CN116057158A - Use of enzymes and surfactants for inhibiting microorganisms - Google Patents

Abstract

The present invention relates to the use of enzymes and surfactants in detergent compositions for the inhibition of microorganisms. The invention relates in particular to the use of enzymes and surfactants in detergent compositions for antiviral activity. While detergent compositions having pH typically in the range of 8 to 13 are known to impart detergency benefits, they are not known to impart antimicrobial, in particular antibacterial and viral inactivation benefits. It is therefore an object of the present invention to achieve inactivation of microorganisms, in particular viruses, from articles of manufacture using detergent compositions having a pH of 8 to 13 in laundry processes. We have now found the use of a combination of an alkylbenzene sulfonate surfactant, a hydrolase and an alkali source in a detergent composition having a pH of from 8 to 13 for inactivating microorganisms on textiles. In particular for the inactivation of bacteria and viruses.

Description

Use of enzymes and surfactants for inhibiting microorganisms

Technical Field

The present invention relates to the use of enzymes and surfactants in detergent compositions for the inhibition of microorganisms. The invention relates in particular to the use of enzymes and surfactants in detergent compositions for antiviral activity.

Background

Human health is affected by a wide variety of microorganisms encountered every day. Viruses and bacteria cause a wide variety of diseases and afflictions.

Disinfection or sterilization of skin and inanimate surfaces is a very important aspect of ensuring health. Important areas of ensuring sterilization include personal use such as hand and body hygiene, and hygiene of hard surfaces such as door handles and soft surfaces such as clothing.

Bacteria, viruses and protozoa are three common microorganisms known to cause diseases in humans and other mammals. Cleaning the skin and other living and inanimate surfaces to reduce microbial populations is the first defense to clear these pathogens and minimize the risk of infection. There are compositions that can be used to disinfect for each of these types of organisms. Although many antimicrobial actives and compositions are available and widely used, killing viruses is more difficult and often requires more harsh chemicals such as chlorine or alcohols.

Viruses are a major concern of a class of pathogens, and viral infection is one of the largest causes of human morbidity. Viral infections of the respiratory tract are commonly transmitted from person to person by direct contact with virus-contaminated respiratory secretions. Typically, such contact is in the form of viral particles that are in physical contact with the contaminated surface or that are transmitted by inhalation air. After initial contamination, the virus can survive for several hours on the environmental surface and if the newly contaminated finger is subsequently used to rub the eye or contact the nasal mucosa, the infection is easily transmitted through finger-finger contact and through contaminated environmental surface-finger contact. Thus, minimizing viral contamination of skin and environmental surfaces (including inanimate and animate surfaces) has proven to be effective in reducing the risk of transmitting infections to the general population.

Viruses propagate only within living cells. The main obstacle encountered by viruses is to obtain cell entry, the cells being protected by cell membranes of a thickness comparable to the size of the virus. In order to penetrate cells, the virus must first adhere to the cell surface. Thus, in order to control viral infection, it is important to quickly kill viruses that contact the skin and desirably provide durable antiviral activity on the skin or inanimate surface to control viral infection.

For example, rhinoviruses, influenza viruses, coronaviruses and adenoviruses are known to cause respiratory tract infections. Coronaviruses primarily infect the respiratory and gastrointestinal tracts of mammals and birds. Coronaviruses are enveloped viruses with a positive-sense single-stranded RNA genome and a helically symmetric nucleocapsid. Coronavirus infection begins with the attachment of spike proteins to their cognate cellular receptors. It is desirable to find new methods capable of inactivating viruses, in particular coronaviruses.

Viral control poses a more difficult problem than bacterial control. By sufficiently reducing the bacterial population, the risk of bacterial infection is reduced to acceptable levels. Thus, it is desirable to kill bacteria quickly. However, for viruses, not only quick killing but also durable antiviral activity is required. This difference is because merely reducing the viral population is not sufficient to reduce infection. In theory, a single virus may cause an infection. Thus, for an effective antiviral cleansing composition, substantially all and long lasting antiviral activity is needed or at least desired.

EP1065265B1 (Kao Corporation) discloses a biocidal detergent composition having a pH of 6.5 to 7.5 and comprising a protease.

WO2010/069812A2 (Henkel) discloses a method for disinfecting textiles and/or hard surfaces by contact with a virucidal treatment solution having at least one hydrolase enzyme.

While detergent compositions having pH typically in the range of 8 to 13 are known to impart a detersive benefit, they are not known to impart antimicrobial, in particular antibacterial and viral inactivation benefits.

It is therefore an object of the present invention to achieve the inactivation of microorganisms, in particular viruses, of articles of manufacture using detergent compositions having a pH of 10 to 13 during laundry.

It is a further object that the composition does not contain caustic chemicals that cause undesirable effects that can be considered harmful to the consumer.

Disclosure of Invention

We have now found the use of a combination of an alkylbenzene sulfonate surfactant, a hydrolase and an alkali source in a detergent composition having a pH of from 8 to 13 for inactivating microorganisms on textiles. In particular for the inactivation of bacteria and viruses.

In a first aspect, the present invention relates to the use of a combination of an alkylbenzene sulfonate surfactant, a hydrolase enzyme and an alkali source in a solid detergent composition having a pH of 10 to 13 (as measured at 25 ℃ and at a 10% aqueous solution concentration in deionized water) for inactivating microorganisms on textiles during laundering, wherein the hydrolase enzyme is selected from the group consisting of proteases, lipases, cellulases, amylases, mannanases, or combinations thereof.

In a second aspect, the present invention provides a method of inactivating microorganisms from a textile, the method comprising the steps of:

i) Contacting a surface to be washed with an aqueous solution of a solid detergent composition of the first aspect;

ii) the surface to be washed is kept in intimate contact with the aqueous solution for at least 30 minutes, and preferably also for at least 60 minutes; the method comprises the steps of,

iii) Optionally rinsing the surface with water.

As used herein, the term "solid detergent composition" includes granular, powder, tablet set or bar compositions. Preferably, the composition is a solid laundry detergent composition.

Detailed Description

All percentages mentioned herein are by weight based on the total composition, unless otherwise indicated. The abbreviation "wt%" is understood to mean weight% of the total composition.

Alkylbenzene sulfonate surfactant

According to a first aspect of the present invention there is provided the use of an alkylbenzene sulfonate surfactant in a detergent composition.

Linear alkylbenzene sulfonates or LAS are linear alkylbenzenes that have been sulfonated to include acidic sulfonic acid groups attached to the benzene ring to form the parent acid (linear alkylbenzene sulfonic acid). The linear alkylbenzene sulfonic acid is neutralized using any one of an alkali metal hydroxide, alkaline earth metal hydroxide, ammonium hydroxide, alkylammonium hydroxide, alkanolamine, or any chemical agent known to those skilled in the art to form a water soluble linear alkylbenzene sulfonate.

The composition comprises an alkylbenzenesulfonate, preferably a linear or branched, substituted or unsubstituted C ₈ To C ₂₄ Alkylbenzene sulfonate. C (C) ₈ To C ₂₄ The alkylbenzene sulfonate may be a modified alkylbenzene sulfonate (MLAS) as described in more detail in WO99/05243, WO99/05242, WO99/05244, WO99/05082, WO99/05084, WO99/05241, WO99/07656, WO00/23549 and WO 00/23548. Highly preferred C ₈ To C ₂₄ Alkylbenzene sulfonate is straight chain C ₁₀ To C ₁₆ Alkylbenzene sulfonate. Particularly preferred are straight chain C ₁₀ To C ₁₃ Alkylbenzene sulfonates, which are obtainable by, preferably, sulfonating commercially available Linear Alkylbenzenes (LABs); suitable LABs include lower 2-phenyl LABs, such as those sold under the trade name Sasol

Those provided or under the trade name +.>

Other suitable LABs include higher 2-phenyl LABs, such as those provided by Sasol under the trade name +.>

Those provided. Preferably, the composition comprises alkylbenzene sulfonate, wherein the alkylbenzene sulfonate comprises at least 25% by weight of the 2-phenyl isomer. Suitable alkylbenzene sulfonates having this feature are obtained by DETAL synthesis.

Examples of suitable synthetic anionic detergent compounds are sodium and potassium salts, in particular those obtained by sulfation of alcohols (e.g. produced from tallow or coconut oil), alkyl C ₁₀ To C ₂₀ Sodium and potassium benzenesulfonates, in particular linear secondary alkyl C ₁₀ To C ₁₅ Sodium benzenesulfonate; is C ₁₁ To C ₁₅ Sodium alkylbenzenesulfonate.

Preferably, the detergent composition according to the present invention comprises from 2 wt% to 40 wt% of alkylbenzene sulfonate surfactant. Preferably, the detergent composition comprises at least 6 wt%, still preferably at least 7 wt%, still preferably at least 8 wt%, most preferably at least 10 wt% alkylbenzene sulfonate surfactant, based on the weight of the detergent composition, but typically no more than 35 wt%, still preferably no more than 30 wt%, more preferably no more than 25 wt%, most preferably no more than 15 wt% alkylbenzene sulfonate surfactant in the detergent composition.

Preferably, the use according to the first aspect of the invention relates to the inactivation of microorganisms in a wash liquor prepared by adding a solid detergent composition to water, wherein the alkylbenzene sulfonate surfactant is present in a concentration of 40ppm to 2000 ppm. Preferably, the concentration in the wash liquor is at least 50ppm, still preferably at least 100ppm, still preferably at least 200ppm, most preferably at least 250ppm, but generally not more than 1600ppm, still preferably not more than 1000ppm, more preferably not more than 800ppm, most preferably not more than 600ppm.

Hydrolytic enzyme

According to a first aspect, the present invention discloses the use of a hydrolase enzyme in inactivating microorganisms in a detergent composition for treating textiles.

Hydrolytic enzymes are hydrolytic enzymes that hydrolyse esters, ethers, peptides, glycosides, anhydrides or C-C bonds in a reversible reaction. Hydrolytic enzymes catalyze the hydrolytic cleavage of substances.

The hydrolase is selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof. Preferred additional enzymes for use in the present invention include, but are not limited to, glycosidases, hemicellulases, xylanases, pectinases, glucosidase, carrageenases, or combinations thereof. Preferably, the enzyme is a protease.

The hydrolase enzyme is preferably present in the solid detergent compositions of the present invention at a level of from 0.0001 to about 1%, more preferably from about 0.001 to about 0.5%, especially from about 0.005 to about 0.6%, of active hydrolase enzyme.

Preferably, the washing liquid prepared by diluting the solid detergent composition according to the present invention in water contains 0.0001ppm to 30ppm of pure hydrolase, and still preferably 0.0001ppm to 20ppm of pure hydrolase. Preferably, the detergent composition comprises at least 0.0005ppm, still preferably at least 0.001ppm, still preferably at least 0.002ppm, most preferably at least 0.005ppm, still more preferably 0.4ppm, but generally no more than 22ppm, preferably no more than 20ppm, still preferably no more than 15ppm, most preferably no more than 10ppm.

Protease:

preferably, the hydrolase is a protease. Preferably, the protease is an alkaline protease, preferably a serine protease.

Suitable proteases include proteases of bacterial, fungal, plant, viral or animal origin, preferably proteases of plant or microbial origin. Microbial sources are preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. Serine proteases may be, for example, of the S1 family, such as trypsin, or of the S8 family, such as subtilisin. For example, the metalloprotease protease may be a thermolysin from, for example, family M4 or other metalloprotease such as those from the M5, M7 or M8 families.

Serine proteases are a subgroup of carbonyl hydrolases comprising diverse enzyme classes with broad specificity and biological function. The term "subtilase" refers to the serine protease subgroup according to Siezen et al 1991,Protein Engng.4:719-737 and Siezen et al 1997,Protein Science 6:501-523. Serine proteases are a subset of proteases characterized by serine in the active site forming a covalent adduct with a substrate. Subtilases can be divided into 6 sub-parts, namely the subtilisin family, the thermophilic proteinase family, the proteinase K family, the lanthiobacterial peptidase family, the Kexin family and the Pyrolysin family.

Examples of subtilases are those derived from Bacillus lentus (Bacillus lentus), bacillus alkalophilus, bacillus subtilis, bacillus amyloliquefaciens, bacillus pumilus and Bacillus gibsonii as described in US7,262,042 and WO2009/021867, and the subtilisins lens, subtilisin Novo, subtilisin Carlsberg, bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 and the proteases PD138 as described in WO 93/18140. Other useful proteases may be those described in WO92/175177, WO01/16285, WO02/026024, US8753861B2 and WO 02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium proteases described in WO89/06270, WO94/25583 and WO2005/040372, and chymotrypsin from Cellulomonas (Cellulomonas) described in WO2005/052161 and WO 2005/052146.

Further preferred proteases are alkaline proteases from Bacillus lentus DSM 5483 as described, for example, in WO95/23221, and variants thereof as described in WO92/21760, WO95/23221, EP1921147 and EP 1921148.

Examples of metalloproteases are neutral metalloproteases as described in WO2007/044993 (Genencor int.) such as those derived from bacillus amyloliquefaciens.

Examples of useful proteases are variants described in the following documents: WO92/19729, WO96/034946, WO98/20115, WO98/20116, WO 99/01768, WO01/44452, WO03/006602, WO2004/03186, WO 2004/04979, WO2007/006305, WO2011/036263, WO2011/036264, in particular variants having substitutions at one or more of the following positions: 3. 4, 9, 15, 27, 36, 57, 68, 76, 87, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252, and 274, using BPN' numbering. More preferably, the subtilase variant may comprise the following mutations: s3 49 15R, 36 68 76 87S, R, 97 98G, 99G, D, 99AD, S101G, M, 103 104I, Y, 106V, 120D, 123 128 129 130 160 167 170 194 199 217 218 222 232 235 236 245 274A (using BPN' numbering).

Suitable commercially available proteases include those under the trade name Alcalase ^TM 、Duralase ^TM 、Durazym ^TM 、Relase ^TM 、Relase ^TM Ultra、Savinase ^TM 、Savinase ^TM Ultra、Primase ^TM 、Polarzyme ^TM 、Kannase ^TM 、Liquanase ^TM 、Liquanase ^TM Ultra、Ovozyme ^TM 、Coronase ^TM 、Coronase ^TM Ultra、Neutrase ^TM 、Everlase ^TM And Esperase ^TM Those sold under the trade name Maxatase by NovozymeA/S ^TM 、Maxaca ^TM 、Maxapem ^TM 、Purafect ^TM 、Purafect Prime ^TM 、Preferenz ^TM 、Purafect MA ^TM 、Purafect Ox ^TM 、Purafect OxP ^TM 、Puramax ^TM 、Properase ^TM 、Effectenz ^TM 、FN2 ^TM 、FN3 ^TM 、FN4 ^TM 、Excellase ^TM 、Opticlean ^TM And Optimase ^TM Those sold by Danisco/DuPont Axamem ^TM (Gist-brocas N.V.), BLAP (sequence shown in FIG. 29 of US 5352604) and variants thereof (Henkel AG) and variants thereof fromKAP { alcaligenes bacillus subtilis protease of Kao).

Lipase:

lipases are enzymes that catalyze the hydrolysis of ester bonds of edible fats and oils (i.e., triglycerides) to free fatty acids, mono-and diglycerides, and glycerol.

Clean lipases are discussed in Jan H.Van Ee, onno Misset and Erik J.Baas edited Enzymes in Detergency (1997Marcel Dekker,New York). The lipase may be selected from lipases in e.c. class 3.1, 3.2 or combinations thereof.

Preferably, the cleaning lipase selected is triacylglycerol lipase (e.c. 3.1.1.3). Suitable triacylglycerol lipases may be selected from variants of Humicola lanuginosa (Humicola lanuginose) (Thermomyces lanuginosus) lipase. Other suitable triacylglycerol lipases may be selected from variants of Pseudomonas lipases, for example from Pseudomonas alcaligenes or Pseudomonas alcaligenes (EP 218272), pseudomonas cepacia (EP 331376), pseudomonas stutzeri (GB 1,372,034), pseudomonas fluorescens, pseudomonas SD705 strain (WO 95/06720 and WO 96/27002), pseudomonas Wisconsin 25 (WO 96/12012), bacillus lipases, for example from Bacillus subtilis (Dartois et al (1993), biochemica et Biophysica Acta,1131, 253-360), bacillus stearothermophilus (JP 64/744992) or Bacillus pumilus (WO 91/16422).

Other examples of EC 3.1.1.3 lipases include those described in WIPO publications WO00/60063, WO99/42566, WO02/062973, WO97/04078, WO97/04079 and U.S. Pat. No. 5,869,438. Preferred lipases are produced by Absidia reflexa (Absidia reflexa), absidia umbrella (Absidia corymbefera), rhizomucor miehei (rhizmucor miehei), rhizopus deleman (Aspergillus niger), aspergillus tubingensis (Aspergillus tubigensis), fusarium oxysporum (Fusarium oxysporum), fusarium heterosporum (Fusarium heterosporum), aspergillus oryzae (Aspergillus oryzea), kanji Bai Qingmei (Penicillium carmichaeli), aspergillus foetidus (Aspergillus foetidus), aspergillus niger, thermomyces lanuginosus (Thermomyces lanoginosus) (synonym: humicola lanuginosa (Humicola lanuginosa)) and Landerina penisapora, in particular Thermomyces lanuginosus.

Certain preferred lipases are provided by Novozymes and include those under the trade name

Lipolase

And->

(registered trade name of Novozymes) and LIPASE P +.>

Areario Pharmaceutical Co.Ltd. From Japanese famous ancient house under the trade name AMANO-/for the first time>

Those purchased from Toyo Jozo co. Of the japanese famous old house; and other Chromobacter viscosum lipases from Amersham Pharmacia biotech. And Diosynth co. Of the netherlands, new jersey, piscataway, usa, and other lipases, such as pseudomonas gladiolus (Pseudomonas gladioli).

Further examples are lipase variants, such as those described in EP407225, WO92/05249, WO94/01541, WO94/25578, WO95/14783, WO95/30744, WO95/35381, WO95/22615, WO96/00292, WO97/04079, WO97/07202, WO00/34450, WO00/60063, WO01/92502, WO07/87508 and WO 09/109500.

Preferred commercial lipase products include Lipolase ^TM 、Lipex ^TM ；Lipolex ^TM And lipoclear ^TM (Novozymes A/S)，Lumafast ^TM (originally from Genencor) and Lipomax ^TM (originally from Gist-broades).

Is particularly preferred, but +.>

100TB is further particularly preferred.

Other useful lipases are described in WIPO publications WO02062973, WO2004/101759, WO2004/101760 and WO 2004/101763. In one embodiment, suitable lipases include the "first cycle lipase" described in WO00/60063 and U.S. Pat. No. 6,939,702B1, preferably variants of SEQ ID No.2, more preferably variants of SEQ ID No.2 comprising substitution of an electrically neutral or negatively charged amino acid with R or K at any position of 3, 224, 229, 231 and 233, most preferably variants of SEQ ID No.2 having at least 90% homology to SEQ ID No.2, the most preferred variants comprising T231R and N233R mutations, such most preferred variants being under the trade name of

(Novozymes) sales.

The above lipases may be used in combination (any lipase mixture may be used). Suitable lipases are available from Novozymes of eryngii; areario Pharmaceutical co.ltd. of the japanese famous ancient house; toyo Jozo co., tagata, japan; amersham Pharmacia biotech of piscataway, new jersey, usa; diosynth co. Of austs, netherlands, and/or prepared according to the examples contained herein.

As described in WO2007/087243, lipases with reduced odor production potential and good relative properties are particularly preferred. These include

(Novozyme)。

Amylase:

suitable amylases include alpha-amylase and/or glucoamylase, and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. For example, amylases include alpha amylases obtained from a particular strain of bacillus (e.g., bacillus licheniformis (Bacillus licheniformis), described in more detail in GB1,296,839).

Suitable amylases include those having SEQ ID NO. 2 of WO95/10603 or variants thereof having 90% sequence identity to SEQ ID NO. 3. Preferred variants are described in SEQ ID NO. 4 of WO94/02597, WO94/18314, WO97/43424 and WO99/019467, for example variants having substitutions at one or more of the following positions: 15. 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.

Suitable amylases include those having SEQ ID NO. 6 of WO02/010355 or variants thereof having 90% sequence identity to SEQ ID NO. 6. Preferred variants of SEQ ID NO. 6 are those having a deletion at positions 181 and 182 and a substitution at position 193. Other suitable amylases are hybrid alpha-amylases comprising residues 1-33 of the Bacillus amyloliquefaciens-derived alpha-amylase shown in SEQ ID NO. 6 of WO2006/066594 and residues 36-483 of the Bacillus licheniformis alpha-amylase shown in SEQ ID NO. 4 of WO2006/066594, or variants thereof having 90% sequence identity thereto. Preferred variants of the hybrid alpha-amylase are those having substitutions, deletions or insertions in one or more of the following positions: g48, T49, G107, H156, a181, N190, M197, I201, a209, and Q264. The most preferred variants of hybrid alpha-amylases comprising residues 1-33 of the alpha-amylase from Bacillus amyloliquefaciens shown in SEQ ID NO. 6 and residues 36-483 of SEQ ID NO. 4 of WO2006/066594 are those with the following substitutions:

M197T; h156y+a181t+n190f+a209v+q264S; or g48a+t49 i+g600a+h156 y+a181 t+n190f+i180f+a209 v+q264S.

Other suitable amylases are those having SEQ ID NO. 6 of WO99/019467 or variants thereof having 90% sequence identity to SEQ ID NO. 6. Preferred variants of SEQ ID NO. 6 are those having substitutions, deletions or insertions in one or more of the following positions: r181, G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletions in the R181 and G182 or H183 and G184 positions.

Other amylases which may be used are those having SEQ ID NO. 1, SEQ ID NO. 3, SEQ ID NO. 2 or SEQ ID NO. 7 of WO96/023873 or variants thereof having 90% sequence identity with SEQ ID NO. 1, SEQ ID NO. 2, SEQ ID NO. 3 or SEQ ID NO. 7. Preferred variants of SEQ ID NO. 1, SEQ ID NO. 2, SEQ ID NO. 3 or SEQ ID NO. 7 are those having substitutions, deletions or insertions in one or more of the following positions: 140. 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476 are numbered using SEQ ID NO:2 of WO 96/023873. More preferred variants are those having deletions in two positions selected from 181, 182, 183 and 184, such as 181 and 182, 182 and 183, or 183 and 184 positions. The most preferred amylase variants of SEQ ID NO. 1, SEQ ID NO. 2 or SEQ ID NO. 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.

Other amylases which may be used are those having SEQ ID NO. 2 of WO08/153815, SEQ ID NO. 10 of WO01/66712 or variants thereof having 90% sequence identity to SEQ ID NO. 2 of WO08/153815 or 90% sequence identity to SEQ ID NO. 10 of WO 01/66712. Preferred variants of SEQ ID NO. 10 of WO01/66712 are variants having substitutions, deletions or insertions in one or more of the following positions: 176. 177, 178, 179, 190, 201, 207, 211 and 264.

Other examples are amylase variants such as those described in WO2011/098531, WO2013/001078 and WO 2013/001087.

A commercially available amylase is Duramyl ^TM 、Termamyl ^TM 、Fungamyl ^TM 、Stainzyme ^TM 、Stainzyme Plus ^TM 、Natalase ^TM 、Liquozyme X ^TM And BAN ^TM (from Novozymes AS) and Rapid ^TM 、Purastar ^TM /Effectenz ^TM 、Powerase ^TM 、Preferenz S1000 ^TM 、Preferenz S100 ^TM And Preferenz S110 ^TM (from Genencor International inc./DuPont).

Lyase:

the lyase may be a pectate lyase derived from Bacillus, in particular Bacillus licheniformis or Bacillus mucilaginosus (Bacillus agaradhaerens), or a variant derived from any of these, e.g.as described in US6124127, WO99/27083, WO99/27084, WO02/006442, WO02/092741, WO03/095638, the commercially available pectate lyase being XPect ^TM ；Pectawash ^TM And Pectaway ^TM (NovozymesA/S)。

Mannanase:

Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be a basic mannanase of family 5 or 26. It may be a wild type from bacillus or humicola, in particular bacillus mucilaginosus, bacillus licheniformis, bacillus halodurans (b), bacillus clausii or humicola insolens (h.insolens). Suitable mannanases are described in WO 1999/064619. The commercially available mannanase is Mannaway ^TM (NovozymesA/S)。

Cellulase:

suitable cellulases include cellulases of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, pseudomonas, humicola, fusarium, thielavia, acremonium, e.g., fungal cellulases produced by Humicola insolens, thielavia, myceliophthora thermophila and Fusarium oxysporum as disclosed in U.S. Pat. No. 4,435,307, U.S. Pat. No. 5,648,263, U.S. Pat. No. 5,691,178, U.S. Pat. No. 5,776,757, WO89/09259, WO96/029397 and WO 98/0123307.

Commercially available cellulases include Celluzyme ^TM 、Carezyme ^TM 、Celluclean ^TM 、Endolase ^TM 、Renozyme ^TM (Novozymes A/S)、Clazinase ^TM And Puradax HA ^TM (Genencor International Inc.) and KAC-500 (B) ^TM (Kao Corporation)。

Preferably, the use according to the first aspect of the invention is substantially free of hydrolases selected from the group consisting of deoxyribonucleases, hexosaminidases or combinations thereof. The term "substantially free" means that there is no intentionally added deoxyribonuclease and/or aminohexosaminidase hydrolase in the composition, preferably in an amount of 0% by weight. It is highly preferred that all hydrolases are detersive hydrolases.

Alkali source

According to a first aspect, the present invention discloses the use of an alkaline source in a detergent composition for treating textiles to inactivate microorganisms.

Examples of the alkali source include, but are not limited to, alkali metal or alkaline earth metal salts of carbonic acid, dicarbonic acid, silicic acid, metasilicic acid, or combinations thereof.

In a preferred embodiment, the source of alkalinity is a carbonate. Examples of preferred carbonates are alkaline earth and alkali metal carbonates, including sodium carbonate, sodium bicarbonate and sodium sesquicarbonate or mixtures thereof.

The carbonates and bicarbonates preferably have an amorphous structure. Preferably, the carbonates and bicarbonates are coated with a coating material. The particles of carbonate and bicarbonate can have an average particle size of 250 microns or more, preferably 500 microns or more.

Preferably, the alkali metal and/or alkaline earth metal carbonate is present in the detergent composition of the invention in an amount in the range of 10 wt% to 35 wt%. The term carbonate includes bicarbonate and sesquicarbonate.

Preferably, the detergent composition according to the present invention comprises from 10 wt% to 40 wt% of a carbonate salt source. Preferably, the detergent composition comprises at least 12 wt%, still preferably at least 15 wt%, still preferably at least 18 wt%, most preferably at least 20 wt% of the carbonate salt source, based on the weight of the detergent composition, but typically no more than 35 wt%, still preferably no more than 30 wt%, more preferably no more than 25 wt% of the carbonate salt source in the solid detergent composition.

The alkaline system may include other components, such as silicates. Preferably, the silicate is present in the detergent composition in an amount in the range of from 1 wt% to 10 wt%.

Suitable silicates include SiO with 1.0-2.8 ₂ :Na ₂ O ratio, preferably 1.6-2.0, most preferably 2.0. The silicate may be in the form of an anhydrous salt or a hydrated salt. SiO with 2.0 ₂ :Na ₂ Sodium silicate in the O ratio is the most preferred silicate. Preferably the silicate has an amorphous structure. Alkali metal persilicates or metasilicates are also suitable silicate sources herein.

Preferred crystalline layered silicates for use herein have the general formula namsixo2χ+l.yh2o, wherein M is sodium or hydrogen, x is a number from 1.9 to 4 and y is a number from 0 to 20. Crystalline layered sodium silicate of this type is disclosed in EP-A-0164514 and processes for their preparation are disclosed in DE-A-3417649 and DE-A-3742043. Here, x in the above formula preferably has a value of 2, 3 or 4, and preferably 2. The most preferred material is delta-Na available as NaSKS-6 from Hoechst AG ₂ Si ₂ O ₅ 。

Preferably, the detergent composition according to the present invention comprises 10 to 40 wt% of the alkalinity source. Preferably, the detergent composition comprises at least 12 wt%, still preferably at least 15 wt%, still preferably at least 18 wt%, most preferably at least 20 wt% of the alkalinity source, based on the weight of the detergent composition, but typically no more than 35 wt%, still preferably no more than 30 wt%, more preferably no more than 25 wt% of the alkalinity source in the detergent composition.

Preferably, the use according to the first aspect of the invention relates to the inactivation of microorganisms in a wash liquor prepared by adding a solid detergent composition to water, wherein the alkali source is present at a concentration of 120ppm to 2500 ppm. Preferably, the concentration in the wash liquor is at least 150ppm, still preferably at least 200ppm, still preferably at least 500ppm, most preferably at least 600ppm, but generally not more than 1800ppm, still preferably not more than 1600ppm, more preferably not more than 1500ppm and most preferably not more than 1000ppm. Preferably, the alkali source is selected from sodium carbonate, sodium silicate or a combination of sodium carbonate and sodium silicate.

Detergent composition

The combination of alkylbenzene sulfonate surfactant, hydrolase selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof, and an alkalinity source according to the invention may be used in any suitable detergent composition having a pH of 10 to 13.

Preferably, the pH of the composition is from 10.2 to 13, still preferably from 10.5 to 13, still preferably from 10.2 to 12, more preferably from 10.2 to 11, still more preferably from 10.2 to 11, most preferably from 10.5 to about 11, as measured at 25 ℃ and at a concentration of 10% aqueous solution in deionized water. The pH of the composition may be adjusted using pH adjusting ingredients known in the art.

The detergent composition must be suitable for use on soft surfaces, preferably textiles.

The detergent composition may be in any form, such as solid, granular, powder, or unit dose product form, wherein the solid detergent composition is at least partially enclosed in a water-soluble film.

The solid detergent composition in particulate form may comprise agglomerates, spray dried powders, extrudates, flakes, needles, noodles, beads or any combination thereof. The composition may be in the form of compacted granules, such as tablets or bars. The composition may be in some other unit dosage form, such as a pouch; typically at least partially, and preferably substantially completely, surrounded by a water-soluble film such as polyvinyl alcohol. Preferably, the composition is in the form of free-flowing particles; free-flowing particulate form generally means that the composition is in the form of discrete particles that are independent. The solid composition may be prepared by any suitable method including agglomeration, spray drying, extrusion, mixing, dry blending, liquid spraying, roller compaction, spheronization, tabletting, or any combination thereof.

The solid detergent composition typically has a bulk density of 450g/l to 1,000g/l, the preferred low bulk density detergent composition has a bulk density of 550g/l to 650g/l, and the preferred high bulk density detergent composition has a bulk density of 750g/l to 900 g/l. During the laundry process, the composition is typically contacted with water to obtain a wash liquor having a pH of from 8 to 13, preferably from 8.5 to less than 11.

The compositions may be used only to deliver alkylbenzene sulfonate surfactant/hydrolase and alkali source during the laundry process, or they may have additional functions such as cleaning.

Inactivation of microorganisms

The present invention discloses in a first aspect the use of a combination of an alkylbenzene sulfonate, a hydrolase selected from the group consisting of a protease, a lipase, a cellulase, an amylase, a mannanase or a combination thereof, and an alkaline source in a solid detergent composition for inactivating microorganisms on a textile surface during laundering, said solid detergent composition having a pH of 10 to 13 as measured at 25 ℃ and at a 10% aqueous solution concentration in deionized water.

The term inactivation is understood in the context of the present invention as an activity against at least one virus (antiviral effect) or bacterial species.

Antiviral effect is understood to mean any reduction in viral titer and associated infectivity of the virus, infectivity being the ability of the virus to infect a host. Thus, an antiviral effect is advantageously achieved by disrupting one or more viruses, in particular in terms of adhesion to the host cell and/or the ability to introduce and/or replicate genetic material in the host cell.

Antimicrobial activity is assessed as a log reduction, or alternatively a percent reduction, of the population of microorganisms provided by the antimicrobial composition. For a particular contact time, it is typically 15 seconds to 5 minutes, more preferably the contact time is 15 seconds to at least 1 hour, preferably 1 to 3log reduction, most preferably 3 to 5log reduction, and most preferably less than 1log reduction. Thus, highly preferred antimicrobial compositions exhibit 3 to 5log reductions for a broad spectrum of microorganisms over short contact times.

Preferably, the use according to the first aspect of the invention provides a log1 to log 5, and still preferably a log 2 to log 5, viral reduction. Preferably, the use according to the invention provides a reduction in viral titer of at least 50%, also preferably at least 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99% and especially preferably about 99.999% (corresponding to at least 5log10 levels). Preferably, the contact time with the aqueous liquid of the detergent composition according to the first aspect is from at least 30 minutes to at least 2 hours, preferably at least 1 hour.

Viruses (singular: a virus) are meant to be intracellular but not cellular parasites that can infect biological cells. Viruses contain at least one genetic program (genetic material) in the form of nucleic acids (deoxyribonucleic acids (DNA) or ribonucleic acids (RNA)) and optionally other accessory components for their proliferation and transmission. Viruses may be enveloped or non-enveloped.

The use according to the first aspect provides for the inactivation of a virus which may be selected from the group consisting of adenoviridae, alphaherpesviridae, astroviridae, herpesviridae, bisrnaviridae, vitroneviridae, bunyaviridae, caliciviridae, vertebrate poxviridae (chord), gordopoxoviridae, chordopoxviridae, vertebrate poxviridae (chord), hepadnaviridae, herpesviridae, iridoviridae, orthomyxoviridae, orthoretroviridae, papillomaviridae, paramyxoviridae, parvoviridae, picornaviridae, pneumoviridae, polyomaviridae, reoviridae, togiviridae, coronaviridae and ronivireridae.

This includes, inter alia, viruses belonging to one of the following genera: alpha papilloma, alpha retrovirus, alpha virus, aphthovirus, aquatic double RNA virus, aquatic animal reovirus, adenovirus, avian double RNA virus, avian paramyxovirus, beta papilloma virus, beta retrovirus, bocka virus, boernavirus, cardovirus, colivirus delta virus, dependent virus, ebola virus, enterovirus, transient heat virus, epsilon retrovirus, equine rhinovirus, red virus, fijivirus, flavivirus, mycoprion, gamma papilloma virus, gamma retrovirus, hantavirus, henipavirus, hepacivalirus Virus influenza c, iris, ke Bu, lentivirus, lymphocryptovirus, rabies, mammalian astrovirus, marburg, mammalian adenovirus, megaly, measles, mupaplloviridae, murine cytomegalovirus, fungal reovirus, inner rovirus, norovirus, coronavirus, murine norovirus, bovine coronavirus, novirhabapunovirus, novirhabapvirus, orthoreovirus, paddy, paramylovirus, parvovirus, pestivirus, sand fly virus, plant reovirus, pneumovirus, polyomavirus, respiratory tract virus, simian virus, rhinovirus, and roseola.

The use according to the invention comprises applying the solid detergent composition in liquid diluted form, preferably diluted with water, to a textile to be laundered, to form a wash liquor. The use according to the first aspect of the present invention provides for the inactivation of microorganisms on a textile, which may be a hard surface or a textile surface. Textiles include all types of fabrics, including different compositions, for example, made from cotton, wool, silk, other natural fibers, polyester, and blends of all types. The preferred textile is laundry. This includes all washable textiles. The textile may be woven or nonwoven.

Additional surfactant

In addition to the alkylbenzene sulfonate surfactant, the detergent composition may preferably comprise other surfactants.

The detersive surfactant used may be anionic, nonionic, zwitterionic, amphoteric or cationic, or may comprise compatible mixtures of these types. More preferably the surfactant is selected from anionic, nonionic, cationic surfactants and mixtures thereof. Detergent surfactants useful in the present invention are described in U.S. Pat. No. 3,664,961 to Norris at 5.23 in 1972, U.S. Pat. No. 3,919,678 to Laughlin et al at 12.30 in 1975, U.S. Pat. No. 4,222,905 to Cockrell at 9.16 in 1980, and U.S. Pat. No. 4,239,659 to Murphy at 12.16 in 1980. Preferred are anionic and nonionic surfactants.

Preferably, the composition is substantially free of salts of alkyl sulfosuccinic acids, also known as sulfosuccinates or sulfosuccinates, and which are monoesters and/or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols, in particular ethoxylated fatty alcohols.

Useful anionic surfactants themselves can be of several different types. For example, water soluble salts of higher fatty acids, i.e. "soaps". This includes alkali metal soaps such as sodium, potassium, ammonium, soluble salts of organic bases such as mono-, di-or triethanolamine, and alkylammonium salts of higher fatty acids containing from about 8 to about 24 carbon atoms, preferably from about 12 to about 18 carbon atoms. Soaps may be prepared by direct saponification of fats and oils or by neutralization of free fatty acids. Soaps include sodium and potassium salts of fatty acid mixtures derived from coconut oil and tallow, i.e., sodium or potassium tallow and coconut oil soaps. Soaps include particularly suitable soaps of saturated fatty acids, such as salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid, in particular soap mixtures derived from natural fatty acids, such as coconut, palm kernel or tallow fatty acids.

Preferably, the detergent compositions of the present invention are substantially free of soap.

Other non-soap anionic surfactants suitable for use herein include the water soluble salts, preferably alkali metal and ammonium salts, of organic sulfuric acid reaction products having in their molecular structure an alkyl group containing from about 10 to about 20 carbon atoms and a sulfonic or sulfuric acid ester group. Examples of such combination surfactants are a) sodium, potassium and ammonium alkyl sulphates, especially those obtained by sulphating higher alcohols (C) ₈ To C ₁₈ Carbon atoms) such as those produced by reduction of glycerides of tallow or coconut oil; b) Sodium, potassium and ammonium alkyl polyethoxylated sulfates, particularly those wherein the alkyl group contains from 10 to 22, preferably from 12 to 18, carbon atoms and wherein the polyethoxylated chain contains from 1 to 15, preferably from 1 to 6, ethoxylated moieties; and c) sodium and potassium alkylbenzene sulfonates in which the alkyl group contains from about 9 to about 15 carbon atoms in a straight or branched chain configuration, such as in the united statesThose types described in patent nos. 2,220,099 and 2,477,383.

Preferred nonionic surfactants are of formula R ¹ (OC ₂ H ₄ ) Those of nOH, wherein R ¹ Is C ₁₀ -C ₁₆ Alkyl or C ₈ To C ₁₂ Alkylphenyl, and n is 3 to about 80. Particularly preferred is C ₁₂ To C ₁₅ Condensation products of alcohols with about 5 to about 20 moles of ethylene oxide per mole of alcohol, e.g. C condensed with about 6.5 moles of ethylene oxide per mole of alcohol ₁₂ To C ₁₃ . Preferred nonionic surfactants that may be used include the reaction products of compounds having a hydrophobic group and a reactive hydrogen atom (e.g., fatty alcohols, acids, amides) with alkylene oxides, particularly ethylene oxide alone or with propylene oxide. Specific nonionic detergent compounds are the condensation products of aliphatic linear or branched primary or secondary alcohols with ethylene oxide, typically 5 to 40EO, preferably 7EO to 9EO.

In all aspects of the invention, an additional anionic surfactant is preferably present, which may be selected from C ₁₀ To C ₂₀ Alkyl sulfate, C ₁₀ To C ₂₀ Alkyl ether sulfates and mixtures thereof. More preferably, the additional anionic surfactant is different from C ₁₀ To C ₂₀ Linear alkylbenzene sulfonates, and includes a mixture of anionic surfactants as previously specified. Preferred additional anionic surfactants that may be used are generally water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher acyl radicals.

Examples of suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, in particular those obtained by sulphating alcohols, sodium alkyl glyceryl ether sulphates, in particular those ethers of higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum. Preferred further anionic detergent compounds are C ₁₂ To C ₁₄ Sodium alkyl sulfate. Also applicable are surfactants such as those described in EP-A-328177 (Unilever), which exhibit resistance to salting out, described in EP-A-070074Alkyl polyglycoside surfactants and alkyl monoglycosides.

Further preferably, the additional surfactant may be selected from cationic surfactants, nonionic surfactants, amphoteric surfactants, zwitterionic surfactants, or combinations thereof.

In general, the nonionic and anionic surfactants of the surfactant system may be selected from the surfactants described in "Surface Active Agents" Vol.1, schwartz & Perry, interscience 1949,Vol.2,Schwartz,Perry&Berch,Interscience 1958, the current version of "McCutcheon's Emulsifiers and Detergents" published by Manufacturing Confectioners Company or "Tenside-Taschenbuch", H.Stache,2nd Edn,Carl Hauser Verlag,1981. Preferably the surfactant used is saturated.

Preferred zwitterionic surfactants include cocamidopropyl betaine. The preferred content of the zwitterionic surfactant is from 0.1 to 5% by weight, preferably from 0.5 to 4% by weight.

Further preferred ingredients

The detergent composition may comprise other preferred ingredients which may include complexing agents, fluorescers, dyes, enzyme stabilizers, other builders, perfumes, polymers, enzyme stabilizers, fillers selected from sulphates, bleaching agents and combinations thereof.

The solid detergent composition preferably comprises 1 to 3 wt% moisture, and also preferably a moisture content of 1 to 2 wt%.

Other builders:

the builder material may be selected from 1) calcium chelating agent materials, 2) precipitation materials, 3) calcium ion exchange materials, and 4) mixtures thereof.

Examples of calcium chelator builders include alkali metal polyphosphates, such as sodium tripolyphosphate, and organic chelators, such as ethylenediamine tetraacetic acid.

Examples of precipitated builder materials include sodium orthophosphate.

Examples of calcium ion-exchange builder materials include various types of water-insoluble crystalline or amorphous aluminosilicates, of which zeolites are the most well known representatives, such as zeolite a, zeolite B (also known as zeolite P), zeolite C, zeolite X, zeolite Y and zeolite P types as described in EP-a-0,384,070.

The composition may also contain 0 to 65% by weight of an organic builder or complexing agent, such as ethylenediamine tetraacetic acid, diethylenetriamine-pentaacetic acid, alkyl-or alkenyl succinic acids, nitrilotriacetic acid or other builders mentioned below. Many builders are also bleach stabilizers by virtue of their ability to complex metal ions.

Zeolite, bicarbonate and sesquicarbonate are examples of preferred builders.

The composition may contain a crystalline aluminosilicate as builder, preferably an alkali metal aluminosilicate, more preferably sodium aluminosilicate. This is typically present at a level of less than 15% by weight. Aluminosilicates are materials having the general formula: 0.8-1.5M ₂₀ .Al ₂ O ₃ .0.8-6SiO ₂

Wherein M is a monovalent cation, preferably sodium. These materials contain some bound water and are required to have a calcium ion exchange capacity of at least 50mg CaO/g. Preferred sodium aluminosilicates contain 1.5 to 3.5 SiO's in the above formula ₂ A unit. They can be readily prepared by the reaction between sodium silicate and sodium aluminate, as fully described in the literature. The ratio of surfactant to aluminosilicate (when present) is preferably greater than 5:2, more preferably greater than 3:1.

Alternatively or in addition to aluminosilicate builders, phosphate builders can be used. In the art, the term "phosphate" includes the di-, tri-and phosphonate species. Other forms of builder include silicates, such as soluble silicate, metasilicate, layered silicate (e.g. SKS-6 from Hoechst).

In the case of laundry compositions, it is preferred that the laundry detergent formulation is a non-phosphate-assisted laundry detergent formulation, i.e. comprising less than 1 wt% phosphate.

Fluorescent agent:

these materials are particularly useful in liquid laundry detergent compositions for hand washing. The composition preferably comprises a fluorescent agent (optical brightener).

Fluorescent agents are well known and many such fluorescent agents are commercially available. Typically, these fluorescent agents are provided and used in the form of their alkali metal salts, e.g., sodium salts. The total amount of one or more fluorescent agents used in the composition is typically 0.005 to 2 wt%, more preferably 0.01 to 0.1 wt%. Preferred classes of fluorescent agents are: stilbene biphenyl compounds, such as Tinopal (trade mark) CBS-X, diamine stilbenedisulfonic acid compounds, such as Tinopal DMS pure Xtra and Blankophor (trade mark) HRH, and pyrazoline compounds, such as Blankophor SN. Preferred fluorescers are: sodium 2 (4-styryl-3-sulfophenyl) -2H-naphthol [1,2-d ] triazoles, disodium 4,4' -bis { [ (4-anilino-6- (N-methyl-N-2-hydroxyethyl) amino 1,3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' -disulfonate, disodium 4,4' -bis { [ (4-anilino-6-morpholino-1, 3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' -disulfonate and disodium 4,4' -bis (2-sulfostyryl) biphenyl.

Preferably, the aqueous solution used in the method has a fluorescent agent present. When present in the aqueous solution used in the method, the fluorescent agent is preferably in the range of 0.0001g/l to 0.1g/l, preferably 0.001 to 0.02 g/l.

Dye:

the composition preferably comprises a dye. Dyes are discussed in K.Hunger (ed.) Industrial Dyes: chemistry, properties, applications (Weinheim: wiley-VCH 2003). The organic dyes are listed in the color index (Society of Dyers and Colourists and the American Association of Textile Chemists and Colorists).

Preferred dye chromophores are azo, azine, anthraquinone, phthalocyanine and triphenylmethane.

Azo, anthraquinone, phthalocyanine and triphenylmethane dyes are preferably either net anionic charged or uncharged. Azine dyes are preferably net anionic or cationic in charge.

Preferred non-shading dyes are selected from blue dyes, most preferably anthraquinone dyes with sulfonate groups and triphenylmethane dyes with sulfonate groups. Preferred compounds are acid blue 80, acid blue 1, acid blue 3; acid blue 5, acid blue 7, acid blue 9, acid blue 11, acid blue 13, acid blue 15, acid blue 17, acid blue 24, acid blue 34, acid blue 38, acid blue 75, acid blue 83, acid blue 91, acid blue 97, acid blue 93, acid blue 93:1, acid blue 97, acid blue 100, acid blue 103, acid blue 104, acid blue 108, acid blue 109, acid blue 110, and acid blue 213. Upon dissolution, the particles with non-hueing dye provide an attractive color to the wash liquor.

Blue or violet hueing dyes are most preferred. During the washing or rinsing step of the washing process, hueing dye is deposited onto the fabric, thereby providing a visible hue to the fabric. In this regard, the dye imparts a blue or violet color to the white cloth at a hue angle of 240 to 345, more preferably 260 to 320, most preferably 270 to 300. The white cloth used in this test was a bleached non-mercerized cotton sheet.

Hueing dyes are discussed in WO2005/003274, WO2006/032327 (Unilever), WO2006/032397 (Unilever), WO2006/045275 (Unilever), WO2006/027086 (Unilever), WO2008/017570 (Unilever), WO2008/141880 (Unilever), WO2009/132870 (Unilever), WO2009/141173 (Unilever), WO2010/099997 (Unilever), WO2010/102861 (Unilever), WO2010/148624 (Unilever), WO2008/087497 (P & G), WO2011/011799 (P & G), WO2012/054820 (P & G), WO2013/142495 (P & G) and WO2013/151970 (P & G).

Mixtures of hueing dyes may be used.

The hueing dye chromophore is most preferably selected from monoazo, disazo, anthraquinone and azine.

The monoazo dye preferably contains a heterocyclic ring, and most preferably is a thiophene dye. Monoazo dyes are preferably alkoxylated and are preferably uncharged or anionically charged at ph=7. Alkoxylated thiophene dyes are discussed in WO2013/142495 and WO 2008/087497.

Most preferred hueing dyes are selected from direct violet 9, direct violet 99, direct violet 35, solvent violet 13, disperse violet 28, dyes of the following structure:

perfume:

preferably, the composition comprises a perfume. The perfume is preferably in the range of 0.001 to 3 wt%, most preferably 0.1 to 1 wt%. Many examples of suitable fragrances are provided in CTFA (Cosmetic, toiletry and Fragrance Association) 1992International Buyers Guide published by CFTA Publications and OPD 1993Chemicals Buyers Directory 80th Annual Edition published by Schnell Publishing co.

It is common for a variety of perfume components to be present in the formulation. In the compositions of the present invention, it is envisaged that there are four or more, preferably five or more, more preferably six or more or even seven or more different perfume components.

Preferably 15 to 25% by weight of the perfume mixture is a top note. The top note is defined by Poucher (Journal of the Society of Cosmetic Chemists 6 (2): 80[1955 ]). Preferred top notes are selected from citrus oils, linalool, linalyl acetate, lavender, dihydromyrcenol, rose ethers and cis-3-hexanol.

It is preferred that the laundry treatment composition is free of peroxygen bleach, for example sodium percarbonate, sodium perborate and peracid.

And (2) polymer:

the composition may comprise one or more other polymers. Examples are carboxymethyl cellulose, poly (ethylene glycol), poly (vinyl alcohol), polycarboxylates (e.g. polyacrylates), maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers. Polymers that prevent dye deposition may be present in the formulation, such as poly (vinylpyrrolidone), poly (vinylpyridine-N-oxide), and poly (vinylimidazole).

Thickening polymers, such as anionic acrylic polymers, may be included, examples including Acusol820.

Enzyme stabilizer:

any enzyme present in the composition may be stabilised using conventional stabilisers, for example polyols such as propylene glycol or glycerol, sugars or sugar alcohols, lactic acid, boric acid or derivatives of boric acid (e.g. aromatic borates) or phenylboronic acid derivatives (e.g. 4-formylphenylboronic acid), and the composition may be formulated as described, for example, in WO92/19709 and WO 92/19708.

Alkyl groups encompass branched, cyclic, and straight alkyl chains when the alkyl groups are long enough to form branched or cyclic chains. The alkyl group is preferably linear or branched, most preferably linear.

The indefinite articles "a" and "an" and their corresponding definite articles are used herein unless otherwise indicated to mean at least one, or one or more.

The invention will be further described by the following non-limiting examples.

Sulfate:

in the present invention, the ratio of sulfate to acidic dispersing aid is preferably from 12:1 to 1:1, most preferably 11:1-2:1.

The sulphate may be present in the detergent composition in any form, preferably an inorganic sulphate, such as sodium sulphate, magnesium sulphate, ammonium sulphate or a mixture of sulphate forms. The sulphate is preferably substantially anhydrous (i.e. typically no more than 50 wt%, preferably no more than 25 wt%, more preferably no more than 15 wt%, most preferably no more than 10 wt% of the sulphate is aqueous), preferably it is anhydrous sodium sulphate. It is preferably combined with a small amount of magnesium sulphate, preferably 0.2% to 5% by weight of the composition.

Bleaching agent:

the use according to the first aspect of the invention may preferably comprise a bleach.

Such bleaching agents include hydrogen peroxide, or substances which can generate perhydroxyl radicals, such as inorganic or organic peroxides. In general, peroxygen bleaching compounds or hydrogen peroxide must be activated. The solid detergent composition preferably comprises a bleach. The bleaching agent preferably has a peroxide source. It is also preferred that a bleach is present together with a bleach activator.

Examples of bleach activators are tetraacetyl ethylenediamine (TAED) and nonyloxy benzenesulfonsodium salt (NOBS). The bleach activator reacts with the perhydroxide anion (OOH-) of hydrogen peroxide released by the peroxygen bleaching compound in aqueous solution to form a peroxyacid that is more reactive as a bleach than the peroxide bleach alone.

Hydrogen peroxide sources are well known in the art. Sources of hydrogen peroxide are described in detail in Kirk Othmer' sEncyclopedia of Chemical Technology,4th Ed (1992,John Wiley&Sons), vol.4, pp.271-300"Bleaching Agents (Supvey)," and include sodium perborate and alkali metal salts of sodium percarbonate, including various coated and modified forms. Suitable peroxy bleach compounds include hydrogen peroxide or any solid adduct thereof, such as the organic peroxide examples; urea peroxide and inorganic persalts such as alkali metal perborates, percarbonates, perphosphates, persilicates and persulphates. Mixtures of two or more such compounds may also be suitable.

Preferred inorganic persalts are sodium perborate monohydrate and tetrahydrate, and sodium percarbonate. Hydrogen peroxide is particularly preferred in liquid cleaning compositions.

Percarbonate is stable during storage and dissolves rapidly in cleaning solutions, and is particularly preferred. It is believed that this rapid dissolution results in the formation of higher levels of percarboxylic acid and thus enhances the bleaching performance of the substrate. Highly preferred percarbonates are in uncoated or coated form. Preferably the average particle size of the uncoated and coated percarbonate ranges from about 400 to about 1200 microns, most preferably from about 400 to about 600 microns. If coated percarbonates are used, preferred coating materials include mixtures of carbonates and sulfates, zeolites, precipitated silica, waxes, borates, polymers, citrates, silicates, borosilicate or fatty acids.

Preferably, the disclosed cleaning compositions have from 4 wt% to 35 wt% peroxygen bleaching compound.

Preferred bleach activators include compounds from the class of the polyacylated alkylene diamines, preferably tetraacetyl ethylenediamine (TAED). Yet another preferred bleach activator is a hydroxybenzoic acid derivative of formula (I)

Wherein R is C ₈ To C ₁₂ An alkyl group. Preferably, the bleach activator is decanoyloxybenzoic acid (DOBA) and derivatives thereof.

The following non-limiting examples further illustrate preferred embodiments of the invention. All percentages mentioned in the examples and throughout the specification are by weight based on total weight unless otherwise indicated.

According to a second aspect, a method of inactivating microorganisms of a textile is disclosed, the method comprising the steps of:

i) Applying a solid detergent composition to the textile, wherein the solid detergent composition comprises a combination of alkylbenzene sulfonate, a hydrolase enzyme selected from the group consisting of protease, amylase, lipase, cellulase, mannanase, or a combination thereof, and an alkalinity source, and the detergent composition has a pH of 10 to 13;

ii) contacting the textile with the solid detergent composition for a period of at least 30 minutes, and preferably also at least 1 hour.

Preferably the solid detergent composition is applied in a liquid diluted form. The liquid is preferably water. The solid detergent composition is diluted to form a wash liquor. The wash liquor preferably comprises alkylbenzene sulfonate surfactant at a concentration of 40ppm to 2000ppm, hydrolase at a concentration of 0.0001ppm to 30ppm and an alkaline source at a concentration of 120ppm to 2500 ppm.

Examples

Example 1: viral inactivation was assessed using different detergent compositions.

Solid powder laundry detergent compositions as shown in table 1 were prepared and used to evaluate the effect of inhibiting viral growth. 2 different solid detergent compositions having different amounts of LAS surfactant as shown in table 1 below were obtained for evaluation.

TABLE 1

Antiviral study:

each of the detergent compositions shown in table 1 was diluted separately with sterile hard water to prepare aqueous liquids having concentrations of 4 g/l, 2 g/l and 0.4 g/l according to the EN144476 standard described below.

Aqueous liquids having 3 different concentrations as described above were prepared from the detergent composition of Ex 1 and tested for virucidal effect according to european standard method EN14476:2013+a2:2019 (quantitative suspension test-test method and requirement for evaluation of virucidal activity in chemical disinfectants and antimicrobial-medical fields (stage 2/step 1).

Experimental conditions:

the test product solutions of the above three concentrations were used for the virucidal effect test and gave a 60 minute contact time. The test temperature was maintained at 27 ℃ and the disturbing condition was cleaning with low levels of organic fouling.

The tested compositions were tested for their virucidal effect on adenovirus, murine norovirus, poliovirus and bovine coronavirus, and the final virucidal effect was expressed as log reduction.

Similarly, aqueous liquids were prepared and tested for Ex 2 and the test results are provided in table 2.

TABLE 2

* The alkali source is sodium carbonate

* The alkali source is sodium carbonate

* The alkali source is sodium carbonate.

The results in table 2 show that the use of a solid detergent composition having a pH in the range of 10 to 13 and a combination of LAS surfactant, alkali source and protease (hydrolase selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or combinations thereof) provides improved virucidal effect (log kill of at least 1) on both enveloped and non-enveloped viruses.

Example 2: evaluation of bacterial inactivation Using different detergent compositions

The detergent compositions according to table 3 were diluted with sterile hard water to prepare aqueous liquids having a concentration of 7.5 g/l according to EN1276 standard described below.

TABLE 3 Table 3

Composition of the components	Ex 3 (wt.%)
		LAS (Linear alkylbenzenesulfonate surfactant)	11.27
Sodium carbonate	31.09
		Sulfate salt	55
Zeolite	2.35
		Hydrolytic enzyme	0.3

The aqueous liquids described above were prepared from the detergent compositions of Ex 3 and tested for antibacterial effect according to the european standard method EN1276 test.

Experimental conditions:

the antibacterial effect test was performed with the test product solution at a concentration of 7.5 g/l as described above and provided a contact time of 60 minutes. The test temperature was maintained at 27 ℃ and the disturbing condition was a low level of cleaning of organic fouling. The antimicrobial effect of the tested compositions was tested using staphylococcus aureus (s.aureus), enterococcus hainanensis (e.hirae), and the final antimicrobial effect was expressed as log reduction. The test results are provided in table 4.

TABLE 4 Table 4

The results in table 4 show that the use of a solid detergent composition having a pH in the range of 10 to 13 and having a combination of LAS surfactant, alkali source and hydrolase enzyme (a hydrolase enzyme selected from the group consisting of protease, lipase, cellulase, amylase, mannanase or a combination thereof) provides improved bactericidal effect (log kill of at least 1) on bacteria.

Claims (15)

1. Use of a combination of an alkylbenzene sulfonate surfactant, a hydrolase enzyme and an alkali source in a solid detergent composition having a pH of 10 to 13 measured at 25 ℃ and at a 10% aqueous solution concentration in deionized water for inactivating microorganisms on textiles in a laundry process, wherein the hydrolase enzyme is selected from the group consisting of proteases, lipases, cellulases, amylases, mannanases, or combinations thereof.

2. The use according to any one of the preceding claims, wherein the protease is a serine protease.

3. The use of claim 1, wherein the alkali source is selected from the group consisting of alkali metal or alkaline earth metal salts of carbonic acid, dicarbonic acid, silicic acid, metasilicic acid, or combinations thereof.

4. Use according to claim 1, wherein the detergent composition having a combination of alkylbenzene sulfonate surfactant, hydrolase and alkali source is applied to the textile to be washed in liquid diluted form, preferably diluted with water, to form a wash liquor.

5. The use according to any one of the preceding claims, wherein the microorganism is a virus or a bacterium.

6. The use according to any preceding claim, wherein the microorganism is in intimate contact with the detergent composition for at least 30 minutes, and preferably also for at least 1 hour.

7. The use according to any one of the preceding claims, wherein the combination of alkylbenzene sulfonate surfactant, hydrolase and alkali source has a viral inactivating effect against enveloped and/or non-enveloped viruses.

8. The use of any one of the preceding claims, wherein the combination of alkylbenzene sulfonate surfactant, hydrolase and alkali source has a virally inactivating effect against a virus selected from the group consisting of adenoviridae, alphaherpesviridae, astroviridae, herpesviridae, bisrnaviridae, vitroneviridae, bunyaviridae, calicivviridae, vertebratiopoxviridae, flaviviridae, herpesviridae, hepadnaviridae, herpesviridae, iridoviridae, orthomyxoviridae, orthoretroviridae, papillomaviridae, paramyxoviridae, parvoviridae, picoviridae, pneumoviridae, romovoviridae, polyomaviridae, coronaviridae, arteriviridae, marine viridae, cycloviridae and bar viridae.

9. The use according to any preceding claim, wherein the detergent composition achieves a log 1 to log 5 reduction of the virus when the contact time is at least 30 minutes, further preferably at least 1 hour.

10. The use of any preceding claim, wherein the alkylbenzene sulfonate surfactant is present in the detergent composition at a concentration of from 2 wt% to 40 wt%.

11. The use according to any preceding claim, wherein the hydrolase enzyme is present in the wash liquor during the laundry process at a concentration of from 0.0001ppm to 30 ppm.

12. The use according to any preceding claim, wherein the detergent composition further comprises a bleach, preferably the bleach has a peroxide source.

13. The use of claim 12, wherein the detergent composition comprises a combination of bleach and bleach activator.

14. The use according to any preceding claim, wherein the solid detergent composition is in the form of a unit dose product, wherein the solid detergent composition is at least partially surrounded by a water-soluble film.

15. A method of inactivating microorganisms from a textile, the method comprising the steps of:

i) Applying a solid detergent composition to the textile, wherein the solid detergent composition comprises an alkylbenzene sulfonate, a combination of a hydrolase enzyme selected from the group consisting of a protease, an amylase, a lipase, a cellulase, a mannanase or a combination thereof, and an alkalinity source, and the detergent composition has a pH of 10 to 13;

ii) contacting the textile with the solid detergent composition for a period of at least 30 minutes, and preferably also at least 1 hour.