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Title:
DETERGENT COMPOSITIONS
Document Type and Number:
WIPO Patent Application WO/2020/260006
Kind Code:
A1
Abstract:
The invention concerns a detergent composition product, comprising from 1 to 95 wt.%, preferably from 2 to 50 wt.%, more preferably from 4 to 40 wt.%, most preferably from 6 to 25 wt.% of surfactant; wherein the surfactants used are saturated or mono-unsaturated; and, wherein the surfactant comprises only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used; to a method of reducing the environmental impact as measured by arable land use and greenhouse gas production of one or more detergent composition products; to a domestic method of treating a textile, and to the use of rapeseed oil in a surfactant comprising only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used, to reduce the environmental impact of said surfactant as measured by arable land use and greenhouse gas production.

Inventors:
BATCHELOR STEPHEN (GB)
Application Number:
EP2020/065904
Publication Date:
December 30, 2020
Filing Date:
June 09, 2020
Export Citation:
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Assignee:
UNILEVER PLC (GB)
UNILEVER NV (NL)
CONOPCO INC D/B/A UNILEVER (US)
International Classes:
C11D1/00; C11D3/00; C11D11/00
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Attorney, Agent or Firm:
MCHUGH, Paul, Edward (NL)
Download PDF:
Claims:
CLAIMS

1. A detergent composition product, preferably a laundry detergent composition

product, more preferably a liquid laundry composition, comprising from 1 to 95 wt.%, preferably from 2 to 50 wt.%, more preferably from 4 to 40 wt.%, most preferably from 6 to 25 wt.% of surfactant;

wherein the surfactants used are saturated or mono-unsaturated; and,

wherein the surfactant comprises only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used.

2. A detergent composition according to claim 1 , wherein the surfactant comprises only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 40 to 71 wt.%, of the total plant oil used.

3. A detergent composition according to claim 1 or claim 2, wherein the surfactants are selected from: anionic, nonionic or amphoteric surfactants and mixtures thereof.

More preferably the surfactant comprises anionic and/or nonionic surfactants.

4. A detergent composition according to any preceding claim, comprising from 0.5 to 20 wt.%, preferably from 2 to 12 wt.%, more preferably from 2 to 6 wt.%, most preferably from 2 to 5 wt.% of nonionic surfactants, wherein the nonionic surfactant is selected from saturated and mono-unsaturated aliphatic alcohol ethoxylate, preferably selected from Ci6 to Cis with a mole average of from 5 to 25 ethoxylates.

5. A detergent composition according to any preceding claim, comprising from 0.5 to 20 wt.%, more preferably from 1 to 16 wt.%, even more preferably from 1.5 to 14 wt.%, most preferably from 2 to 12 wt.% of anionic surfactant, wherein the anionic surfactant is selected from C16 and/or C18 ether sulfate with mole average of 5 to 20 ethoxylate groups; citric acid ester of a C16 to C18 monoglyceride (citrem), tartartic acid esters of a C16 to C18 monoglyceride (tatem) and diacetyl tartaric acid ester of a C16 to C18 monoglyceride (datem).

6. A detergent composition according to any preceding claim, wherein the composition comprises from 0.5 to 15 wt.%, more preferably from 0.75 to 15 wt.%, even more preferably from 1 to 12 wt.%, most preferably from 1.5 to 10 wt.% of cleaning boosters selected from antiredeposition polymers, soil release polymers, alkoxylated polycarboxyl ic acid esters and mixtures thereof.

7. A detergent composition according to claim 6, wherein the antiredeposition polymers are alkoxylated polyamines; and/or the soil release polymer is a polyester soil release polymer.

8. A detergent composition according to any preceding claim, wherein the composition comprises one or more enzymes from the group: lipases, proteases, alpha-amylases, cellulases, peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof, preferably lipases, proteases, alpha-amylases, cellulases and mixtures thereof, wherein the level of each enzyme in the composition of the invention is from 0.0001 wt.% to 0.1 wt.%.

9. A method of reducing the environmental impact as measured by arable land use and greenhouse gas production of one or more detergent composition products, the method comprising:

(a) replacement of a surfactant from said detergent composition products with alkyl chains derived from the triglycerides of a plant oil, selected from palm oil, soybean oil or a mixture thereof; with,

(b) a surfactant comprising only alkyl chains derived from the triglycerides of a

mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used.

10. A domestic method of treating a textile, the method comprising the step of: treating a textile with an aqueous solution of 0.5 to 20 g/L of a detergent composition according to any one of claims 1 to 8.

11. Use of rapeseed oil in a surfactant comprising only alkyl chains derived from the

triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used, to reduce the environmental impact of said surfactant as measured by arable land use and greenhouse gas production.

Description:
DETERGENT COMPOSITIONS

Field of Invention

The present invention concerns a detergent composition.

Background of the Invention

Surfactants typically consist of a branched or linear C10 to C20 alkyl chain attached to a water solubilising group such as sulphate, ethoxylate, ether carboxylate, ether sulphate.

Many consumers want to use detergent products that are derived from plants, in this respect the alkyl chain of the surfactant should be obtained from plant oils.

There are a multitude of oil producing plants with the major plant oils in global production being palm oil, soybean oil, rapeseed oil, sunflower oil and peanut oil. The main alkyl chain found in plant oils are linear C16 and C18 chains.

The production of plant oils produces greenhouse gases and it is desired to miminise the greenhouse gases produced by human activity. The production of plant oils requires arable land. Arable land is land capable of being ploughed and used to grow crops. The amount of arable land on earth is limited and therefore use for non-food purposes should be minimised. Palm oil is currently used as the major source of plant oil for producing alkyl chains for surfactant.

It is desired to find a solution to the problem of how to find plant oils that minimise both the environmental impact of arable land use and greenhouse gas production.

Surprisingly, this problem can be solved by using surfactants with alkyl chains derived from a mixture of oils, which are selected from rapeseed oil, palm oil and soybean oil.

Summary of the Invention

The invention relates to a detergent composition product, preferably a laundry detergent composition product, more preferably a liquid laundry composition, comprising from 1 to 95 wt.%, preferably from 2 to 50 wt.%, more preferably from 4 to 40 wt.%, most preferably from 6 to 25 wt.% of surfactant;

wherein the surfactants used are saturated or mono-unsaturated; and, wherein the surfactant comprises only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used.

Preferably the surfactants are selected from: anionic, nonionic or amphoteric surfactants and mixtures thereof. More preferably the surfactant comprises anionic and/or nonionic surfactants.

Preferably the nonionic surfactant is saturated and mono-unsaturated aliphatic alcohol ethoxylate, preferably selected from Ci 6 to Cis with a mole average of from 5 to 25 ethoxylates. Preferably the total amount of nonionic surfactants in a composition of the invention ranges from 0.5 to 20 wt.%, more preferably from 2 to 12 wt.%, even more preferably from 2 to 6 wt.%, most preferably from 2 to 5 wt.%.

Preferably the anionic surfactant is selected from C16 and/or C18 ether sulfate with mole average of 5 to 20 ethoxylate groups; citric acid ester of a C16 to C18 monoglyceride (citrem), tartartic acid esters of a C16 to C18 monoglyceride (tatem) and diacetyl tartaric acid ester of a C16 to C18 monoglyceride (datem). Preferably the total amount of anionic surfactant in a composition of the invention ranges from 0.5 to 20 wt.%, more preferably from 1 to 16 wt.%, even more preferably from 1.5 to 14 wt.%, most preferably from 2 to 12 wt.%.

Preferably the detergent composition comprises from 0.5 to 15 wt.%, more preferably from 0.75 to 15 wt.%, even more preferably from 1 to 12 wt.%, most preferably from 1.5 to 10 wt.% of cleaning boosters selected from antiredeposition polymers, soil release polymers, alkoxylated polycarboxylic acid esters and mixtures thereof.

Preferably the antiredeposition polymers are alkoxylated polyamines; and/or the soil release polymer is a polyester soil release polymer.

Preferably the composition comprises one or more enzymes from the group: lipases proteases, alpha-amylases, cellulases, peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof, more preferably lipases, proteases, alpha-amylases, cellulases and mixtures thereof, wherein the level of each enzyme in the composition of the invention is from 0.0001 wt.% to 0.1 wt.%. In a second aspect the invention provides a method of reducing the environmental impact as measured by arable land use and greenhouse gas production of one or more detergent composition products, the method comprising:

(a) replacement of a surfactant from said detergent composition products with alkyl chains derived from the triglycerides of a plant oil, selected from palm oil, soybean oil or a mixture thereof; with,

(b) a surfactant comprising only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used.

In a third aspect the invention provides a domestic method of treating a textile, the method comprising the step of: treating a textile with an aqueous solution of 0.5 to 20 g/L of a detergent composition as defined in the first aspect of the invention.

In a fourth aspect the invention provides the use of rapeseed oil in a surfactant comprising only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used, to reduce the environmental impact of said surfactant as measured by arable land use and greenhouse gas production.

Detailed Description of the Invention

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.

All enzyme levels refer to pure protein. wt.% relates to the amount by weight of the ingredient based on the total weight of the composition. For anionic charged surfactants wt.% is calculated based on the protonated form of the surfactant.

The values of n and m where used are the mole average values. The invention relates to a detergent composition product, preferably a laundry detergent composition product, more preferably a liquid laundry composition, comprising from 1 to 95 wt.%, preferably from 2 to 50 wt.%, more preferably from 4 to 40 wt.%, most preferably from 6 to 25 wt.% of surfactant;

wherein the surfactants used are saturated or mono-unsaturated; and,

wherein the surfactant comprises only alkyl chains derived from the triglycerides of a mixture of plant oils, selected from palm oil, soybean oil and rapeseed oil, wherein rapeseed oil is from 13 to 99 wt.%, preferably 27 to 84 wt.%, most preferably 40 to 71 wt.%, of the total plant oil used.

Plant oils

Plant oils are discussed in Food chemistry by H.-D. Belitz, W. Grosch and P. Schieberle (3 rd edition Springer 2004). Rapeseed oil is the oil obtained from seeds of cuiltivars of

Brassicaceae, for example Brassica napus, Brassica juncea, Brassica rapa and includes high and low erucic acids cultivars. Palm oil is the oil obtained from palm kernel and palm fruit of palms trees, preferably Elaeis guiineensis, Cocos nucifera and Orbignya speciose, more preferably Elaeis guiineensis, most preferably the oil extracted from the fruit of Elaeis guiineensis. Soybean oil is the oil extracted from the bean of cultivars of Glycine Max.

Most preferably the mixture of oils is selected from a mixture of rapeseed oil and palm oil, or a mixture of rapeseed oil and soybean oil.

Surfactants

Oils are preferably hydrogenated before use for surfactant synthesis, so that the level of polyunsaturated oil is less than 1wt%.

Surfactants derived from the triglyceride of plant oil may be obtained in a variety of ways, preferably selected from

(i) Hydrolysis of the triglyceride to the fatty acids, followed by reduction to the fatty alcohol and reaction with a suitable surfactant head group, preferably to form surfactants selected from: fatty alcohol ethoxylates; alkyl ether sulfates; alkyl ether carboxylates;

(ii) Partial hydrolysis of the triglyceride to from monoglyceride and diglycerides

followed by the reaction of the monoglyceride and diglyceride with a suitable surfactant head group, preferably to form surfactants preferably selected from Organic acid ester derivatives of mono- glyceride and diglycerides. Surfactants are discussed in Anionic Surfactants edited by H. Stache (Surfactant Science Series Volume 56, Dekker) and Non-ionic Surfactants edited by M.J. Schick (Surfactant Science Series Volume 1 , Dekker). Organic acid ester derivatives of mono- glycerides and diglycerides are discussed in Hasenhuettl, G.L and Hartel, R.W. (Eds) Food Emulsifiers and Their Application, 2008 (Springer); and in Whitehurst, R.J. (Ed) Emulsifiers in Food

Technology 2008 (Wiley-VCH) and in the 2nd edition of this book edited by V. Norn 2015 (Wiley-Blackwell).

Preferably the surfactants used have C16, C18 chains, most preferably where C18 chains are at least 70 wt.% of the mix.

Preferably the detergent composition products are classified as detergent compositions for home and personal care use, more preferably home care, most preferably a domestic detergent composition for cleaning clothes and household textiles.

Preferably the detergent composition is a laundry composition. Said composition may be in any form for example a liquid, solid, powder, liquid unit dose. Preferably the composition is a liquid composition, for example a liquid laundry composition.

Detergent Compositions

If a laundry composition, then preferably the formulation when dissolved in demineralised water at 20°C has a pH of 3 to 10, more preferably from 4 to 8, even more preferably 6.5 to 7.5, most preferably 7.

Preferred Detergent Composition Ingredients

Anionic surfactant

Any anionic surfactant may be used. However preferred surfactants are described below.

Examples of suitable anionic detergent compounds are selected from C16 and/or C18 ether sulfate with mole average of 5 to 20 ethoxylate groups; citric acid ester of a C16 to C18 monoglyceride (citrem), tartartic acid esters of a C16 to C18 monoglyceride (tatem) and diacetyl tartaric acid ester of a C16 to C18 monoglyceride (datem); and mixtures thereof. Citrem, tatem and datem are described in Hasenhuettl, G.L and Hartel, R.W. (Eds) Food Emulsifiers and Their Application. 2008 (Springer) and in Whitehurst, R.J. (Ed) Emulsifiers in Food Technology 2008 (Wiley-VCH).

Most preferably, the anionic surfactant comprises C16 and/or C18 ether sulfate with mole average of 5 to 20 ethoxylate groups; C16 to C18 alkyl ether carboxylates; citric acid ester of a C16 to C18 monoglyceride (citrem), tartartic acid esters of a C16 to C18 monoglyceride (tatem) and diacetyl tartaric acid ester of a C16 to C18 monoglyceride (datem).

Preferably the total amount of anionic surfactant in a composition of the invention ranges from 0.5 to 20 wt.%, more preferably from 1 to 16 wt.%, even more preferably from 1.5 to 14 wt.%, most preferably from 2 to 12 wt.%.

Preferably the surfactants used are saturated or mono-unsaturated. Preferably the alkyl chains are derived from natural sources.

Nonionic surfactant

Any nonionic surfactant may be used, however, preferred nonionic surfactants are described below.

Nonionic surfactants are preferably selected from saturated and mono-unsaturated aliphatic alcohol ethoxylates.

Preferably the nonionic surfactant is saturated and mono-unsaturated aliphatic alcohol ethoxylate, preferably Cie to Cie with an average of from 5 to 25 ethoxylates. Preferably the alkyl chain is mono-unsaturated.

Mixtures of any of the above described materials may also be used.

Preferably the total amount of nonionic surfactants in a composition of the invention ranges from 0.5 to 20 wt.%, more preferably from 2 to 12 wt.%, even more preferably from 2 to 6 wt.%, most preferably from 2 to 5 wt.%.

Amphoteric surfactant

Amphoteric surfactant my be present or absent. Amphoteric surfactants preferably include betaines, more preferably cocoamidopropyl betaine. Preferably the amphoteric surfactant is present at a level of from 0.1 to 10 wt.%, preferably 0.25 to 8 wt.%, more preferably 0.5 to 6 wt.%.

Cleaning Boosters

The composition preferably comprises from 0.5 to 15 wt.%, more preferably from 0.75 to 15 wt.%, even more preferably from 1 to 12 wt.%, most preferably from 1.5 to 10 wt.% of cleaning boosters selected from antiredeposition polymers; soil release polymers;

alkoxylated polycarboxylic acid esters as described in WO/2019/008036 and

WO/2019/007636; and mixtures thereof.

Antiredeposition polymers

Preferred antiredeposition polymers include alkoxylated polyamines.

A preferred alkoxylated polyamine comprises an alkoxylated polyethylenimine, and/or alkoxylated polypropylenimine. The polyamine may be linear or branched. It may be branched to the extent that it is a dendrimer. The alkoxylation may typically be ethoxylation or propoxylation, or a mixture of both. Where a nitrogen atom is alkoxylated, a preferred average degree of alkoxylation is from 10 to 30, preferably from 15 to 25. A preferred material is ethoxylated polyethyleneimine, with an average degree of ethoxylation being from 10 to 30 preferably from 15 to 25, where a nitrogen atom is ethoxylated.

Soil release polymer

Preferably the soil release polymer is a polyester soil release polymer.

Preferred soil release polymers include those described in WO 2014/029479 and WO 2016/005338.

Preferably the polyester based soil release polymer is a polyester according to the following formula (I)

wherein R 1 and R 2 independently of one another are X-(OC 2 H 4 ) n -(OC 3 H 6 ) m wherein X is C 1-4 alkyl and preferably methyl, the -(OC 2 H 4 ) groups and the -(OC 3 H 6 ) groups are arranged blockwise and the block consisting of the -(OC3H6) groups is bound to a COO group or are HO-(C 3 H 6 ), and preferably are independently of one another X- (OC 2 H4)n-(OC 3 H6)m,

n is based on a molar average number of from 12 to 120 and preferably of from 40 to 50,

m is based on a molar average number of from 1 to 10 and preferably of from 1 to 7, and

a is based on a molar average number of from 4 to 9.

Preferably the polyester provided as an active blend comprising:

A) from 45 to 55 % by weight of the active blend of one or more polyesters according to the following formula (I)

wherein

R 1 and R 2 independently of one another are X-(OC 2 H 4 ) n -(OC 3 H 6 ) m wherein X is C 1-4 alkyl and preferably methyl, the -(OC 2 H 4 ) groups and the -(OC 3 H 6 ) groups are arranged blockwise and the block consisting of the -(OC3H6) groups is bound to a COO group or are HO-(C 3 H 6 ), and preferably are independently of one another X- (OC 2 H4)n-(OC 3 H6)m,

n is based on a molar average number of from 12 to 120 and preferably of from 40 to 50,

m is based on a molar average number of from 1 to 10 and preferably of from 1 to 7, and

a is based on a molar average number of from 4 to 9 and

B) from 10 to 30 % by weight of the active blend of one or more alcohols selected from the group consisting of ethylene glycol, 1 ,2-propylene glycol, 1 ,3-propylene glycol, 1 ,2-butylene glycol, 1 ,3-butylene glycol, 1 ,4-butylene glycol and butyl glycol and

C) from 24 to 42 % by weight of the active blend of water. Alkoxylated polycarboxylic acid esters

Alkoxylated polycarboxylic acid esters are obtainable by first reacting an aromatic polycarboxylic acid containing at least three carboxylic acid units or anhydrides derived therefrom, preferably an aromatic polycarboxylic acid containing three or four carboxylic acid units or anhydrides derived therefrom, more preferably an aromatic polycarboxylic acid containing three carboxylic acid units or anhydrides derived therefrom.

Enzymes

Preferably enzymes, such as lipases, proteases, alpha-amylases, cellulases,

peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof, may be present in the formulation.

If enzymes are present, then preferably they are selected from: lipases, proteases, alpha- amylases, cellulases and mixtures thereof.

If present, then the level of each enzyme in the laundry composition of the invention is from 0.0001 wt.% to 0.1 wt.%.

Levels of enzyme present in the composition preferably relate to the level of enzyme as pure protein.

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, 1131 , 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 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.

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 W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD138 described in (WO 93/18140). Other useful proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 05/052161 and WO 05/052146.

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

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 W009/021867, 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). 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 WO 09/021867. 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).

The invention may use 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. licheniformis, 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 WO 2009/087524, WO 2009/090576, WO 2009/107091 , WO 2009/111258 and WO 2009/148983.

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.

Further Ingredients

The formulation may contain further ingredients.

Builders or Complexing Agents

The composition may comprise a builder or a complexing agent.

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.

The composition may also contain 0-10 wt.% of a builder or complexing agent such as ethylenediaminetetraacetic acid, diethylenetriamine-pentaacetic acid, citric acid, alkyl- or alkenylsuccinic acid, nitrilotriacetic acid or the other builders mentioned below.

More preferably the laundry detergent formulation is a non-phosphate built laundry detergent formulation, i.e., contains less than 1 wt.% of phosphate. Most preferably the laundry detergent formulation is not built i.e. contain less than 1 wt.% of builder.

If the detergent composition is an aqueous liquid laundry detergent it is preferred that mono propylene glycol or glycerol 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.

The total amount of the fluorescent agent or agents used in the composition is generally from 0.0001 to 0.5 wt.%, preferably 0.005 to 2 wt.%, more preferably 0.01 to 0.1 wt.%.

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 fluorescers with CAS-No 3426-43-5; CAS-No 35632-99-6; CAS-No 24565-13-7; CAS-No 12224-16-7; CAS-No 13863-31-5; CAS-No 4193-55-9; CAS-No 16090- 02-1 ; CAS-No 133-66-4; CAS-No 68444-86-0; CAS-No 27344-41-8.

Most preferred fluorescers are: sodium 2 (4-styryl-3-sulfophenyl)-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' disulphonate, 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.

Shading dye

It is advantageous to have shading dye present in the formulation.

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), Wley-VCH Weinheim 2003).

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 .

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

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

Blue or violet Shading dyes are most preferred. 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 260 to 320, most preferably 270 to 300. The white cloth used in this test is bleached non-mercerised woven cotton sheeting.

Shading dyes are discussed in W02005/003274, W02006/032327(Uni lever),

W02006/032397(Unilever), W02006/045275(Unilever), WO 2006/027086(Unilever), W02008/017570(Unilever), WO 2008/141880(Unilever), W02009/132870(Uni lever),

WO 2009/141173 (Unilever), WO 2010/099997(Unilever), WO 2010/102861 (Unilever), WO 2010/148624(Unilever), W02008/087497 (P&G), WO2011/011799 (P&G), W02012/054820 (P&G), WO2013/142495 (P&G) and W02013/151970 (P&G), W02018/085211 (P&G), and WO2019/075149 (P&G).

A mixture of shading dyes may be used. The shading dye chromophore is most preferably selected from mono-azo, bis-azo and azine.

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 WO2013/142495 and W02008/087497. A preferred example of a thiophene dye is 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 11 , 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 W02012/054058 and WO/2010/151906.

An example of an alkoxylated bis-azo dye is :

Azine dyes 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:

X 3 is selected from: -H; -F; -CH 3 ; -C 2 H 5 ; -OCH 3 ; and, -OC 2 H 5 ; X4 is selected from: -H; -CH3; -C2H5; -OCH3; and, -OC2H5;

Y 2 is selected from: -OH; -OCH2CH2OH; -CH(OH)CH 2 OH; -0C(0)CH 3 ; and, C(0)0CH 3. Anthraquinone dyes covalently bound to ethoxylate or propoxylated polyethylene imine may be used as described in WO2011/047987 and WO 2012/119859.

The shading dye is preferably present is present in the composition in range from 0.0001 to 0.1wt %. 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 preferably a blue or violet shading dye.

Perfume

The composition preferably comprises a perfume. 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 Flavour Ingredients, 1975, CRC Press; Synthetic Food Adjuncts, 1947 by M. B. Jacobs, edited by Van Nostrand; or Perfume and Flavour 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 (perfumes) in 2011. (http://www.ifraorg.Org/en-us/ingredients#.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), poly(vinyl alcohol), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid

copolymers.

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.

Enzymes

Preferably enzymes, such as lipases, proteases, alpha-amylases, cellulases,

peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof, may be present in the formulation.

If further enzymes are present, then preferably they are selected from: lipases, proteases, alpha-amylases, cellulases and mixtures thereof. If present, then the level of each enzyme in the laundry composition of the invention is from

O.0001 wt.% to 0.1 wt.%.

Levels of enzyme present in the composition preferably relate to the level of enzyme as pure protein.

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, 1131 , 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 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.

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 W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD138 described in (WO 93/18140). Other useful proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 05/052161 and WO 05/052146.

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

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 W009/021867, 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). 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 WO 09/021867. 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).

The invention may use 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. licheniformis, 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 WO 2009/087524, WO 2009/090576, WO 2009/107091 , WO 2009/111258 and WO 2009/148983.

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.

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

Adjunct Ingredients

The detergent compositions optionally include one or more laundry adjunct ingredients.

To prevent oxidation of the formulation an anti-oxidant may be present in the formulation.

The term "adjunct ingredient" includes: perfumes, dispersing agents, stabilizers, pH control agents, metal ion control agents, colorants, brighteners, dyes, odour control agent, pro perfumes, cyclodextrin, perfume, solvents, soil release polymers, preservatives,

antimicrobial agents, chlorine scavengers, anti-shrinkage agents, fabric crisping agents, spotting agents, anti-oxidants, anti-corrosion agents, bodying agents, drape and form control agents, smoothness agents, static control agents, wrinkle control agents, sanitization agents, disinfecting agents, germ control agents, mould control agents, mildew control agents, antiviral agents, antimicrobials, drying agents, stain resistance agents, soil release agents, malodour control agents, fabric refreshing agents, chlorine bleach odour control agents, dye fixatives, dye transfer inhibitors, shading dyes, colour maintenance agents, colour restoration, rejuvenation agents, anti-fading agents, whiteness enhancers, anti-abrasion agents, wear resistance agents, fabric integrity agents, anti-wear agents, and rinse aids, UV protection agents, sun fade inhibitors, insect repellents, anti-allergenic agents, enzymes, flame retardants, water proofing agents, fabric comfort agents, water conditioning agents, shrinkage resistance agents, stretch resistance agents, and combinations thereof. If present, such adjuncts can be used at a level of from 0.1% to 5% by weight of the composition.

Example

Experimental

Values obtained for Craddle to Gate determination of Green House Gases and Land occupation are given in the following table, according to J. Schmidt in Journal of Cleaner Production 87 (2015) 130-138.

kg CO2 eq per metric tonne of oil includes biogenic CO2 uptake and indirect Land Use Changes.

The principles and framework for life cycle assessment is given in ISO 14040 and

I S014044.

Craddle to Gate determination of Green House Gases are in kg CO2 equivalent per metric tonne of oil.

Biogenic CO2 uptake and indirect Land Use Changes is included.

Land occupation is the amount of arable land in m 2 /year required to plant crop that would produce 1 tonne of oil using the same farming processes as for the Craddle to Gate determination of carbon dioxide.

Soybean oil has the same values as palm oil because soybeans are primarily produced for protein and the oil is a secondary product. Therefore, if more soybean oil is required it will not lead to a change in supply, as the protein demand controls supply.

Instead an increased demand for soybean oil will be compensated by the biggest production oil, which is Palm.

For comparison the values are normalised to Palm Oil.

The Impact average value given is the root mean square of the Normalised CO2 eq and Normalised Land occupation. The impact average (IA) for mixtures of Palm and Rapeseed oil were computed and are given in the following table, where %RS is the weight percent of rapeseed oil in the mix.

Surprisingly the Impact Average (IA) is lower for the mixture of oils than for either oil alone (Palm oil 1.4142, Rapeseed oil 1.3762), as indicated by the values in italics when the %RS (% Rapeseed Oil) is between 38 to 99%.

The minimum Impact Average (IA) of 1.3112 is found at an %RS of 56%. Minima were not found in mixes of Palm with Sunflower oil, or Palm with Peanut oil.