monomer or its salt may be a derivative of a C ₄ -C ₈ -dicarboxylic acid, with maleic acid being particularly preferred, and / or a derivative of an alkylsulfonic acid which is substituted in the 2-position by an alkyl or aryl radical , Such polymers generally have a molecular weight between 1,000 and 200,000. Further preferred copolymers are those which preferably have as monomers acrolein and acrylic acid / acrylic acid salts or vinyl acetate. The organic builder substances can be used, in particular for the preparation of liquid surfactant preparations, in the form of aqueous solutions, preferably in the form of 30 to 50 percent by weight aqueous solutions. All of the acids mentioned are generally used in the form of their water-soluble salts, in particular their alkali metal salts.

If desired, such 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.

Suitable water-soluble inorganic builder materials are, in particular, alkali metal silicates, alkali metal carbonates and alkali metal phosphates, which may be in the form of their alkaline, neutral or acidic sodium or potassium salts. Examples of these are trisodium phosphate, tetra sodium diphosphate, disodium dihydrogen diphosphate, pentasodium triphosphate, so-called sodium hexametaphosphate, oligomeric trisodium phosphate with degrees of oligomerization of from 5 to 1000, in particular from 5 to 50, and the corresponding potassium salts or mixtures of sodium and potassium salts. As water-insoluble, water-dispersible inorganic builder materials are in particular crystalline or amorphous alkali metal aluminosilicates, in amounts of up to 50 wt .-%, preferably not more than 40 wt .-% and in liquid surfactant preparations, in particular from 1 wt .-% to 5 wt .-%, used. Among these, preferred are the detergent grade crystalline sodium aluminosilicates, particularly zeolite A, P and optionally X, alone or in mixtures, for example in the form of a cocrystal of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA) , Amounts near the stated upper limit are preferably used in solid, particulate surfactant formulations. In particular, suitable aluminosilicates have no particles with a particle size of more than 30 μm and preferably consist of at least 80% by weight of particles of one size below 10 μm. Their calcium binding capacity, which can be determined according to the specifications of the German patent DE 24 12 837, is generally in the range of 100 to 200 mg CaO per gram.

Suitable substitutes or partial substitutes for the said aluminosilicate are crystalline alkali silicates which may be present alone or in a mixture with amorphous silicates. The alkali metal silicates useful as builders in the surfactant formulations preferably have a molar ratio of alkali metal oxide to SiO ₂ below 0.95, in particular from 1: 1, 1 to 1: 12, and may be present in amorphous or crystalline form. Preferred alkali metal silicates are the sodium silicates, in particular the amorphous sodium silicates, with a molar ratio of Na ₂ O: SiO ₂ of 1: 2 to 1: 2.8. The crystalline silicates which may be present alone or in admixture with amorphous silicates, are crystalline layer silicates with the general formula Na ₂ Si _x O y are used _{2x + 1} H ₂ O, in which x, known as the modulus, an integer of 1, 9 to 22, in particular 1, 9 to 4 and y is a number from 0 to 33 and preferred values for x are 2, 3 or 4. Preferred crystalline phyllosilicates are those in which x in the abovementioned general formula assumes the values 2 or 3. In particular, both β- and δ-sodium disilicates (Na ₂ Si ₂ O ₅ y H ₂ O) are preferred. Also prepared from amorphous alkali metal silicates, practically anhydrous crystalline alkali silicates of the abovementioned general formula in which x is a number from 1, 9 to 2.1, can be used in surfactant preparations according to the invention. In a further preferred surfactant preparation, a crystalline sodium layer silicate having a modulus of 2 to 3 is used, as can be prepared from sand and soda. Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further preferred surfactant preparation. Crystalline layer-form silicates of formula (I) given above are sold by Clariant GmbH under the trade name Na-SKS, eg Na-SKS-1 (Na ₂ Si ₂₂ O ₄₅ XH ₂ O, Kenyaite), Na-SKS-2 (Na ₂ Sii ₄ 0 ₂₉ x H ₂ 0, magadiite), Na-SKS-3 (Na ₂ Si ₈ Oi ₇ XH ₂ O) or Na-SKS-4 (Na ₂ Si ₄ O ₉ XH ₂ O, makatite). Of these, especially Na-SKS-5 ((X-Na ₂ Si ₂ O _5), are Na-SKS-7 (.beta.-Na ₂ Si ₂ 0 _5, natrosilite), Na SKS-9 (NaHSi ₂ O ₅ 3H ₂ O), Na-SKS-10 (NaHSi ₂ O ₅ 3H ₂ O, kanemite), Na-SKS-11 (t-Na ₂ Si ₂ 0 ₅₎ and Na SKS-13 (NaHSi ₂ O ₅₎ In particular, Na-SKS-6 (5-Na ₂ Si ₂ O ₅ ) In a preferred embodiment of a surfactant preparation according to the invention, a granular compound of crystalline phyllosilicate and citrate, of crystalline phyllosilicate and the abovementioned (co-) polymeric polycarboxylic acid, or from alkali metal silicate and alkali metal carbonate, as it is commercially available, for example, under the name Nabion® 15.

Builder substances are preferably present in the surfactant preparations in amounts of up to 75% by weight, in particular 5% by weight to 50% by weight.

Suitable peroxygen compounds for use in surfactant preparations in the context of the invention are in particular organic peracids or peracid salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and under the washing conditions hydrogen peroxide-releasing inorganic salts, which include perborate, percarbonate, persilicate and / or persulfate such as caroate into consideration. If solid peroxygen compounds are to be used, they can be used in the form of powders or granules, which can also be enveloped in a manner known in principle. If a surfactant preparation contains peroxygen compounds, they are present in amounts of preferably up to 50% by weight, especially from 5% to 30% by weight. The addition of small amounts of known bleach stabilizers such as, for example, phosphonates, borates or metaborates and metasilicates and also magnesium salts such as magnesium sulfate may be expedient.

As bleach activators, it is possible to use compounds which, under perhydrolysis conditions, give aliphatic peroxycarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid. Suitable substances are those which carry O- and / or N-acyl groups of the stated C atom number and / or optionally substituted benzoyl groups. Preference is given to polyacylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N- Acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates, in particular n-nonanoyl or isononanoyloxybenzenesulfonate (n- or iso-NOBS), carboxylic anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy- 2,5-dihydrofuran and enol esters and also acetylated sorbitol and mannitol or their described mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfruktose, tetraacetylxylose and octaacetyllactose as well as acetylated, optionally N-alkylated glucamine and gluconolactone, and / or N- acylated lactams, for example N-benzoyl-caprolactam. The hydrophilic substituted acyl acetals and the acyl lactams are also preferably used. Combinations of conventional bleach activators can also be used. Such bleach activators can, in particular in the presence of the abovementioned hydrogen peroxide-supplied bleach, in the usual amount range, preferably in amounts of from 0.5 wt .-% to 10 wt .-%, in particular 1 wt .-% to 8 wt .-%, based on However, the total surfactant preparation, be contained when using percarboxylic acid as the sole bleach, but preferably completely.

In addition to the conventional bleach activators or in their place, sulfone imines and / or bleach-enhancing transition metal salts or transition metal complexes may also be present as so-called bleach catalysts. Among the organic solvents which can be used in the surfactant preparations, especially when they are in liquid or pasty form, are alcohols having 1 to 4 C atoms, in particular methanol, ethanol, isopropanol and tert-butanol, diols having 2 to 4 C atoms. Atoms, in particular ethylene glycol and propylene glycol, and mixtures thereof and derivable from the said classes of compounds ethers. Such water-miscible solvents are preferably present in the surfactant formulations in amounts not exceeding 30% by weight, in particular from 6% by weight to 20% by weight.

To establish a desired, not by itself resulting from the mixture of the other components of the pH, the surfactant formulations systemic and environmentally friendly 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. Such 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.

Graying inhibitors have the task of keeping suspended from the textile fiber dirt suspended in the fleet. Water-soluble colloids of mostly organic nature are suitable for this purpose, for example starch, glue, gelatin, salts of ether carboxylic acids or ether sulfonic acids of starch or of cellulose or salts of acidic sulfuric acid esters of cellulose or starch. Also, water-soluble polyamides containing acidic groups are suitable for this purpose. Furthermore, other than the above-mentioned starch derivatives can be used, for example aldehyde starches. Preference is given to using cellulose ethers, such as carboxymethylcellulose (Na salt), methylcellulose, hydroxyalkylcellulose and mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, methylcarboxymethylcellulose and mixtures thereof, for example in amounts of from 0.1 to 5% by weight, based on the surfactant preparation ,

Laundry detergents may contain, for example, derivatives of diaminostilbenedisulfonic acid or their alkali metal salts as optical brighteners, although they are preferably free of optical brighteners for use as color detergents. For example, salts of 4,4'-bis (2-anilino-4-morpholino-1, 3,5-triazinyl-6-amino) stilbene-2,2'-disulphonic acid or compounds of similar construction which are used instead of the morpholino Group carry a diethanolamino group, a methylamino group, an anilino group or a 2-methoxyethylamino group. Further, brighteners of the substituted diphenylstyrene type may be present, for example, the alkali salts of 4,4'-bis (2-sulfostyryl) -diphenyl, 4,4'-bis (4-chloro-3-sulfostyryl) -diphenyl, or 4 - (4-chlorostyryl) -4 '- (2-sulfostyryl). Mixtures of the aforementioned optical brightener can be used. In particular when used in mechanical processes, it may be advantageous to add conventional foam inhibitors to the surfactant preparations. Suitable foam inhibitors are, for example, soaps of natural or synthetic origin, which have a high proportion of C ₁₈ -C ₂₄ fatty acids. Suitable non-surfactant foam inhibitors are, for example, organopolysiloxanes and mixtures thereof with microfine, optionally silanized silica and paraffins, waxes, microcrystalline waxes and mixtures thereof with silanated silica or bis-fatty acid alkylenediamides. It is also advantageous to use mixtures of various foam inhibitors, for example those of silicones, paraffins or waxes. Preferably, the foam inhibitors, in particular silicone and / or paraffin-containing foam inhibitors, are bound to a granular, water-soluble or dispersible carrier substance. In particular, mixtures of paraffins and bistearylethylenediamide are preferred.

A surfactant preparation in the context of 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. Particularly preferred are halides and sulfates of the alkali metals; Preferably, therefore, 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. Preferably, the salts are selected from the group comprising formate, acetate, propionate, citrate, malate, tartrate, succinate, malonate, oxalate, lactate and mixtures thereof.

For thickening, a surfactant formulation may contain one or more polymeric thickeners. Polymeric thickeners are the polyelectrolytes thickening polycarboxylates, preferably homo- and copolymers of acrylic acid, in particular acrylic acid copolymers such as acrylic acid-methacrylic acid copolymers, and the polysaccharides, especially heteropolysaccharides, and other conventional thickening polymers. Suitable polysaccharides or heteropolysaccharides are the polysaccharide gums, for example gum arabic, agar, alginates, carrageenans and their salts, guar, guar gum, tragacanth, gellan, Ramzan, dextran or xanthan and their derivatives, for example propoxylated guar, and also their mixtures. Other polysaccharide thickeners, such as starches or cellulose derivatives, may be used alternatively, but preferably in addition to a polysaccharide gum, for example starches of various origins and starch derivatives, for example hydroxyethyl starch, starch phosphate esters or starch acetates, or carboxymethylcellulose or its sodium salt, methyl, ethyl, hydroxyethyl, hydroxypropyl, hydroxypropylmethyl or hydroxyethyl methylcellulose or cellulose acetate.

A preferred polymeric thickener is the microbial anionic heteropolysaccharide xanthan gum produced by Xanthomonas campestris and some other species under aerobic conditions having a molecular weight of 2-15x10 ⁶ and available, for example, from Kelco under the trade name Keltrol®, eg cream-colored powder Keltrol® T (transparent) or as white granules Keltrol® RD (Readily Dispersable).

Examples of acrylic acid polymers which are suitable as polymeric thickeners are high molecular weight homopolymers of acrylic acid (INCI Carbomer) crosslinked with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol or propylene (INCI Carbomer), which are also referred to as carboxyvinyl polymers. Such polyacrylic acids are i.a. available from BFGoodrich under the trade name Carbopol®, e.g. Carbopol® 940 (molecular weight about 4,000,000), Carbopol® 941 (molecular weight about 1,250,000) or Carbopol® 934 (molecular weight about 3,000,000). The content of polymeric thickener is usually not more than 8 wt .-%, preferably between 0.1 and 7 wt .-%, particularly preferably between 0.5 and 6 wt .-%, in particular between 1 and 5 wt .-% and most preferably between 1, 5 and 4% by weight, for example between 2 and 2.5% by weight.

A surfactant preparation may further contain volatile alkali. As such, ammonia and / or alkanolamines, which may contain up to 9 C atoms in the molecule, are used. As alkanolamines, the ethanolamines are preferred and of these in turn the monoethanolamine. The content of ammonia and / or alkanolamine is preferably 0.01 to 2 wt .-%; ammonia is particularly preferably used. In addition, small amounts of bases may be included. Preferred bases are selected from the group of alkali and alkaline earth metal hydroxides and carbonates, in particular the alkali metal hydroxides, of which potassium hydroxide and especially sodium hydroxide is particularly preferred.

A surfactant preparation may also contain a hydrophilizing agent. These are understood in the context of the present invention means for the hydrophilization of surfaces. In particular, colloidal silica sols in which the silicon dioxide is present nanoparticulate are suitable for hydrophilization. Colloidal nanoparticulate silica sols for the purposes of this invention are stable dispersions of amorphous particulate silicon dioxide SiO ₂ having particle sizes in the range from 1 to 100 nm. The particle sizes are preferably in the range from 3 to 50 nm, particularly preferably from 4 to 40 nm a silica sol which is suitable for use in the context of this invention is that under the trade name Bindzil® 30/360 from Akzo available silica sol with a particle size of 9 nm. Further suitable silica sols are Bindzil® 15/500, 30/220, 40/200 (Akzo), Nyacol® 215, 830, 1430 , 2034DI and Nyacol® DP5820, DP5480, DP5540, etc. (Nyacol Products), Levasil® 100/30, 100F / 30, 100S / 30, 200/30, 200F / 30, 300F / 30, VP 4038, VP 4055 (HC Starck / Bayer) or else CAB-O-SPERSE® PG 001, PG 002 (aqueous dispersions of CAB-O-SIL®, Cabot), Quartron PL-1, PL-3 (Fuso Chemical Co.), Köstrosol 0830, 1030, 1430 (Chemiewerk Bad Köstritz). The silica sols used may also be surface-modified silica treated with sodium aluminate (alumina-modified silica).

In addition, it is also possible to use certain polymers for the hydrophilization of surfaces. Particularly suitable hydrophilizing polymers are amphoteric polymers, for example copolymers of acrylic or methacrylic acid and MAPTAC, DADMAC or another polymerisable quaternary ammonium compound. Furthermore, it is also possible to use copolymers with AMPS (2-acrylamido-2-methylpropanesulfonic acid). Polyethersiloxanes, ie copolymers of polymethylsiloxanes with ethylene oxide or propylene oxide segments, are further suitable polymers. Also usable are acrylic polymers, maleic acid copolymers and polyurethanes with PEG (polyethylene glycol) units. Suitable polymers are, for example, under the trade names Mirapol Surf-S 100, 110, 200, 210, 400, 410, A 300, A 400 (Rhodia), Tegopren 5843 (Goldschmidt), Sokalan CP 9 (BASF) or Polyquart Ampho 149 (Cognis ) commercially available.

The constituents of the surfactant preparation to be selected, as well as the conditions under which they are used according to the invention, such as temperature, pH, ionic strength, redox ratios or mechanical influences, are usually optimized for the respective field of application.

In the context of the present invention, the hydrolytic enzyme and thus the virucidal treatment solution containing it have a virus activity against at least one virus, preferably against several viruses. However, it is not mandatory that virus activity be against a virus belonging to the poliovirus species. Polioviruses can be excluded from the method according to the invention, since they can be efficiently controlled on the basis of steadily improved vaccinations or vaccination campaigns and, in addition, are considered extinct almost worldwide. Another method according to the invention is therefore characterized in that the method is not directed against a virus belonging to the species Poliovirus. Such a method can therefore also be carried out with a virucidal treatment solution which has a virus activity against a virus which is not a member of the species poliovirus. The poliovirus is a virus belonging to the genus Enterovirus of the family Picornaviridae. It triggers polio or poliomyelitis in humans. It is a very simple virus without envelope with a genome of single stranded plus RNA. The approximately round virus particle has a diameter of 28 to 30 nanometers. Each virion contains a copy of the single-stranded RNA genome enveloped by an icosahedral capsid. The capsid consists of 60 copies each of the four capsid proteins (VP1, VP2, VP3 and VP4). The virus has no shell. The poliovirus proliferates in the cytoplasm of the host cell. In order to enter the cell, the virus needs a specific receptor, the CD155 protein. Then the virus can transfer its RNA into the cell, where it is translated directly to the polyprotein. The polyprotein itself can proteolytically break down into individual structural and functional proteins. The RNA is not only translated but also replicated. The latter is done by a viral RNA-dependent RNA polymerase (3Dpol), which rewrites the original plus RNA into a minus RNA and immediately generates new plus RNA from it. The RNA is finally packaged with the structural proteins to a new virion. Eventually, the host cell dies and the viruses are released.

Preferred methods according to the invention are characterized in that the hydrolytic enzyme has a virus activity against a virus selected from the group consisting of Adenoviridae, Alphaherpesvirinae, Astroviridae, Betaherpesvirinae, Birnaviridae, Bornaviridae, Bunyaviridae, Caliciviridae, Chordopoxviridae, Filoviridae, Flaviviridae, Gammaherpesvirinae, Hepadnaviridae, Herpesviridae, Iridoviridae, Orthomyxoviridae, Orthoretroviridae, Papillomaviridae, Paramyxovirinae, Parvovirinae, Picornaviridae, Pneumovirinae, Polyomaviridae, Reoviridae, Rhabdoviridae, Roniviridae, Spumaretroviridae and Togaviridae.

In particular, it is a virus belonging to one of the following genera: alpha papillomavirus, alpharetrovirus, alphavirus, aphthovirus, aquabirnavirus, aquareovirus, avibirnavirus, avulavirus, betapapillomavirus, betaretrovirus, bocavirus, bornavirus, cardiovirus, coltivirus, cypovirus, cytomegalovirus, Deltaretrovirus, Deltavirus, Dependovirus, Ebola virus, Enterovirus, Ephemerovirus, Epsilonretrovirus, Erbovirus, Erythrovirus, Fijivirus, Flavivirus, Fungal Prions, Gammapapillomavirus, Gammaretrovirus, Hantavirus, Henipavirus, Hepacivirus, Hepatovirus, Hepevirus, Ictalurivirus, Idnoreovirus, Iflavirus, Influenza A, Influenza B , Influenza virus C, Iridovirus, Kobuvirus, Lentivirus, Lymphocryptovirus, Lyssavirus, Mamastrovirus, Marburgvirus, Mastadenovirus, Megalocytivirus, Morbillivirus, Mupapillomavirus, Muromegalovirus, Mycoreovirus, Nairovirus, Norovirus, Novirhabdovirus, Nupapillomavirus, Okavirus, Orbivirus, Orthobunyavirus, Orthohepadnavirus, Orthopoxvirus, Orthoreovirus, Oryzavirus, Parechovirus, Parvovirus, Pestivirus, Phlebovirus, Phytoreovirus, Pneumovirus, Polyomavirus, Respirovirus, Rhadinovirus, Rhinovirus, Roseolovirus, Rotavirus, Rubivirus, Rubulavirus, Sapovirus, Seadornavirus, Simplexvirus, Spumavirus, Teschovirus, Varicellovirus, Vesiculovirus, Vesivirus.

The said genera in turn comprise one or more virus species (virus species), and these in turn may comprise different virus serotypes. Serotypes are serologically distinguishable variations of a virus. The serotype can be determined by serological tests (for example enzyme-linked immunosorbent assay (ELISA)), which are based on the specific properties of the antibodies directed against certain surface structures (antigens) of the virus particle The different strains each represent a distinct serotype that can be determined by a serological test The immune system treats each serotype of a virus as an immunologically distinct virus so that each serotype leads to a type-specific immunity Serotypes are therefore distinguishable in particular on the basis of the antibodies directed against them.

The designation of the viruses is carried out according to the usual and established virus taxonomy of the International Committee on Taxonomy of Viruses (ICTV, see in particular CM Fauquet, MA Mayo et al .: Eighth Report of the International Committee on Taxonomy of Viruses, London, San Diego, 2004). In particular, this taxonomy considers the genome structure (DNA, RNA, single-stranded, double-stranded, polarity, linear, circular, segmented), the shape (symmetry) of the capsid, the presence of a shell, the location of the genes within the genome, the replication strategy, and virus size ,

For viruses of the aforementioned virus families and virus genera, it has been found that their disinfection on textiles and / or hard surfaces by the hydrolytic enzymes in the virucidal treatment solution is particularly advantageous.

Since the hydrolytic enzyme makes a significant contribution to the disinfection of the textile or the hard surface, an inventive method under such conditions (such as temperature, pH, ionic strength, redox ratios), under which the hydrolytic enzyme is catalytically active. Conversely, the hydrolytic enzyme may be chosen to be catalytically active under the particular conditions under which the virucidal treatment solution is applied. Preferably, a process according to the invention is carried out in a temperature range between 1O ⁰ C and 6O ⁰ C, in particular between 1O ⁰ C and 5O ⁰ C and particularly preferably between 1O ⁰ C and 4O ⁰ C. Thermostable hydrolytic enzymes could even at even higher temperatures than 6O ⁰ C can be used in the inventive method, for example to 7O ⁰ C or 75 ⁰ C. The pH at which an inventive Method advantageously carried out, may be dependent on the subject to be disinfected according to the invention. For example, a virucidal treatment solution based on a toilet detergent advantageously has an acidic pH, for example a pH between pH 2 and pH 5. A virucidal treatment solution 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 pH1 1 or between pH7 and pH10. For example, a virucidal treatment solution based on a hand dishwashing detergent has a pH between pH 6.5 and pH 8.

In a further embodiment, a method according to the invention is characterized in that the virucidal treatment solution is in contact with the textile or the hard surface for at least 10 seconds and more preferably for at least 15, 20, 25 and 30 seconds. This aspect relates to the minimum exposure time of the virucidal treatment solution to the virus to achieve a satisfactory viral efficacy. However, the exposure time may be longer, for example at least 60, 90, 120, 150, 180, 210, 240, 270 or 300 seconds, or at least 10, 20, 30, 40, 50 or 60 minutes.

In a further embodiment, the hydrolytic enzyme or the virucidal treatment solution containing the hydrolytic enzyme has an RF value greater than one, determined according to the DVV / RKI guideline. As explained above, the RF value is a measure of the decrease in virus titer in the presence of a hydrolytic enzyme or a virucidal treatment solution containing the hydrolytic enzyme as compared to a water batch. The RF value is determined as described above. RF values greater than one indicate viral efficacy, since in this case the decrease in virus titer in the assay is greater than the decrease in virus titer in the water. More preferably, the hydrolytic enzyme or the virucidal treatment solution containing the hydrolytic enzyme has an RF value greater than or equal to 1, 5, 2, 2.5, 3, 3.5, and more preferably greater than or equal to 4.

In a further preferred embodiment of a method according to the invention, the hydrolytic enzyme is a protease, amylase, cellulase, glycosidase, hemicellulase, mannanase, xylanase, pectinase, β-glucosidase, carrageenase or a lipase or a mixture comprising at least two of these enzymes.

Because for all these enzymes a virus activity was found so that they are suitable for the disinfection of viruses on textiles and / or hard surfaces in the context of inventive methods. Most preferably, the hydrolytic enzyme is a Protease and including preferably a serine protease, more preferably a subtilase and most preferably a subtilisin.

Subtilases (also subtilopeptidases, EC 3.4.21.62) are serine proteases and act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. For an overview of this family, see, for example, the article "Subtilases: Subtilisin-like Proteases" by R. Siezen, pages 75-95 in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996. Subtilases become natural formed by microorganisms. Among the subtilases, the most subtilisins formed and secreted by Bacillus species are the most important group.

Numerous proteases and in particular subtilisins are formed as so-called pre-proteins, ie together with a propeptide and a signal peptide, the function of the signal peptide usually being to ensure the release of the protease from the cell producing it into the periplasm or the medium surrounding the cell. and the propeptide is usually necessary for the correct folding of the protease. The signal peptide and the propeptide are usually the N-terminal part of the preprotein. The signal peptide and the propeptide are cleaved from the rest of the protease under natural conditions during the secretion and folding process. Due to their enzymatic activity, mature (mature) proteases, e.g. the pre-processed enzymes without signal and propeptide, preferred over the preproteins. The proteases may be modified by the cells producing them after production of the polypeptide chain, for example by attachment of sugar molecules, formylations, aminations, etc. Such post-translational modifications may or may not exert an influence on the function of the protease.

Examples of 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. The 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. Further useful proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® by the company Novozymes, which are among others 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® of Wuxi Snyder Bioproducts Ltd., China, sold under the trade names Proleather® and Protease P® by the company Amano Pharmaceuticals Ltd., Nagoya, Japan, and the proteinase K-16 by the company Kao Corp., Tokyo, Japan, available enzymes. Also particularly preferred are the proteases from Bacillus gibsonii and Bacillus pumilus disclosed in international patent applications WO 08/086916 and WO 07/131656. Further advantageous proteases are disclosed in 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 naturally present in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius and Bacillus sphaericus.

Examples of amylases are the α-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. Further development products of this α-amylase are 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 α-amylase is sold by the company Novozymes under the name BAN®, and variants derived from the Bacillus stearothermophilus α-amylase under the names BSG® and Novamyl®, also from the company Novozymes. Furthermore, for this purpose, the α-amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948). Also useful are the amylolytic enzymes disclosed in International Patent Applications WO 03/002711, WO 03/054177 and WO07 / 079938. Likewise, fusion products of all the molecules mentioned can be used. In addition, the further developments of the α-amylase from Aspergillus niger and A. oryzae available under the trade name Fungamyl® from the company Novozymes are suitable. Further usable commercial products are, for example, the Amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus®, the latter also from the company Novozymes. Also variants of these enzymes obtainable by point mutations can be used according to the invention. Examples of cellulases (endoglucanases, EG) is the fungal, endoglucanase (EG) -rich cellulase preparation or its further developments, which is offered by the company Novozymes under the trade name Celluzyme®. Endolase® and Carezyme®, also available from Novozymes, 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®. Furthermore, for example, the 20 kD-EG from Melanocarpus, which are available from the company AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®. Other commercial products of 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 commercial products of Danisco / Genencor are "Genencor detergent cellulase L" and lndiAge®Neutra.

Further preferred 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, β-glucosidases, xyloglucanases (xylanases) and pectin-degrading enzymes (pectinases ). Preferred glycosidases are also summarized by the term hemicellulases. Hemicellulases include, in particular, mannanases, xyloglucanases (xylanases), β-glucosidases and carrageenases, and also pectinases, pullulanases and β-glucanases. Pectinases are pectin-degrading enzymes, wherein the hydrolytic pectin-degrading enzymes belong in particular to the enzyme classes EC 3.1.1.1 1, EC 3.2.1.15, EC 3.2.1.67 and EC 3.2.1.82. Other names include pectin esterase, pectin methethoxylase, pectin methoxylase, pectin methyl esterase, pectase, pectin methyl esterase, pectin esterase, pectin pectyl hydrolase, pectin polymerase, endopolygalacturonase, pectolase, pectin hydrolase, pectin polygalacturonase, endo-polygalacturonase, poly-α-1, 4-galacturonide glycanohydrolase, endogalacturonase, endo D-galacturonase, galacturan 1, 4-α-galacturonidase, exopolygalacturonase, poly (galacturonate) hydrolase, exo-D-galacturonase, exo-D-galacturonanase, exopoly-D-galacturonase, exo-poly-α-galacturonosidase, exopolygalacturonosidase or Exopolygalacturanosidase.

Suitable enzymes for this purpose are, for example, under the name Gamanase® and Pektinex AR® from the company Novozymes, under the name Rohapec® B1 L from the company AB Enzymes and under the name Pyrolase® from Diversa Corp., San Diego, CA, USA available. The β-glucanase obtained from Bacillus subtilis is available under the name Cereflo® from the company Novozymes. Particularly according to the invention preferred glycosidases or hemicellulases are mannanases, which are sold, for example, under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Danisco / Genencor.

Examples of 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®. Furthermore, for example, the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens. Also useful 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. Other important commercial products are preparations M1 Lipase® and Lipomax®, originally sold 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.

Of all these enzymes, particular preference is given to those which are comparatively stable per se by oxidation or have been stabilized, for example, by mutations, in particular by substitution, deletion or insertion of one or more amino acids. For this purpose, in particular the already mentioned commercial products Everlase and Purafect® OxP are to be cited as examples of such proteases and Duramyl as an example of such an α-amylase.

The enzymes used according to the invention are preferably originally derived from microorganisms, such as the genera Bacillus, Streptomyces, Humicola or Pseudomonas, and / or are produced by biotechnological methods known per se by suitable microorganisms, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi. It is emphasized that these may in particular also be technical enzyme preparations of the particular hydrolytic 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 stabilizers.

If several hydrolytic enzymes are used according to the invention for disinfecting viruses on textiles or hard surfaces, they show a particularly preferred one in this respect synergistic effect. This means that the combination of the hydrolytic enzymes used has an improved viral efficacy compared to the viral efficacy of either one of these enzymes, or even compared to the expected viral efficacy of the enzymes due to the mere addition of the individual contributions of these enzymes to viral efficacy. Most preferably, such a synergy exists between two proteases or between a protease and an amylase and / or a mannanase and / or a lipase.

Another object of the invention is a process for the preparation of a virucidal treatment solution for the disinfection of textiles and / or hard surfaces, which is characterized in that at least one hydrolytic enzyme is added to the treatment solution.

All facts, objects and embodiments described above for inventive method are also applicable to this subject of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive method for producing a virucidal treatment solution for the disinfection of textiles and / or hard surfaces.

Example:

The virus activity of the following hydrolytic enzymes was determined according to the DVV / RKI Guideline (German Association for the Control of Viral Diseases eV / Robert Koch Institute, see Bundesgesundheitsblatt (2005), 48, 1420-1426), ie it was the decrease the virus titer of the virus examined in the presence of the respective hydrolytic enzyme determined in comparison to the decrease of the virus titer of the virus examined in a water batch without the hydrolytic enzyme. All test solutions were dissolved in dest. Water attached. It was incubated at 4O ⁰ C for the indicated times in the following table. The application concentration of the hydrolytic enzyme was 100 ppm. For some enzymes, additional measurements were made at an application level of 1 ppm. The host cells used for titer determination according to the DVV / RKI guideline are also given in Tables 1 and 2 below.

The following enzymes were used:

1. variant F49 of the protease from Bacillus lentus according to WO 95/23221

2. Everlase® 16 LEX (Novozymes A / S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark)

3. Alcalase® 2.5L (Novozymes A / S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark)

4. Stainzyme® 12.0 L (Novozymes A / S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark)

5. Ecostone® N400 (AB Enzymes GmbH, Feldbergstrasse 78, 64293 Darmstadt, Germany)

6. Carezyme® 4500L (Novozymes A / S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark)

7. Mannaway® 4.0T (Novozymes A / S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark)

8. Lipolase® 100 L (Novozymes A / S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark)

The results are shown in Tables 1 and 2 below as RF values. Duplicate determinations are separated by slashes. It is clear that the hydrolytic enzymes, especially after 30 minutes incubation period have a significant virus activity against the indicated virus (indicated by RF values greater than or equal to one, in particular RF values greater than two or even greater than three). Thus, hydrolytic enzymes can be used virus-effectively in the context of inventive method for the disinfection of textiles and / or hard surfaces. Table 1 :

Table 2:

Claims

claims

1. A method for disinfecting textiles and / or hard surfaces, characterized in that the textile and / or the hard surface is brought into contact with a virucidal treatment solution comprising at least one hydrolytic enzyme.

2. The method according to claim 1, characterized in that the hydrolytic enzyme in the virucidal treatment solution in a concentration of 0.000005-0.1 g of dry enzyme per 100 g of treatment solution, and more preferably of 0.0005-0.1 g of dry enzyme per 100 g of treatment solution and 0.005-0.05 g dry enzyme per 100 g treatment solution.

3. The method according to claim 1 or 2, characterized in that the virucidal treatment solution further comprises at least one further disinfecting ingredient.

4. The method according to any one of claims 1 to 3, characterized in that the virucidal treatment solution further comprises a surfactant preparation, in particular a diluted or undiluted washing, cleaning, Textilvor- or post-treatment agent or disinfectant.

5. The method according to claim 4, characterized in that the surfactant preparation further comprises at least one further ingredient, preferably one selected from the group consisting of surfactant, builder, peroxygen compound, bleach activator, alcohol, acid, grayness inhibitor, optical brightener, foam inhibitor, water-soluble salt, polymeric thickener, volatile alkali and / or base, hydrophilizing agent and combinations thereof.

6. The method according to any one of claims 1 to 5, characterized in that the hydrolytic enzyme has a viral activity against a virus selected from the group consisting of Adenoviridae, Alphaherpesvirinae, Astroviridae, Betaherpesvirinae, Birnaviridae, Bornaviridae, Bunyaviridae, Caliciviridae, Chordopoxviridae , Filoviridae, Flaviviridae, Gammaherpesvirinae, Hepadnaviridae, Herpesviridae, Iridoviridae, Orthomyxoviridae, Orthoretroviridae, Papillomaviridae, Paramyxovirinae, Parvovirinae, Picornaviridae, Pneumovirinae, Polyomaviridae, Reoviridae, Rhabdoviridae, Roniviridae, Spumaretroviridae and Togaviridae.

7. The method according to any one of claims 1 to 6, characterized in that it takes place in a temperature range between 1O ⁰ C and 6O ⁰ C, in particular between 1O ⁰ C and 5O ⁰ C and particularly preferably between 1O ⁰ C and 4O ⁰ C.

8. The method according to any one of claims 1 to 7, characterized in that the virucidal treatment solution for at least 10 seconds, and more preferably for at least 15, 20, 25 and 30 seconds in contact with the textile or the hard surface.

9. The method according to any one of claims 1 to 8, characterized in that the hydrolytic enzyme or the virucidal treatment solution containing the hydrolytic enzyme has an RF value greater than one, determined according to the DVV / RKI guideline.

10. The method according to any one of claims 1 to 9, characterized in that the hydrolytic enzyme is a protease, amylase, cellulase, glycosidase, hemicellulase, mannanase, xylanase, pectinase, ß-glucosidase, carrageenase or a lipase or a mixture containing at least two of these enzymes, in particular a protease, preferably a serine protease, more preferably a subtilase and most preferably a subtilisin.

11. A process for the preparation of a virucidal treatment solution for the disinfection of textiles and / or hard surfaces, characterized in that the treatment solution at least one hydrolytic enzyme is added.