EP3417040A1

EP3417040A1 - Whitening composition

Info

Publication number: EP3417040A1
Application number: EP16798783.3A
Authority: EP
Inventors: Stephen Norman Batchelor; Jayne Michelle Bird; Carsten Cohrs; Jan DIEDERICHS; Dirk Leinweber; Kevin James MUTCH; Steffen ROMANSKI
Original assignee: Unilever PLC
Current assignee: Unilever PLC
Priority date: 2016-02-17
Filing date: 2016-11-23
Publication date: 2018-12-26
Anticipated expiration: 2036-11-23
Also published as: CN108603140A; WO2017140392A1; BR112018016674B1; ZA201804919B; BR112018016674A2; CN108603140B; EP3417040B1; AR107626A1

Abstract

The present invention provides a domestic laundry cleaning composition.

Description

WHITENING COMPOSITION

Field of Invention

The present invention concerns the use of cleaning laundry compositions.

Background of the Invention

Maintaining and improving the cleaning of textiles during domestic laundry is desirable.

Protease enzymes are used in laundry detergent formulations to remove protein containing stains from fabrics. Protease enzyme do not perform well at low temperatures and with short wash times.

There is a need to increase stain removal in laundry formulations containing protease enzymes for low temperature quick washes.

Summary of the Invention

There is a need for technologies to increase stain removal in laundry formulations containing protease enzymes.

We have found that selected alkoxylated substituted phenol (ASP) dispersants when incorporated into laundry detergents with a protease enzyme increase stain removal.

In one aspect the present invention provides a laundry detergent composition comprising:

(i) from 0.5 to 20 wt%, preferably 1 to 10 wt%, most preferably 2 to 6 wt%, of an

alkoxylated substituted phenol dispersant of the following structure:

wherein

X is selected from: ethoxy; and, mixtures of ethoxy and propoxy groups where the number of ethoxy groups is greater than the number of propoxy groups, and wherein n is from 6 to 70, preferably from 8 to 34; most preferably n is selected from 14; 15; 16; 17; 18; 19; 20; 21 ; 22; 23; 24; 25; 26; 27; 28; 29; 30; 31 ; and, 32; preferably X is ethoxy;

Y is selected from: Ri ; ORi , COOR_5; F; CI; Br; I; CN; and N0₂, wherein Ri is a C1 to C4 linear or branched alkyl group and wherein R₅ is a C1 to C18 linear or branched alkyl group, preferably Rs is a C1 to C4 linear or branched alkyl group, most preferably Rs is methyl; preferably Y is selected from methyl, ethyl, methoxy, ethoxy, most preferably methoxy or methyl;

R2 and R3 are selected from: C1 to C3 linear or branched alkyl aryl groups; and, aryl groups; preferably R2 and R3 are selected from styryl and cumyl, most preferably styryl, preferably both R2 and R3 are in the ortho position to the -0-[X]_n-T group;

T is selected from: H; CH₃; S0₃ ^"; CH₂COO^"; PO3^2"; C₂H₅; n-propyl, i-propyl; n-butyl; t-butyl; and, sulfosuccinate, T is preferably H;

(ii) from 0 to 50 wt% surfactant, other than the alkoxylated substituted phenol

dispersant; preferably the surfactant is selected from: anionic and non-ionic surfactants, preferably the level of surfactant is from 4 to 40 wt%, more preferably 6 to 30 wt%, most preferably 8 to 20 wt%; preferably the weight fraction of non-ionic surfactant anionic surfactant is from 0 to 0.3, preferably 0 to 0.15, most preferably 0.05 to 0.12; and, (iii) from 0.0005 to 0.2 wt% of a protease enzyme, preferably from 0.002 to 0.05 wt %.

The level of a protease enzyme in the laundry composition of the invention is the level of pure protein.

Preferably the composition additionally comprises from 0.0001 to 0.5 wt % of a fluorescent agent and/or from 0.0001 wt% to 0.1 wt% shading dye.

The laundry detergent composition is preferably selected from a granular detergent powder; and an aqueous laundry liquid detergent; most preferably the laundry detergent composition is an aqueous laundry liquid detergent composition.

In another aspect the present invention provides a domestic method of treating a textile, the method comprising the steps of:

(i) treating a textile with an aqueous solution of the alkoxylated substituted phenol dispersant the aqueous solution comprising from 10 ppm to 5000 ppm, more preferably from 100 ppm to l OOOppm, of the alkoxylated substituted phenol dispersant as defined herein; from 0.01 to 1 ppm of a protease enzyme and, 0 to 6 g/L of a surfactant, preferably 0.2 to 1 g/L, other than the alkoxylated substituted phenol dispersant; and,

(ii) optionally rinsing and drying the textile. In the method the level of the protease in the aqueous solution is more preferably from 0.02 to 0.2 ppm.

In the method the surfactant is of the type as preferred herein. In the method the level of the perfume in the aqueous solution is preferably from 0.1 to 100 ppm, more preferably from 1 to 10 ppm.

In the method aspects of the present invention the surfactant used is preferably as preferred for the composition aspects of the present invention. Domestic methods are preferably conducted in a domestic washing machine or by hand washing. The temperature of the wash is preferably from 285 to 313K. The main wash time is preferably 5 to 30 minutes.

The textile is preferably an item of clothing, bedding or table cloth. Preferred items of clothing are cotton containing shirts, trousers, underwear and jumpers.

Detailed Description of the Invention Alkoxylated Substituted Phenol

In the context of the current invention the alkoxylated substituted phenol (ASP) is not considered a surfactant and does not contribute numerically to the surfactant as defined herein.

The most preferred aryl groups are phenyl and substituted phenyl.

C1 to C3 linear or branched alkyi aryl groups are C1 to C3 linear or branched alkyi groups substituted by an aromatic group, for example: styryl, cumyl, benzyl.

A styryl group is -CH(CH3)Ph; a cumyl group is -C(CH3)2Ph; a benzyl group is ChbPh, where Ph is phenyl.

The value n is the mole average number of alkoxyl groups. The value of n may be measured using NMR.

Sulfoccinate has the structure, depicted as the Na salt:

S0₃Na O

10

The ASP in combination with the protease enzyme enhance stain removal and reduces the redeposition of soils, both of which enhance the whiteness of fabrics.

Surfactant

The laundry composition may comprises anionic and non-ionic surfactant (which includes a mixture of the same).

The nonionic and anionic surfactants of the surfactant system may be chosen from the surfactants described "Surface Active Agents" Vol. 1 , by Schwartz & Perry, Interscience 1949, Vol. 2 by Schwartz, Perry & Berch, Interscience 1958, in the current edition of "McCutcheon's Emulsifiers and Detergents" published by Manufacturing Confectioners Company or in "Tenside-Taschenbuch", H. Stache, 2nd Edn., Carl Hauser Verlag, 1981 or in Anionic Surfactants: Organic Chemistry edited by Helmut W. Stache (Marcel Dekker 1996) . Suitable anionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher alkyl radicals. Examples of suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher Cs to Cie alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl Cg to C20 benzene sulphonates, particularly sodium linear secondary alkyl C10 to C15 benzene sulphonates; and sodium alkyi glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum. The anionic surfactant is preferably selected from: linear alkyi benzene sulphonate; alkyi sulphates; alkyi ether sulphates; alkyi ether carboxylates; soaps; alkyi (preferably methyl) ester sulphonates, and mixtures thereof.

The most preferred anionic surfactants are selected from: linear alkyi benzene sulphonate; alkyi sulphates; alkyi ether sulphates and mixtures thereof. Preferably the alkyi ether sulphate is a C12-C14 n-alkyl ether sulphate with an average of 1 to 3EO (ethoxylate) units. Sodium lauryl ether sulphate is particularly preferred (SLES).

Preferably the linear alkyi benzene sulphonate is a sodium Cn to C15 alkyi benzene sulphonates. Preferably the alkyi sulphates is a linear or branched sodium C12 to C18 alkyi sulphates. Sodium dodecyl sulphate is particularly preferred, (SDS, also known as primary alkyi sulphate).

The level of anionic surfactant in the laundry composition is preferably from 4 to 40 wt%, more preferably 6 to 30 wt%, and most preferably 8 to 20 wt%.

Preferably two or more anionic surfactant are present, for example linear alkyi benzene sulphonate together with an alkyi ether sulphate.

Preferably the laundry composition in addition to the anionic surfactant comprises alkyi ethoxylated non-ionic surfactant

Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having an aliphatic hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids or amides, especially ethylene oxide either alone or with propylene oxide. Specific nonionic detergent compounds are the condensation products of aliphatic Cs to C18 primary or secondary linear or branched alcohols with ethylene oxide.

Preferably the alkyi ethoxylated non-ionic surfactant is a Cs to C18 primary alcohol with an average ethoxylation of 7EO to 9EO units. Preferably the surfactants used are saturated.

Also applicable are surfactants such as those described in EP-A-328 177 (Unilever), which show resistance to salting-out, the alkyl polyglycoside surfactants described in EP-A-070 074, and alkyl monoglycosides.

Builders or Complexing Agents

Builder materials may be selected from 1 ) calcium sequestrant materials, 2) precipitating materials, 3) calcium ion-exchange materials and 4) mixtures thereof.

Examples of calcium sequestrant builder materials include alkali metal polyphosphates, such as sodium tripolyphosphate and organic sequestrants, such as ethylene diamine tetra-acetic acid.

Examples of precipitating builder materials include sodium orthophosphate and sodium carbonate.

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

The composition may also contain 0-65 % of a builder or complexing agent such as ethylenediaminetetraacetic acid, diethylenetriamine-pentaacetic acid, alkyl- or alkenylsuccinic acid, nitrilotriacetic acid or the other builders mentioned below. Many builders are also bleach-stabilising agents by virtue of their ability to complex metal ions.

Zeolite and carbonate (carbonate (including bicarbonate and sesquicarbonate)) are preferred builders with carbonates being particularly preferred.

The composition may contain as builder a crystalline aluminosilicate, preferably an alkali metal aluminosilicate, more preferably a sodium aluminosilicate. This is typically present at a level of less than 15%w. Aluminosilicates are materials having the general formula: 0.8-1.5 M₂0. AI2O3. 0.8-6 Si0₂ where 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 50 mg CaO/g. The preferred sodium aluminosilicates contain 1.5-3.5 S1O2 units in the formula above. They can be prepared readily by reaction between sodium silicate and sodium aluminate, as amply described in the literature. The ratio of surfactants to alumuminosilicate (where present) is preferably greater than 5:2, more preferably greater than 3:1 .

Alternatively, or additionally to the aluminosilicate builders, phosphate builders may be used. In this art the term 'phosphate' embraces diphosphate, triphosphate, and phosphonate species. Other forms of builder include silicates, such as soluble silicates, metasilicates, layered silicates (e.g. SKS-6 from Hoechst).

Preferably the laundry detergent formulation is a non-phosphate built laundry detergent formulation, i.e., contains less than 1 wt% of phosphate. Preferably powder laundry detergent formulations are predominantly carbonate built. Powders, should preferably give an in use pH of 9.5-1 1 .

Most preferably the laundry detergent is an aqueous liquid laundry detergent, preferably with a pH of from 7 to 9.

In the aqueous liquid laundry detergent it is preferred that mono propylene glycol is present at a level from 1 to 30 wt%, most preferably 2 to 18 wt%, to provide the formulation with appropriate, pourable viscosity.

Fluorescent Agent The composition preferably comprises a fluorescent agent (optical brightener).

Fluorescent agents are well known and many such fluorescent agents are available commercially. Usually, these fluorescent agents are supplied and used in the form of their alkali metal salts, for example, the sodium salts. Preferred classes of fluorescer are: Di-styryl biphenyl compounds, e.g. Tinopal (Trade Mark) CBS-X, Di-amine stilbene di-sulphonic acid compounds, e.g. Tinopal DMS pure Xtra and Blankophor (Trade Mark) HRH, and Pyrazoline compounds, e.g. Blankophor SN.

Preferred fluorescers are: sodium 2 (4-styryl-3-sulphophenyl)-2H-napthol[1 ,2-d]triazole, disodium 4,4'-bis{[(4-anilino-6-(N methyl-N-2 hydroxyethyl) amino 1 ,3,5-triazin-2- yl)]amino}stilbene-2-2' disulophonate, disodium 4,4'-bis{[(4-anilino-6-morpholino-1 ,3,5- triazin-2-yl)]amino} stilbene-2-2' disulphonate, and disodium 4,4'-bis(2- sulphostyryl)biphenyl.

The total amount of the fluorescent agent or agents used in the composition is preferably from 0.0001 to 0.5 wt %, more preferably 0.005 to 2 wt %, most preferably 0.05 to 0.25 wt %.

The aqueous solution used in the method has a fluorescer present. The fluorescer is present in the aqueous solution used in the method preferably in the range from 0.0001 g/l to 0.1 g/l, more preferably 0.001 to 0.02 g/l. Perfume

The composition preferably comprises a perfume. The perfume is preferably in the range from 0.001 to 3 wt %, more preferably 0.05 to 0.5 wt%, most preferably from 0.1 to 1 wt %. Many suitable examples of perfumes are provided in the CTFA (Cosmetic, Toiletry and Fragrance Association) 1992 International Buyers Guide, published by CFTA Publications and OPD 1993 Chemicals Buyers Directory 80th Annual Edition, published by Schnell Publishing Co.

Preferably the perfume comprises at least one note (compound) from: alpha-isomethyl ionone, benzyl salicylate; citronellol; coumarin; hexyl cinnamal; linalool; Pentanoic acid, 2- methyl-, ethyl ester; octanal; benzyl acetate; 1 ,6-octadien-3-ol, 3,7-dimethyl-, 3-acetate; cyclohexanol, 2-(1 ,1-dimethylethyl)-, 1-acetate; delta-damascone; beta-ionone; verdyl acetate; dodecanal; hexyl cinnamic aldehyde; cyclopentadecanolide; benzeneacetic acid, 2-phenylethyl ester;amyl salicylate; beta-caryophyllene; ethyl undecylenate; geranyl anthranilate; alpha-irone; beta-phenyl ethyl benzoate; alpa-santalol; cedrol; cedryl acetate; cedry formate; cyclohexyl salicyate; gamma-dodecalactone; and, beta phenylethyl phenyl acetate.

Useful components of the perfume include materials of both natural and synthetic origin. They include single compounds and mixtures. Specific examples of such components may be found in the current literature, e.g., in Fenaroli's Handbook of Flavor Ingredients, 1975, CRC Press; Synthetic Food Adjuncts, 1947 by M. B. Jacobs, edited by Van Nostrand; or Perfume and Flavor Chemicals by S. Arctander 1969, Montclair, N.J. (USA). It is commonplace for a plurality of perfume components to be present in a formulation. In the compositions of the present invention it is envisaged that there will be four or more, preferably five or more, more preferably six or more or even seven or more different perfume components. In perfume mixtures preferably 15 to 25 wt% are top notes. Top notes are 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 oxide and cis-3-hexanol. The International Fragrance Association has published a list of fragrance ingredients (perfums) in 201 1. (http://www.ifraorq.Org/en-us/inqredients#.U7Z4hPldWzk)

The Research Institute for Fragrance Materials provides a database of perfumes

(fragrances) with safety information.

Perfume top note may be used to cue the whiteness and brightness benefit of the invention.

Some or all of the perfume may be encapsulated, typical perfume components which it is advantageous to encapsulate, include those with a relatively low boiling point, preferably those with a boiling point of less than 300, preferably 100-250 Celsius. It is also advantageous to encapsulate perfume components which have a low CLog P (ie. those which will have a greater tendency to be partitioned into water), preferably with a CLog P of less than 3.0. These materials, of relatively low boiling point and relatively low CLog P have been called the "delayed blooming" perfume ingredients and include one or more of the following materials: allyl caproate, amyl acetate, amyl propionate, anisic aldehyde, anisole, benzaldehyde, benzyl acetate, benzyl acetone, benzyl alcohol, benzyl formate, benzyl iso valerate, benzyl propionate, beta gamma hexenol, camphor gum, laevo-carvone, d-carvone, cinnamic alcohol, cinamyl formate, cis-jasmone, cis-3-hexenyl acetate, cuminic alcohol, cyclal c, dimethyl benzyl carbinol, dimethyl benzyl carbinol acetate, ethyl acetate, ethyl aceto acetate, ethyl amyl ketone, ethyl benzoate, ethyl butyrate, ethyl hexyl ketone, ethyl phenyl acetate, eucalyptol, eugenol, fenchyl acetate, flor acetate (tricyclo decenyl acetate) , frutene (tricyclco decenyl propionate) , geraniol, hexenol, hexenyl acetate, hexyl acetate, hexyl formate, hydratropic alcohol, hydroxycitronellal, indone, isoamyl alcohol, iso menthone, isopulegyl acetate, isoquinolone, ligustral, linalool, linalool oxide, linalyl formate, menthone, menthyl acetphenone, methyl amyl ketone, methyl

anthranilate, methyl benzoate, methyl benyl acetate, methyl eugenol, methyl heptenone, methyl heptine carbonate, methyl heptyl ketone, methyl hexyl ketone, methyl phenyl carbinyl acetate, methyl salicylate, methyl-n-methyl anthranilate, nerol, octalactone, octyl alcohol, p-cresol, p-cresol methyl ether, p-methoxy acetophenone, p-methyl

acetophenone, phenoxy ethanol, phenyl acetaldehyde, phenyl ethyl acetate, phenyl ethyl alcohol, phenyl ethyl dimethyl carbinol, prenyl acetate, propyl bornate, pulegone, rose oxide, safrole, 4-terpinenol, alpha-terpinenol, and /or viridine. It is commonplace for a plurality of perfume components to be present in a formulation. In the compositions of the present invention it is envisaged that there will be four or more, preferably five or more, more preferably six or more or even seven or more different perfume components from the list given of delayed blooming perfumes given above present in the perfume.

Another group of perfumes with which the present invention can be applied are the so- called aromatherapy' materials. These include many components also used in perfumery, including components of essential oils such as Clary Sage, Eucalyptus, Geranium, Lavender, Mace Extract, Neroli, Nutmeg, Spearmint, Sweet Violet Leaf and Valerian.

It is preferred that the laundry treatment composition does not contain a peroxygen bleach, e.g., sodium percarbonate, sodium perborate, and peracid. Polymers

The composition may comprise one or more further polymers. Examples are

carboxymethylcellulose, poly (ethylene glycol), polyvinyl alcohol), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.

Polymers present to prevent dye deposition may be present, for example

poly(vinylpyrrolidone), poly(vinylpyridine-N-oxide), and poly(vinylimidazole).

Shading Dye

Dyes are described in Color Chemistry Synthesis, Properties and Applications of Organic Dyes and Pigments, (H Zollinger, Wiley VCH, Zurich, 2003) and, Industrial Dyes

Chemistry, Properties Applications. (K Hunger (ed), Wiley-VCH Weinheim 2003).

Shading Dyes for use in laundry detergents preferably have an extinction coefficient at the maximum absorption in the visible range (400 to 700nm) of greater than

5000 L mol^"1 cm^"1, preferably greater than 10000 L mol^"1 cm^"1. The dyes are blue or violet in colour.

Preferred shading dye chromophores are azo, azine, anthraquinone, and

triphenylmethane. Azo, anthraquinone, phthalocyanine and triphenylmethane dyes preferably carry a net anionic charged or are uncharged. Azine preferably carry a net anionic or cationic charge. Blue or violet shading dyes deposit to fabric during the wash or rinse step of the washing process providing a visible hue to the fabric. In this regard the dye gives a blue or violet colour to a white cloth with a hue angle of 240 to 345, more preferably 250 to 320, most preferably 250 to 280. The white cloth used in this test is bleached non- mercerised woven cotton sheeting.

Shading dyes are discussed in WO2005/003274, WO2006/032327(Unilever),

WO 2006/032397(Unilever), WO2006/045275(Unilever), WO 2006/027086(Unilever), WO 2008/017570(Unilever), WO 2008/141880 (Unilever), WO2009/132870(Unilever), WO 2009/141 173 (Unilever), WO 2010/099997(Unilever), WO 2010/102861 (Unilever), WO 2010/148624(Unilever), WO2008/087497 (P&G), WO201 1/01 1799 (P&G),

WO2012/054820 (P&G), WO2013/142495 (P&G) and WO2013/151970 (P&G).

Mono-azo dyes preferably contain a heterocyclic ring and are most preferably thiophene dyes. The mono-azo dyes are preferably alkoxylated and are preferably uncharged or anionically charged at pH=7. Alkoxylated thiophene dyes are discussed in

WO/2013/142495 and WO/2008/087497. Preferred examples of thiophene dyes are shown below:

Bis-azo dyes are preferably sulphonated bis-azo dyes. Preferred examples of sulphonated bis-azo compounds are direct violet 7, direct violet 9, direct violet 1 1 , direct violet 26, direct violet 31 , direct violet 35, direct violet 40, direct violet 41 , direct violet 51 , Direct Violet 66, direct violet 99 and alkoxylated versions thereof. Alkoxylated bis-azo dyes are discussed in WO2012/054058 and WO2010/151906. An example of an alkoxylated bis-azo dye is :

Azine dye are preferably selected from sulphonated phenazine dyes and cationic phenazine dyes. Preferred examples are acid blue 98, acid violet 50, dye with CAS-No 72749-80-5, acid blue 59, and the phenazine dye selected from:

wherein:

X₃ is selected from: -H; -F; -CH₃; -C₂H₅; -OCH₃; and, -OC₂H₅; X₄ is selected from: -H; -CH₃; -C₂H₅; -OCH₃; and, -OC₂H₅;

Y₂ is selected from: -OH; -OCH₂CH₂OH; -CH(OH)CH₂OH; -OC(0)CH₃; and, C(0)OCH₃.

The shading dye is present is present in the composition in range from 0.0001 to 0.5 wt %, preferably 0.001 to 0.1 wt%. Depending upon the nature of the shading dye there are preferred ranges depending upon the efficacy of the shading dye which is dependent on class and particular efficacy within any particular class. As stated above the shading dye is a blue or violet shading dye. A mixture of shading dyes may be used. The shading dye is most preferably a reactive blue anthraquinone dye covalently linked to an alkoxylated polyethyleneimine. The alkoxylation is preferably selected from

ethoxylation and propoxylation, most preferably propoxylation. Preferably 80 to 95 mol% of the N-H groups in the polyethylene imine are replaced with iso-propyl alcohol groups by propoxylation. Preferably the polyethylene imine before reaction with the dye and the propoxylation has a molecular weight of 600 to 1800.

An example structure of a preferred reactive anthraquinone covalently attached to a propoxylated polyethylene imine is:

(Structure I).

Preferred reactive anthraquinone dyes are: Reactive blue 1 ; Reactive blue 2; Reactive blue 4; Reactive blue 5; Reactive blue 6; Reactive blue 12; Reactive blue 16; reactive blue 19; Reactive blue 24 ; Reactive blue 27; Reactive blue 29; Reactive blue 36;

Reactive blue 44; Reactive blue 46 ; Reactive blue 47; reactive blue 49; Reactive blue 50; Reactive blue 53; Reactive blue 55; Reactive blue 61 ; Reactive blue 66; Reactive blue 68; Reactive blue 69; Reactive blue 74; Reactive blue 86; Reactive blue 93; Reactive blue 94; Reactive bluel 01 ; Reactive blue103; Reactive blue1 14; Reactive blue1 17; Reactive blue125; Reactive blue141 ; Reactive blue142; Reactive blue 145; Reactive blue 149; Reactive blue 155; Reactive blue 164; Reactive blue 166; Reactive blue 177;

Reactive blue 181 ; Reactive blue 185; Reactive blue 188; Reactive blue 189; Reactive blue 206; Reactive blue 208; Reactive blue 246; Reactive blue 247; Reactive blue 258; Reactive blue 261 ; Reactive blue 262; Reactive blue 263; and Reactive blue 172.

The dyes are listed according to Colour Index (Society of Dyers and Colourists/American Association of Textile Chemists and Colorists) classification.

Protease Enzyme

Protease enzymes hydrolyse bonds within peptides and proteins, in the laundry context this leads to enhanced removal of protein or peptide containing stains. Examples of suitable proteases families include aspartic proteases; cysteine proteases; glutamic proteases; aspargine peptide lyase; serine proteases and threonine proteases. Such protease families are described in the MEROPS peptidase database

(http://merops.sanger.ac.uk/). Serine proteases are preferred. Subtilase type serine proteases are more preferred. The term "subtilases" refers to a sub-group of serine protease according to Siezen et al., Protein Engng. 4 (1991 ) 719-737 and Siezen et al. Protein Science 6 (1997) 501 -523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.

Examples of subtilases are those derived from Bacillus such as Bacillus lentus, B.

alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and WO09/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in

(WO93/18140). Other useful proteases may be those described in W092/175177, WO01/016285, WO02/026024 and WO02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO89/06270, W094/25583 and WO05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO05/052161 and WO05/052146.

Further Examples of useful proteases are the variants described in: W092/19729, WO96/034946, WO98/201 15, WO98/201 16, WO99/01 1768, WO01/44452,

WO03/006602, WO04/03186, WO04/041979, WO07/006305, W01 1/036263, W01 1/036264, especially the variants with substitutions in 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, 1 18, 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 the BPN' numbering. More preferred the subtilase variants may comprise the mutations: S3T, V4I, S9R, A15T, K27R, ^*36D, V68A, N76D, N87S,R, ^*97E, A98S, S99G,D,A, S99AD, S101 G,M,R S103A, V104I,Y,N, S106A, G1 18V,R, H 120D,N, N123S, S128L, P129Q, S130A, G160D, Y167A, R170S, A194P, G195E, V199M, V205I, L217D, N218D, M222S, A232V, K235L, Q236H, Q245R, N252K, T274A (using BPN' numbering).

Most preferably the protease is a subtilisins (EC 3.4.21.62).

(WO93/18140). Preferably the subsilisin is derived from Bacillus, preferably Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii as described in US 6,312,936 Bl, US 5,679,630, US 4,760,025, US7,262,042 and WO09/021867. Most preferably the subtilisin is derived from Bacillus gibsonii or Bacillus Lentus. Suitable commercially available protease enzymes include those sold under the trade names names Alcalase®, Blaze®; DuralaseTm, DurazymTm, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®,

Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase® and Esperase® all could be sold as Ultra® or Evity® (Novozymes A/S). Those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Properase®, Purafect®, Purafect Prime®, Purafect Ox®, FN3®, FN4®, Excellase® and Purafect OXP® by Genencor International. Those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect Prime®, PreferenzTm, Purafect MA®, Purafect Ox®, Purafect OxP®,

Puramax®, Properase®, EffectenzTm, FN2®, FN3® , FN4®, Excellase®, Opticlean® and Optimase® (Danisco/DuPont), Axapem™ (Gist-Brocases N.V.), Those available from Henkel/ Kemira, namely BLAP (sequence shown in Figure 29 of US 5,352,604 with the following mutations S99D + SIOI R + S103A + V104I + G159S, hereinafter referred to as BLAP), BLAP R (BLAP with S3T + V4I + V199M + V205I + L217D), BLAP X (BLAP with S3T + V4I + V205I) and BLAP F49 (BLAP with S3T + V4I + A194P + V199M + V205I + L217D) - all from Henkel/Kemira; and KAP (Bacillus alkalophilus subtilisin with mutations A230V + S256G + S259N) from Kao.

Further Enzymes

One or more further enzymes are preferred present in a laundry composition of the invention and when practicing a method of the invention.

Preferably the level of each enzyme in the laundry composition of the invention is from 0.0001 wt% to 0.1 wt% protein. Preferably the further enzyme is selected from: alpha-amylases; lipases; and, cellulases, preferably a protease.

Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa (T. lanuginosus) as described in EP 258 068 and EP 305 216 or from H. insolens as described in

WO 96/13580, a Pseudomonas lipase, e.g. from P. alcaligenes or

P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri

(GB 1 ,372,034), P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), a Bacillus lipase, e.g. from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Acta, 1 131 , 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).

Other examples are lipase variants such as those described in WO 92/05249,

WO 94/01541 , EP 407 225, EP 260 105, WO 95/35381 , WO 96/00292,

WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and

WO 97/07202, WO 00/60063.

Preferred commercially available lipase enzymes include Lipolase™ and Lipolase Ultra™, Lipex™ and Lipoclean™(Novozymes A/S).

The method of the invention may be carried out in the presence of phospholipase classified as EC 3.1 .1 .4 and/or EC 3.1 .1.32. As used herein, the term phospholipase is an enzyme which has activity towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1 ) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol. Phospholipases are enzymes which participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases Ai and A2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B) which can hydrolyze the remaining fatty acyl group in lysophospholipid.

Phospholipase C and phospholipase D (phosphodiesterases) release diacyl glycerol or phosphatidic acid respectively.

The method of the invention may be carried out in the presence of cutinase classified in EC 3.1.1 .74. The cutinase used according to the invention may be of any origin.

Preferably cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.

Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin.

Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g. a special strain of

B. lichen iformis, described in more detail in GB 1 ,296,839, or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060. Commercially available amylases are Duramyl™, Termamyl™, Termamyl Ultra™, Natalase™, Stainzyme™, Fungamyl™ and BAN™ (Novozymes A S), Rapidase™ and Purastar™ (from Genencor International Inc.).

Suitable cellulases include those 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. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307.

Commercially available cellulases include Celluzyme™, Carezyme™, Celluclean™,

Endolase™, Renozyme™ (Novozymes A/S), Clazinase™ and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation). Celluclean™ is preferred.

Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin.

Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.

Commercially available peroxidases include Guardzyme™ and Novozym™ 51004 (Novozymes A/S).

Further enzymes suitable for use are discussed in WO2009/087524, WO2009/090576, WO2009/107091 , WO2009/1 1 1258 and WO2009/148983.

Enzyme Stabilizers

Any enzyme present in the composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708.

Where alkyl groups are sufficiently long to form branched or cyclic chains, the alkyl groups encompass branched, cyclic and linear alkyl chains. The alkyl groups are preferably linear or branched, most preferably linear. The indefinite article "a" or "an" and its corresponding definite article "the" as used herein means at least one, or one or more, unless specified otherwise.

Experimental

Example 1

An aqueous liquid laundry detergent was prepared of the following formulation:

The formulation was used to wash eight 5x5cm EMPA 1 17 stain monitor (blood/milk/ink stain on polycotton) in a tergotometer set at 200rpm. A 20 minute wash was conducted in 800ml of 26o French Hard water at 25oC, with 2.3g/L of the formulation. To simulate oily soil (7.2g) of an SBL2004 soil strip (ex Warwick Equest) was added to the wash liquor.

Once the wash had been completed the cotton monitors were rinsed once in 400ml clean water, removed dried and the colour measured on a reflectometer and expressed as the CIE L^*a^*b^* values.

Equivalent Formulations but with the addition of 8.7 wt% of the ASP dispersant (n = 20):

Experiments were repeated with and without the addition of a subtilisin serine protease ((EC no. 232-752-2) to the wash liquor (Evity® 16L ex Novozymes). The enzyme was added to give 0.009 wt % pure active protein to the formulation.

95% confidence limits are also given calculated from the standard deviation on the measurements from the 8 monitors.

Once the wash had been completed the cotton monitors were rinsed once in 400ml clean water, removed dried and the colour measured on a reflectometer and expressed as the CIE L^*a^*b^* values. The cleaning anti-redeposition benefit was expressed as the AL value:

AL = L(dispersant)- L(control)

The larger the AL value the greater the prevention of deposition of the carbon black soil. 95% confidence limits based on the 8 separate cotton monitors were calculated.

Formulations were made with and without the addition of 8.7wt% of the dispersant:

The cleaning benefit was expressed as the AL value:

AL = L(test)- L(control)

The larger the AL value the greater the prevention of deposition of the carbon black soil test AL 95%

Protease 1.55 0.60

ASP dispersant 1.32 0..41

Protease + ASP dispersant 4.05 0.44 The ASP dispersant alone and the protease alone enhance stains removal. A further increase is seen when the 2 are combined and ΔΙ_= 4.05 is larger than expected by summing the individual performance, 1 .55 + 1.32 = 2.88.

Claims

1. A laundry detergent composition comprising:

(i) from 0.5 to 20 wt% of an alkoxylated substituted phenol dispersant of the following structure:

wherein

X is selected from: ethoxy; and, mixtures of ethoxy and propoxy groups where the number of ethoxy groups is greater than the number of propoxy groups, and wherein n is from 6 to 70;

Y is selected from: Ri ; ORi , COOR_5; F; CI; Br; I; CN; and N0₂, wherein Ri is a C1 to C4 linear or branched alkyl group and Rs is selected from C1 to C18 linear or branched alkyl groups;

R2 and R3 are selected from: C1 to C3 linear or branched alkyl aryl groups; and, aryl groups;

T is selected from: H; CH₃; S0₃ ^"; CH₂COO^"; PO3^2"; C₂H₅; n-propyl, i-propyl; n- butyl; t-butyl; and, sulfosuccinate;

(ii) from 0 to 50 wt% surfactant, other than the alkoxylated substituted phenol; and,

(iii) from 0.0005 to 0.2 wt% of a protease enzyme.

2. A laundry detergent composition according to claim 1 , wherein R2 and R3 are selected from styryl and cumyl,

3. A laundry detergent composition according to claim 1 , wherein R2 and R3 are styryl and both R2 and R3 are in the ortho position to the -0-[X]_n-T group.

4. A laundry detergent composition according to claim 1 , 2 or 3, wherein X is ethoxy.

5. A laundry detergent composition according to any one of the preceding claims, wherein n is from 8 to 34.

6. A laundry detergent composition according to any one of the preceding claims, wherein the surfactant is selected from: anionic and non-ionic surfactants and the level of surfactant is from 4 to 40 wt%.

7. A laundry detergent composition according to any one of the preceding claims, wherein the weight fraction of non-ionic surfactant/anionic surfactant is from 0 to 0.3.

8. A laundry detergent composition according claim 6 or 7, wherein the anionic

surfactant is selected from: linear alkyl benzene sulphonates; alkyl sulphates; and, alkyl ether sulphates; and mixtures thereof.

9. A laundry detergent composition according to any one of the preceding claims, wherein the level of the alkoxylated substituted phenol dispersant from 1 to 10 wt%.

10. A laundry detergent composition according to any one of the preceding claims, wherein T is H.

1 1 . A laundry detergent composition according to any one of the preceding claims, wherein the Y is selected from: methyl; ethyl; methoxy; and, ethoxy.

12. A laundry detergent composition according to claim 1 , wherein the the alkoxylated substituted phenol dispersant is:

and the protease enzyme is a subtilisin (EC 3.4.21.62).

13. A laundry detergent composition according to any one of the preceding claims, wherein n is selected from: 14; 15; 16; 17; 18; 19; 20; 21 ; 22; 23; 24; 25; 26; 27; 28; 29; 30; 31 ; and, 32.

14. A domestic method of treating a textile, the method comprising the steps of:

(i) treating a textile with an aqueous solution of the alkoxylated substituted

phenol dispersant the aqueous solution comprising from 10 ppm to 5000 ppm of the alkoxylated substituted phenol dispersant as defined in any one of the preceding claims; from 0.01 to 1 ppm of a protease enzyme; and, 0 to 6 g/L of a surfactant, other than the alkoxylated substituted phenol dispersant; and,

(ii) optionally rinsing and drying the textile.

15. A domestic method of treating a textile according to claim 14 wherein in the method the protease enzyme is a subtilisin (EC 3.4.21 .62).