Aqueous liquid cleaning compositions and their use

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An isotropic aqueous liquid detergent composition comprising: a succinate dimer surfactant selected from alkyl and alkenyl succinate dimers in which two succinic acid moieties or derivatives thereof are joined by a (poly)alkyleneoxy bridge and each carboxylic acid group is independently in the free acid form, salt form or is esterified or is a corresponding amide group; and mixtures thereof; one or more other surfactants; and water.

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Description
FIELD OF INVENTION

The present invention relates to aqueous liquid cleaning compositions. It also relates to methods of using such compositions for the cleaning of fabrics.

BACKGROUND OF INVENTION

Aqueous liquid detergent compositions can generally be considered to fall into one of two categories, namely isotropic or structured. Structured compositions usually contain lamellar phases formed of surfactant and water, which cause them to be relatively viscous, shear thinning and often, to have solid suspending properties. Isotropic compositions, on the other hand, usually have a viscosity similar to that of water and are substantially Newtonian. In addition, consumers generally prefer isotropic compositions to be substantially transparent, or at least, translucent.

Lack of clarity in such aqueous liquid detergent compositions can be the result of a number of factors. One such factor is the formation of micellar or more ordered phases. Another cause of loss of clarity is potentially due to instability of one or more ingredients. Such instability can be due to the presence of highly reactive species, such as bleach catalysts, for example, of the type used to catalyse bleaching by atmospheric oxygen. It can also be due to species which degrade too readily. Reactive species can attack and degrade organic molecules within the formulation. An example of an ingredient of the kind which degrades very easily is enzymes.

In isotropic aqueous liquid detergent compositions, it is common to include one or more hydrotropes such as ethanol, sodium xylene sulphonate (SXS) or sodium cumene sulfonate (SCS), as well as polypropylene glycol (PPG). These materials have the function of inhibiting the formation of ordered phases and so promote the clarity of the liquid. However, they are relatively costly and do not really contribute to the leaning performance of the product.

It is also common to use organic bases to neutralise fatty acids, in order to result in the formation of a more soluble soap. Such basis are typically, monoethanolamine or triethanolamine. Using these organic bases as the cation in a soap and/or adding an organic base when a soap is present, can stabilise the formulation at low temperatures. However, these materials have the potential disadvantage of inducing colour instability at higher temperatures.

Thus, the use of hydrotropes has a cost penalty in formulation of the product. The use of organic bases as stabilisers for soap can promote instability at high temperatures.

There is therefore a need to find an alternative form of stabiliser which does not carry such a cost penalty and/or does not have disadvantages to the same degree as conventional stabilisers. To help avoid the cost penalty disadvantage, it would be helpful to utilise a stabiliser which has another useful function in the formulation. For example, if such an alternative stabiliser were a surfactant, it would contribute to the cleaning performance of the product.

We have now found that succinate dimer, optionally including derivatives thereof, surfactants may fulfil this role of detergent (surfactant) active and stabiliser.

In liquid detergent compositions, alkyl and alkenyl disuccinates have been mentioned as possible detergency builders, as disclosed in US-A-25/0124,528. Alkyl and alkenyl succinates have been disclosed as builders for liquid detergents, according to U.S. Pat. No. 5,945,394. Long chain (di)-alk(en)yl succinates have been disclosed as useful surfactant ingredients in aqueous liquid detergent compositions in many prior documents such as GB-A-2 232 420, GB-A-2 120 272, EP-A-476 212, EP-A-241 073, EP-A-212 713, EP-A-200 263, EP-A-233 306 and EP-A-028 850. These materials have also been disclosed as possible ingredients for fabric conditioner compositions, as disclosed in WO-A-99/27056.

Alkyl succinates and unsubstituted tartrate succinate builders have been described as such in EP-A-342 177.

SUMMARY OF INVENTION

A first aspect of the invention provides an isotropic aqueous liquid detergent composition comprising:

a succinate dimer surfactant as specified in claim 1; one or more other surfactants; and water.

A second aspect of the present invention provides a method of preparation of an isotropic aqueous liquid detergent composition, the method comprising admixture of water, one or more other surfactants and a succinate dimer surfactant of the invention.

A third aspect of the present invention provides use of a succinate dimer surfactant according to the present invention as a stabiliser in an isotropic aqueous liquid detergent composition, the composition also comprising one or more other surfactants and water.

DETAILED DESCRIPTION OF THE INVENTION

The Succinate Dimer Surfactant

The succinate dimer surfactant present in the composition of the invention comprises or consists of at least one compound of formula (I):

wherein in formula (I), each of R1 and R2 is independently selected from alkyl and alkenyl groups having from 8 to 18, preferably from 12 to 18, most preferably 18 carbon atoms; each of R3 and R4 is independently selected from hydrogen, groups M where M is a metal counter-cation, preferably an alkali metal such as sodium, C1-C6, preferably C1-C4 alkyl groups and groups of formula —NR6R7 where R6 and R7 are independently selected from hydrogen and C1-C6, preferably C1-C4 alkyl groups; and

R5 is selected from poly(alkyleneoxy) groups, preferably groups of formula —(CnH2n+1O)m—CnH2n+1— where m is from 0 to 12,

preferably from 6 to 10, more preferably from 8 to 10, most preferably 10 wherein in each CnH2n+1 moiety n is independently from 2 to 4, more preferably 2 and preferably also, each n is the same.

In some preferred embodiments, R1 and R2 are independently selected from groups of formula CH3—(CH2)p—CH═CH—CH2— where p is preferably from 4 to 14, more preferably from 8 to 14 and most preferably is 14.

In some preferred embodiments, R1 and R2 are the same as each other and R3 and R4 are the same as each other, most preferably both hydrogen or both —O−M+.

Preferably also, the composition of the invention comprises from 0.1% to 5%, more preferably from 0.2% to 3%, most preferably from 0.5% to 2% by weight of the succinate dimer surfactant. However, there is no specific limitation on level and it could constitute, for example, from 0.001% to 15% or 0.005% to 10% by weight of the composition.

Compounds of formula (I) can be readily prepared by the following generic procedure using well known textbook chemistry. Alkenyl-succinic anhydride precursors are commercially available (e.g. ex Aldrich) or can be prepared via the “ene reaction” by reaction of an alkene with maleic anhydride (J. March, Advanced Organic Chemistry pg 711, 3rd Edn. 1984 and references cited). If required, the double bond in the alkenylgroup can be hydrogenated using catalytic hydrogenation (J. March, Advanced Organic Chemistry pg 691, 3rd ed. 1984 and references cited). The alkenyl-succinic anhydrides are converted to the mono-ester/diester mix via ring-opening of the anhydride by reaction with one or both alcohol endgroups of a polyethyleneglyccol of choice (J. March, Advanced Organic Chemistry pg 347, 3rd. Edn. 1984 and references cited). The ratio of mono/diester can be influenced by varying the molar ratio of anhydride to polyethyleneglycol. Reaction of 2 equivalents of anhydride with one equivalent of polyethyleneglycol would give the most economic ratio of non-reacted started materials with the products mono-ester and di-ester. The reaction can be done without solvent and can be followed by infrared spectroscopy by monitoring the disappearance of the anhydride carbonyl stretch vibration absorption at 1860 cm−1 and formation of ester carbonyl stretch vibration absorption 1733 cm−1.

The Water

The compositions according to the present invention preferably also comprise from 30% to 90%, more preferably from 40% to 85%, most preferably from 50% to 80% by weight of the water.

Other Surfactant

The compositions of the present invention comprise one or more surfactants other than the succinate dimer. Based on the weight of the total composition such other surfactant(s) preferably are from 5 to 60%, more preferably from 10 to 50% by weight of one or more other surfactants preferably selected from anionic, nonionic, cationic, zwitterionic active detergent material or mixtures thereof.

Non-limiting examples of such other surfactants useful herein typically at levels from about 10% to about 70%, by weight, include the conventional C10-C18 e.g. C10 to C13 alkylbenzene sulphonates (“LAS”), the C10-C18 secondary (2,3) alkyl sulphates of the formula CH3(CH2)x(CHOS03-M+)CH3 and CH3(CH2)y(CHOS03-M+)CH2CH3 where x and (y+1) are integers of at least about 7, preferably at least about 9, and M is a water-solubilising cation, especially sodium, unsaturated sulphates such as oleyl sulphate, C10-C18 alkyl alkoxy carboxylates (especially the EO 1-7 ethoxycarboxylates), the C10-C18 glycerol ethers, the C10-C18alkyl polyglycosides and their corresponding sulphated polyglycosides, and C12-C18 alpha-sulphonated fatty acid esters. If desired, the conventional nonionic and amphoteric surfactants such as the C12-C18 alkyl ethoxylates (“AE”) including the so-called narrow peaked alkyl ethoxylates and C6-C12 alkyl phenol alkoxylates (especially ethoxylates and mixed ethoxy/propoxy), C12-C18 betaines and sulphobetaines (“sultaines”), C10-C18 amine oxides, and the like, can also be included in the overall compositions. The C10-C18 N-alkyl polyhydroxy fatty acid amides can also be used. Typical examples include the C12-C18 N-methylglucamides. See WO 9,206,154. Other sugar-derived surfactants include the N-alkoxy polyhydroxy fatty acid amides, such as C10-C18 N-(3-methoxypropyl)glucamide. C10-C20 conventional soaps may also be used. If high sudsing is desired, the branched-chain C10-C16 soaps may be used.

Mixtures of anionic and nonionic surfactants are especially useful. Other conventional useful surfactants are listed in standard texts.

Other anionic surfactants useful for detersive purposes can also be included in the isotropic compositions hereof. These can include salts (including, for example, sodium potassium, ammonium, and substituted ammonium salts such a mono-, di- and triethanolamine salts) of soap, C9-C20 linear alkylbenzenesulphonates, C8-C22 primary or secondary alkanesulphonates, C8-C24 olefinsulphonates, sulphonated polycarboxylic acids, alkyl glycerol sulphonates, fatty acyl glycerol sulphonates, fatty oleyl glycerol sulphates, alkyl phenol ethylene oxide ether sulphates, paraffin sulphonates, alkyl phosphates, isothionates such as the acyl isothionates, N-acyl taurates, fatty acid amides of methyl tauride, alkyl succinamates and sulphosuccinates, monoesters of sulphosuccinate (especially saturated and unsaturated C12-C18 monoesters) diesters of sulphosuccinate (especially saturated and unsaturated C6-C14 diesters), N-acyl sarcosinates, sulphates of alkylpolysaccharides such as the sulphates of alkylpolyglucoside, branched primary alkyl sulphates, alkyl polyethoxy carboxylates such as those of the formula RO(CH2CH20)kCH2COO-M+ wherein R is a C8-C22 alkyl, k is an integer from 0 to 10, and M is a soluble salt-forming cation, and fatty acids esterified with isethionic acid and neutralised with sodium hydroxide. Further examples are given in Surface Active Agents and Detergents (Vol. I and II by Schwartz, Perry and Berch).

The isotropic compositions of the present invention preferably comprise at least about 5%, preferably at least 10%, more preferably at least 12% and less than 70%, more preferably less than 60% by weight, of an anionic surfactant.

Alkyl sulphate surfactants, either primary or secondary, are a type of anionic surfactant of importance for use herein. Alkyl sulphates have the general formula ROS03M wherein R preferably is a C10-C24 hydrocarbyl, preferably an alkyl straight or branched chain or hydroxyalkyl having a C10-C20 alkyl component, more preferably a C12-C18 alkyl or hydroxyalkyl, and M is hydrogen or a water soluble cation, e.g., an alkali metal cation (e.g., sodium potassium, lithium), substituted or unsubstituted ammonium cations such as methyl-, dimethyl-, and trimethyl ammonium and quaternary ammonium cations, e.g., tetramethyl-ammonium and dimethyl piperdinium, and cations derived from alkanolamines such as ethanolamine, diethanolamine, triethanolamine, and mixtures thereof, and the like.

Typically, alkyl chains of C12-C16 are preferred for lower wash temperatures (e.g., below about 50° C. and C16-C18 alkyl chains are preferred for higher wash temperatures (e.g., about 50° C.). Alkyl alkoxylated sulphate surfactants are another category of preferred anionic surfactant. These surfactants; are water soluble salts or acids typically of the

formula RO(A)mSO3M wherein R is an unsubstituted C10-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-C18 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, and M is hydrogen or a water soluble cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium cation. Alkyl ethoxylated sulphates as well as alkyl propoxylated sulphates are contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl-, trimethyl-ammonium and quaternary ammonium cations, such as tetramethyl-ammonium, dimethyl piperdinium and cations derived from alkanolamines, e.g., monoethanolamine, diethanolamine, and triethanolamine, and mixtures thereof. Exemplary surfactants are C12-C18 alkyl polyethoxylate (1.0) sulphate, C12-C18 alkyl polyethoxylate (2.25) sulphate, C12-C18 alkyl polyethoxylate (3.0) sulphate, and C12-C18 alkyl polyethoxylate (4.0) sulphate wherein M is conveniently selected from sodium and potassium.

The compositions of the present invention preferably comprise at least about 5%, preferably at least 10%, more preferably at least 12% and less than 70%, more preferably less than 60% by weight, of a nonionic surfactant.

Preferred nonionic surfactants such as C12-C18 alkyl ethoxylates (“AE”) including the so-called narrow peaked alkyl ethoxylates and C6-C12 alkyl phenol alkoxylates (especially ethoxylates and mixed ethoxy/propoxy), block alkylene oxide condensate of C6 to C12 alkyl phenols, alkylene oxide condensates of C8-C22 alkanols and ethylene oxide/propylene oxide block polymers (Pluronic™-BASF Corp.), C8-C22 fatty acid methyl ester ethoxylates, as well as semi polar nonionics (e.g., amine oxides and phosphine oxides) can be used in the present isotropic compositions. An extensive disclosure of these types of surfactants is found in U.S. Pat. No. 3,929,678.

Alkylpolysaccharides such as disclosed in U.S. Pat. No. 4,565,647 are also preferred nonionic surfactants in the isotropic compositions of the invention.

Further preferred nonionic surfactants are the polyhydroxy fatty acid amides.

A particularly desirable surfactant of this type for use in the isotropic compositions herein is alkyl-N-methyl glucamide. Other sugar-derived surfactants include the N-alkoxy polyhydroxy fatty acid amides, such as C10-C18 N-(3-methoxypropyl)glucamide. The N-propyl through N-hexyl C12-C18 glucamides can be used for low sudsing. C10-C20 conventional soaps may also be used. If high sudsing is desired, the branched-chain C10-C16 soaps may be used.

Another preferred anionic surfactant is a salt of fatty acids. Examples of fatty acids suitable for use of the present invention include pure or hardened fatty acids derived from palmitoleic, safflower, sunflower, soybean, oleic, linoleic, linolenic, ricinoleic, rapeseed oil or mixtures thereof. Mixtures of saturated and unsaturated fatty acids can also be used herein.

It will be recognised that the fatty acid will be present in the liquid detergent isotropic composition primarily in the form of a soap. Suitable cations include, sodium, potassium, ammonium, monoethanol ammonium diethanol ammonium, triethanol ammonium, tetraalkyl ammonium, e.g., tetra methyl ammonium up to tetradecyl ammonium etc. cations.

The amount of fatty acid will vary depending on the particular characteristics desired in the final detergent isotropic composition. Preferably 0 to 30%, more preferably 1-20 most preferably 5-15% fatty acid is present in the inventive isotropic composition.

Hydrotropes

Liquid detergent compositions according to the invention may be substantially free from or may contain low levels of hydrotrope such as low molecular weight primary or secondary alcohols exemplified by methanol, ethanol, propanol, and isopropanol are suitable. Monohydric alcohols are preferred for solubilising surfactant. The compositions may for example contain from up to 15%, more especially from 0.2% to 8%, typically 0.5% to 8% by weight of hydrotrope material.

Clarity

The clarity of the isotropic compositions according to the present invention does not preclude the isotropic composition being coloured, e.g. by addition of a dye, provided that it does not detract substantially from clarity. Moreover, an opacifier could be included to reduce clarity if required to appeal to the consumer. In that case the definition of clarity applied to the isotropic composition according to any aspect of the invention will apply to the base (equivalent) isotropic composition without the opacifier.

Other Ingredients

Compositions according to the present invention preferably also contain one or more other ingredients such as enzymes, enzyme stabilisers, bleaches (including bleach systems and components thereof).

Enzymes

“Detersive enzyme”, as used herein, means any enzyme having a cleaning, stain removing or otherwise beneficial effect in a laundry application. Enzymes are included in the present detergent compositions for a variety of purposes, including removal of protein-based, saccharide-based, or triglyceride-based stains, for the prevention of refugee dye transfer, and for fabric restoration. Suitable enzymes include proteases, amylases, lipases, cellulases, peroxidases, and mixtures thereof of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Preferred selections are influenced by factors such as pH-activity and/or stability optima, thermostability, and stability to active detergents, builders and the like. In this respect bacterial or fungal enzymes are preferred, such as bacterial amylases and proteases, and fungal cellulases.

Enzymes are normally incorporated into detergent or detergent additive compositions at levels sufficient to provide a “cleaning-effective amount”. The term “cleaning effective amount” refers to any amount capable of producing a cleaning, stain removal, soil removal, whitening, deodorizing, or freshness improving effect on substrates such as fabrics. In practical terms for current commercial preparations, typical amounts are up to about 5 mg by weight, more typically 0.001 mg to 3 mg, of active enzyme per gram of the detergent composition. Stated otherwise, the compositions herein will typically comprise from 0.0001% to 10%, preferably from 0.001% to 5%, more preferably 0.005%-1% by weight of a commercial enzyme preparation.

Proteolytic Enzymes

Compositions according to the present invention may comprise one or more proteolytic enzymes.

Endopeptidases (proteolytic enzymes or proteases) of various qualities and origins and having activity in various pH ranges of from 4-12 are available and can be used in the instant invention. Examples of suitable proteolytic enzymes are the subtilisins, which can be obtained from particular strains of B. subtilis, B. lentus, B. amyloliquefaciens and B. licheniformis, such as the commercially available subtilisins Savinase™, Alcalase™, Relase™, Kannase™ and Everlase™ as supplied by Novo Industri A/S, Copenhagen, Denmark or Purafec™, PurafectOxP™ and Properase™ as supplied by Genencor International. Chemically or genetically modified variants of these enzymes are included such as described in WO-A-99/02632 pages 12 to 16 and in WO-A-99/20727 and also variants with reduced allergenicity as described in WO-A-99/00489 and WO-A-99/49056.

It should be understood that the protease is present in the liquid detergent composition in a dissolved or dispersed form, i.e., the protease is not encapsulated to prevent the protease from the liquid composition. Instead the protease in more or less in direct contact with the liquid composition.

Suitable examples of proteases are the subtilisins which are obtained from particular strains of B. subtilis and B. licheniformis. One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASE™ by Novo Industries A/S of Denmark, hereinafter “Novo”. The preparation of this enzyme and analogous enzymes is described in GB 1,243,784 to Novo. Other suitable proteases include ALCALASE™ and SAVINASE™ from Novo and MAXATASE™ from International Bio-Synthetics, Inc., The Netherlands; as well as Protease A as disclosed in EP 130,756 A, and Protease B as disclosed in EP 303,761 A and EP 130,756 A. See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO 9318140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO 9203529 A. Other preferred proteases include those of WO 9510591 A. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 9507791. A recombinant trypsin-like protease for detergents suitable herein is described in WO 9425583.

Useful proteases are also described in PCT publications: WO 95/30010, WO 95/30011, WO 95/29979.

Preferred proteolytic enzymes are also modified bacterial serine proteases, such as those described in EP-A-251446 (particularly pages 17, 24 and 98), and which is called herein “Protease B”, and in EP-A-199404, which refers to a modified bacterial serine proteolytic enzyme which is called “Protease A” herein, Protease A as disclosed in EP-A-130756.

The preferred liquid laundry detergent compositions according to the present invention comprise at least 0.001% by weight, of a protease enzyme. However, an effective amount of protease enzyme is sufficient for use in the liquid laundry detergent compositions described herein. The term “an effective amount” refers to any amount capable of producing a cleaning, stain removal, soil removal, whitening, deodorizing, or freshness improving effect on substrates such as fabrics. In practical terms for current commercial preparations, typical amounts are up to about 5 mg by weight, more typically 0.001 mg to 3 mg, of active enzyme per gram of the detergent composition. Stated otherwise, the compositions herein will typically comprise from 0.001% to 5%, preferably 0.01%-1% by weight of a commercial enzyme preparation. Typically, the proteolytic enzyme content is up to 0.2%, preferably from 4×10−5% to 0.06% by weight of the composition of pure enzyme.

Other Enzymes

Optionally the compositions of the invention may additionally or alternatively contain one or more other enzymes. For example, they may contain 10-20,000 LU per gram of the detergent composition of a lipolytic enzyme selected from the group consisting of Lipolase, Lipolase ultra, LipoPrime, Lipomax, Liposam, and lipase from Rhizomucor miehei (e.g. as described in EP-A-238 023 (Novo Nordisk).

The enzymatic detergent compositions of the invention further comprise 10-20,000 LU per gram, and preferably 50-2,000 LU per gram of the detergent composition, of an lipolytic enzyme. In this specification LU or lipase units are defined as they are in EP-A-258 068 (Novo Nordisk).

A further method of assessing the enzymatic activity is by measuring the reflectance at 460 nm according to standard techniques.

Suitable other enzymes for use in the compositions of the invention can be found in the enzyme classes of the esterases and lipases, (EC 3.1.1.*, wherein the asterisk denotes any number).

A characteristic feature of lipases is that they exhibit interfacial activation. This means that the enzyme activity is much higher on a substrate which has formed interfaces or micelles, than on fully dissolved substrate. Interface activation is reflected in a sudden increase in lipolytic activity when the substrate concentration is raised above the critical micel concentration (CMC) of the substrate, and interfaces are formed. Experimentally this phenomenon can be observed as a discontinuity in the graph of enzyme activity versus substrate concentration. Contrary to lipases, however, cutinases do not exhibit any substantial interfacial activation.

Suitable lipase enzymes for detergent usage include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in GB 1,372,034. See also lipases in Japanese Patent Application 53,20487. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P “Amano,” or “Amano-P.” Other suitable commercial lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. LIPOLASE™ enzyme derived from Humicola lanygiriosa and commercially available from Novo, see also EP 341,947, is a preferred lipase for use herein. Lipase and amylase variants stabilized against peroxidase enzymes are described in WO 9414951 A to Novo. See also WO 9205249. Cutinase enzymes suitable for use herein are described in WO 8809367 A to Genencor.

Because of this characteristic feature, i.e. the absence of interfacial activation, we define for the purpose of this patent application Cutinases as lipolytic enzymes which exhibit substantially no interfacial activation. Cutinases therefor differ from classical lipases in that they do not possess a helical lid covering the catalytic binding site. Cutinases belong to a different subclass of enzymes (EC 3.1.1.50) and are regarded to be outside the scope of the present invention.

Of main interest for the present invention are fungal lipases, such as those from Humicola lanuginosa and Rhizomucor miehei. Particularly suitable for the present invention is the lipase from Humicola lanuginosa strain DSM 4109, which is described in EP-A-305 216 (Novo Nordisk), and which is commercially available as Lipolase™. Also suitable ar variants of this enzyme, such as described in WO-A-92/05249, WO-A-94/25577, WO-A-95/22615, WO-A-97/04079, WO-A-97/07202, WO-A-99/42566, WO-A-00/60063. Especially preferred is the variant D96L which is commercially available from Novozymes as Lipolase ultra, and the variant which is sold by Novozymes under the trade name LipoPrime.

The lipolytic enzyme of the present invention can usefully be added to the detergent composition in any suitable form, i.e. the form of a granular composition, a slurry of the enzyme, or with carrier material (e.g. as in EP-A-258 068 and the Savinase™ and Lipolase™ products of Novozymes). A good way of adding the enzyme to a liquid detergent product is in the form of a slurry containing 0.5 to 50% by weight of the enzyme in a ethoxylated alcohol nonionic surfactant, such as described in EP-A-450 702 (Unilever).

The enzyme to be used in the detergent compositions according to the invention can be produced by cloning the gene for the enzyme into a suitable production organism, such as Bacilli, or Pseudomonaceae, yeasts, such as Saccharomyces, Kluyveromyces, Hansenula or Pichia, or fungi like Aspergillus. The preferred production organism is Aspergillus with especial preference for Aspergillus oryzae.

Other optional suitable enzymes which may be included alone or in combination with any other enzyme may, for example, be oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. Suitable members of these enzyme classes are described in Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes, 1992, ISBN 0-12-227165-3, Academic Press. The most recent information on the nomenclature of enzymes is available on the Internet through the ExPASy WWW server (http://www.expasy.ch/).

Examples of the hydrolases are carboxylic ester hydrolase, thiolester hydrolase, phosphoric monoester hydrolase, and phosphoric diester hydrolase which act on the ester bond; glycosidase which acts on O-glycosyl compounds; glycosylase hydrolysing N-glycosyl compounds; thioether hydrolase which acts on the ether bond; and exopeptidases and endopeptidases which act on the peptide bond. Preferable among them are carboxylic ester hydrolase, glycosidase and exo- and endopeptidases. Specific examples of suitable hydrolases include (1) exopeptidases such as aminopeptidase and carboxypeptidase A and B and endopeptidases such as pepsin, pepsin B, chymosin, trypsin, chymotrypsin, elastase, enteropeptidase, cathepsin B, papain, chymopapain, ficain, thrombin, plasmin, renin, subtilisin, aspergillopepsin, collagenase, clostripain, kallikrein, gastricsin, cathepsin D, bromelain, chymotrypsin C, urokinase, cucumisin, oryzin, proteinase K, thermomycolin, thermitase, lactocepin, thermolysin, bacillolysin. Preferred among them is subtilisin;

(2) glycosidases such as α-amylase, β-amylase, glucoamylase, isoamylase, cellulase, endo-1,3(4)-β-glucanase (β-glucanase), xylanase, dextranase, polygalacturonase (pectinase), lysozyme, invertase, hyaluronidase, pullulanase, neopullulanase, chitinase, arabinosidase, exocellobiohydrolase, hexosaminidase, mycodextranase, endo-1,4-β-mannanase (hemicellulase), xyloglucanase, endo-β-galactosidase (keratanase), mannanase and other saccharide gum degrading enzymes as described in WO-A-99/09127. Preferred among them are α-amylase and cellulase; (3) carboxylic ester hydrolase including carboxylesterase, lipase, phospholipase, pectinesterase, cholesterol esterase, chlorophyllase, tannase and wax-ester hydrolase.

Examples of transferases and ligases are glutathione S-transferase and acid-thiol ligase as described in WO-A-98/59028 and xyloglycan endotransglycosylase as described in WO-A-98/38288.

Examples of lyases are hyaluronate lyase, pectate lyase, chondroitinase, pectin lyase, alginase II. Especially preferred is pectolyase, which is a mixture of pectinase and pectin lyase.

Examples of the oxidoreductases are oxidases such as glucose oxidase, methanol oxidase, bilirubin oxidase, catechol oxidase, laccase, peroxidases such as ligninase and those described in WO-A-97/31090, monooxygenase, dioxygenase such as lipoxygenase and other oxygenases as described in WO-A-99/02632, WO-A-99/02638, WO-A-99/02639 and the cytochrome based enzymatic bleaching systems described in WO-A-99/02641.

Peroxidase enzymes may be used in combination with oxygen sources, e.g., percarbonate, perborate, hydrogen peroxide, etc., for “solution bleaching” or prevention of transfer of dyes or pigments removed from substrates during the wash to other substrates present in the wash solution. Known peroxidases include horseradish peroxidase, ligninase, and haloperoxidases such as chloro- or bromo-peroxidase.

Peroxidase-containing detergent compositions are disclosed in WO 89099813 A, Oct. 19, 1989 to Novo and WO 8909813 A to Novo.

A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A to Genencor International, WO 8908694 A to Novo, and U.S. Pat. No. 3,553,139, Jan. 5, 1971 to McCarty et al.

A process for enhancing the efficacy of the bleaching action of oxidoreductases is by targeting them to stains by using antibodies or antibody fragments as described in WO-A-98/56885. Antibodies can also be added to control enzyme activity as described in WO-A-98/06812.

A preferred combination is a detergent composition comprising of a mixture of the protease of the invention and conventional detergent enzymes such as lipose, amylase and/or cellulase together with one or more plant cell wall degrading enzymes.

Suitable amylases include those of bacterial or fungal origin. Chemically or genetically modified variants of these enzymes are included as described in WO-A-99/02632 pages 18,19. Commercial cellulase are sold under the tradename Purastar™, Purastar OxAm™ (formerly Purafact Ox Am™) by Genencor; Termamyl™, Fungamyl™, Duramyl™, Natalase™, all available from Novozymes.

Amylases suitable herein include, for example, alfa-amylases sescribed in GB 1,296,839 to Novo; RAPIDASE™, International Bio-Synthetics, Inc. and TERMAMYL™, Novo. FUNGAMYL™ from Novo is especially useful.

See, for example, references disclosed in WO 9402597. Stability-enhanced amylases can be obtained from Novo or from Genencor International. One class of highly preferred amylases herein have the commonality of being derived using site-directed mutagenesis from one or more of the Baccillus amylases, especialy the Bacillus cc-amylases, regardless of whether one, two or multiple amylase strains are the immediate precursors.

Oxidative stability-enhanced amylases vs. the above-identified reference amylase are preferred for use, especially in bleaching, more preferably oxygen bleaching, as distinct from chlorine bleaching, detergent compositions herein. Such preferred amylases include (a) an amylase according to WO 9402597, known as TERMAMYL™,

Particularly preferred amylases herein include amylase variants having additional modification in the immediate parent as described in WO 9510603 A and are available from the assignee, Novo, as DURAMYL™. Other particularly preferred oxidative stability enhanced amylase include those described in WO 9418314 to Genencor International and WO 9402597 to Novo Or WO 9509909 A to Novo.

Suitable cellulases include those of bacterial or fungal origin. Chemically or genetically modified variants of these enzymes are included as described in WO-A-99/02632 page 17. Particularly useful cellulases are the endoglucanases such as the EGIII from Trichoderma longibrachiatum as described in WO-A-94/21801 and the E5 from Thermomonospora fusca as described in WO-A-97/20025. Endoglucanases may consist of a catalytic domain and a cellulose binding domain or a catalytic domain only. Preferred cellulolytic enzymes are sold under the tradename Carezyme™, Celluzyme™ and Endolase™ by Novo Nordisk A/S; Puradax™ is sold by Genencor and KAC™ is sold by Kao corporation, Japan.

Cellulases usable herein include both bacterial and fungal types, preferably having a pH optimum between 5 and 9.5. U.S. Pat. No. 4,435,307 discloses suitable fungal cellulases from Humicola insolens or Humicola strain DSM1800 or a cellulase 212-producing fungus belonging to the genus Aeromonas, and cellulase extracted from the hepatopancreas of a marine mollusk, Dolabella Auricula Solander. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275 and DE-OS-2.247.832. CAREZYME™ (Novo) is especially useful. See also WO 9117243.

Detergent enzymes are usually incorporated in an amount of 0.00001% to 2%, and more preferably 0.001% to 0.5%, and even more preferably 0.005% to 0.2% in terms of pure enzyme protein by weight of the composition. Detergent enzymes are commonly employed in the form of granules made of crude enzyme alone or in combination with other components in the detergent composition. Granules of crude enzyme are used in such an amount that the pure enzyme is 0.001 to 50 weight percent in the granules. The granules are used in an amount of 0.002 to 20 and preferably 0.1 to 3 weight percent. Granular forms of detergent enzymes are known as Enzoguard™ granules, prills, marumes or T-granules. Granules can be formulated so as to contain an enzyme protecting agent (e.g. oxidation scavengers) and/or a dissolution retardant material. Other suitable forms of enzymes are liquid forms such as the “L” type liquids from Novo Nordisk, slurries of enzymes in nonionic surfactants such as the “SL” type sold by Novo Nordisk and microencapsulated enzymes marketed by Novo Nordisk under the tradename “LDP” and “CC”.

The enzymes can be added as separate single ingredients (prills, granulates, stabilised liquids, etc. containing one enzyme) or as mixtures of two or more enzymes (e.g. cogranulates). Enzymes in liquid detergents can be stabilised by various techniques as for example disclosed in U.S. Pat. No. 4,261,868 and U.S. Pat. No. 4,318,818.

The detergent compositions of the present invention may additionally comprise one or more biologically active peptides such as swollenin proteins, expansins, bacteriocins and peptides capable of binding to stains.

Enzyme Stabilisers

Compositions according to the present invention which contain one or more enzymes also preferably contain at least one enzyme stabiliser. Such enzyme stabilisers may be selected from boron-containing protease enzyme stabilisers, non-boron protease enzyme stabilisers and mixtures thereof.

Boron-Containing Enzyme Stabilisers

Typical boron-based stabilisers include boron-based reversible stabilisers which comprise a boron compound and another substance capable of complexing with the boron compound to stabilise the enzyme in the composition but which complexes dissociate in the wash liquor to render the enzyme active.

Suitable boron compounds include sodium metaborate or sodium tetraborate (borax).

Typical substances which form a reversible complex with the boron compound including polyols such as glycerol, propylene glycol, and sorbitol. However, these are not enzyme stabilisers in the absence of the boron compound.

Typical inorganic boron sources are derivatives of boric acid including boric oxide, polyborates, orthoborates and metaborates or mixtures thereof. Preferred compounds are the alkali salts of the boric acid derivatives, such as sodium borate and borax. Typical organic boron stabilisers are aromatic borate esters and boronic acid derivatives, such as alkyl, aryl and peptide boronic acids. Boronic acids are well-known as reversible inhibitors for subtilisine type of proteases.

Another boron-based stabilising system which may be used is the combination of boric acid or a boron compound capable of forming boric acid in the composition and a source of calcium ions, such as disclosed in EP-A-0 199 405.

Non-Boron Enzyme Stabilisers

Non-boron enzyme stabilisers include water soluble calcium compounds such as calcium chloride and/or formate and water soluble short chain carboxylic acids, as well as sources of chlorine scavenge ions such as ammonium sulphates, bisulphites, thiosulphites, thiosulphate and thiols.

Mixtures of one or more boron- and or non-boron enzyme stabilisers may also be based.

The total amount of enzyme stabiliser or stabiliser system is typically from 0.001% to 10%, preferably from 0.005% to 7.5%, especially from 0.01% to 5% by weight of the total composition. Many non-boron stabilisers are protein inhibitors from various sources and modified peptides (such as peptide aldehydes and peptide trifluoromethyl ketones). Suitable examples of these and other non-boron stabilisers include the following:—

WO-A-00/01826 discloses stabilized variants of Streptomycin subtilisin inhibitor (protein inhibitor+variants).

WO-A-98/13459 discloses liquid detergents containing proteolytic enzyme, peptide aldehydes and calcium ions.

EP-A-0 583 534 discloses liquid detergents containing a peptide aldehyde.

EP-A-0 583 535 describes liquid detergents containing a peptide trifluoromethylketone.

WO-A-97/00392 describes enzymatic compositions with improved storage stability of the enzymes contained therein are obtained by including an enzyme stabiliser, preferably by way of a particular process concerns the use of lignosulphonates.

WO-A-00/01831 describes a fusion between a subtilisin and streptomyces inhibiors variants).

Another suitable class of non-boron enzyme stabiliser comprises the reversible protease inhibitors of peptide or protein type, e.g. as disclosed in WO92/03529.

Further, our unpublished European Patent Application No. 00202092.3 discloses other suitable non-boron enzyme stabilisers comprising at least one saccharide selected from disaccharides, trisaccharides and derivatives of either as well as mixtures of these disaccharides, trisaccharides and derivatives.

Yet others are disclosed in WO-A-98/13458, WO-A-98/13460, WO-A-98/13461, U.S. Pat. No. 5,178,789, WO92/03529, WO-A-93/20175 and U.S. Pat. No. 5,156,773.

Further non-boron compounds which may be incorporated as compounds which are capable of stabilising proteases in liquids are organic substances which form complexes with a transition metal, the complex being capable of catalysing bleaching of a substrate by atmospheric oxygen. Such compounds may be used as the free ligand and/or in complex with a transition metal, e.g. as disclosed in WO-A-00/12677. One specific ligand of this kind is N,N-bis(pyridin-2-yl-methyl)-1,1-bis(pyridin-2-yl)-1-aminoethane. Yet other suitable non-boron protease stabilisers are polyoxometalates such as disclosed in CA-A-2 183 814, EP-A-1 141 210 and WO-A-98/20101.

Bleaches

Optionally, any composition according to the invention may contain a bleach or bleach system. Preferred are catalysts for bleaching by atmospheric oxygen.

Alternatively, oxygen bleaches and oxygen bleach systems may be employed, for example in the form of an inorganic persalt preferably with an activator, or as a peroxy acid compound.

In the case of the inorganic persalt bleaches, the activator makes the bleaching more effective at lower temperatures, i.e. in the range from ambient temperature to about 60° C., so that such bleach systems are commonly known as low-temperature bleach systems and are well known in the art. The inorganic persalt such as sodium perborate, both the monohydrate and the tetrahydrate, acts as release active oxygen n solution, and activator is usually an organic compound havine one or more reactive acyl residues, which cause the formation of peracids, the latter providing for more effective bleaching action at lower temperatures than the peroxy-bleach compound alone. The ratio by weight of the peroxy bleach compound to the activator is from about 15:1 to about 2:1, preferably from about 10:1 to about 3.5:1. Whilst the amount of the bleach system, i.e. peroxy bleach compounds and activator may be varied between about 5% and about 35% by weight of the total liquid, it is preferred to use from about 6% to about 30% of the ingredients forming the bleach system. Thus, the preferred level of the peroxy bleach compound in the composition is between 5.5% and about 27% by weight, while the preferred level of the activator is between about 0.5% and about 40%, most preferably between about 1% and about 5% by weight.

Typical examples of the suitable peroxybleach compounds are alkalimetal perborates, both tetrahdyrates and monohydrates, alkali metal, percarbonates, alkylhydroperoxides such as cumene hydroperoxide and t-butyl hydroperoxide, persilicates and perphosphates, of which sodium perborate is preferred. Activators for peroxybleach compounds have been amply described in the literature, including in British patent specifications 836988, 855735, 907356, 907358, 907950, 1003310 and 1246339, U.S. Pat. Nos. 3,332,882 and 4,128,494, Canadian patent specification 844481 and South African patent specification 68/6344.

The exact mode of action of such activators is not known, but it is believed that peracids are formed by reaction of the activators with the inorganic peroxy compound, which peracids then liberate active-oxygen by decomposition.

They are generally compounds which contain N-acyl or O-acyl residues in the molecule and which exert their activating action on the peroxy compounds on contact with these in the washing liquor.

Typical examples of activators within these groups are polyacylated alkylene diamines, such N,N,N1N,1−tetraacetylethylene diamine (TAED) and N,N,N1,N1−tetraacetylmethylene diamine (TAMD); acylated glycolurils, such as tetraacetylgylcoluril (TAGU); triacetylcyanurate and sodium sulphophenyl ethyl carbonic acid ester.

A particularly preferred activator is N,N,N1,N1-tetraacetylethylene diamine (TAED). The activator may be incorporated as fine particles or even in granular form, such as described in the applicants' UK patent specification GB 2 053 998 A. Specifically, it is preferred to have an activator of an average particle size of less than 150 micrometers, which gives significant improvement in bleach efficiency. The sedimentation losses, when using an activator with an average particle size of less than 150 μm, are substantially decreased. Even better bleach performance is obtained if the average particle size of the activator is less than 100 μm. However, too small a particle size can give increased decomposition and handling problems prior to processing. However, these particle sizes have to be reconciled with the requirements for dispersion in the solvent (it will be recalled that the aforementioned first product from requires particles which are as small as possible within practical limits). Liquid activators may also be used, e.g. as hereinafter described.

The organic peroxyacid compound bleaches (which in some cases can also act as structurants/deflocculants) are preferably those which are solid at room temperature and most preferably should have a melting point of at least 50° C. Most commonly, they are the organic peroxyacids and water-soluble salts thereof having the general formula

wherein R is an alkylene or substituted alkylene group containing 1 to 20 carbon atoms or an arylene group containing from 6 to 8 carbon atoms, and Y is hydrogen halogen, alkyl, aryl or any group which provides an anionic moiety in aqueous solution. Such Y groups can include, for example:

wherein M is H or a water-soluble, salt-forming cation.

The organic peroxyacids and salts thereof usable in the present invention can contain either one, two or more peroxy groups and can be either aliphatic or aromatic. When the organic peroxyacid is aliphitic, the unsubstituted acid may have the general formula:

wherein Y can be H, —CH3, —CH2Cl,

And n can be an integer from 60 to 20. Peroxydodecanoic acids, peroxytetradecanoic acids and peroxyhexadecanoic acids are the most preferred compounds of this type, particularly 1,12-diperoxydodecandioic acid (sometimes known as DPDA), 1,14-diperoxytetradecandioic acid and 1,16diperoxyhexadecandioic acid. Examples of other preferred compounds of this type are diperoxyazelaic acid, diperoxyadipic and diperoxysebacic acid.

When the organic peroxyacid is aromatic, a unsubstituted acid may have the general formula:

wherein Y is, for example hydrogen, halogen, alkyl or a group as defined for formulae (IV) above.

The percarboxy and Y groupings can be in any relative position around the aromatic ring. The ring and/or Y group (if alkyl) can contain any non-interfering substitutents such as halogen or sulphonate groups. Examples of suitable aromatic peroxyacids and saltes thereof include monoperoxyphthalic acid, diperoxyterephthalic acid, 4-chlorodiperoxy-phthalic acid, diperoxyisophthalic acid, peroxy benzoic acids and ring-substituted peroxy benzoic acids, such as peroxy-alpha-naphthoic acid. A preferred aromatic peroxyacid is diperoxyisophthalic acid.

Another preferred class of peroxygen compounds which can be incorporated to enhance dispensing/dispersibility in water are the anyhdrous perborates described for that purpose in the applicants' European patent specification EP-A-217 454. Alternatively or in addition to, a transition metal catalyst may used with the peroxyl species, see, for example WO-A-02/48301. A transition metal catalyst may also be used in the absence of peroxyl species where the bleaching is termed to be via atmospheric oxygen, see, for example WO-A-00/52124 and WO-A-02/48301. The transition metal catalysts disclosed in WO-A-00/52124 and WO-A-02/48301 are generally both applicable to what is known in the art as “air mode” and “peroxyl mode” bleaching. Another example of a suitable class of transition metal catalysts is found in WO-A-02/48301 and references found therein.

It is also preferred to include in the compositions, a stabiliser for the bleach or bleach system, for example ethylene diamine tetramethylene pholphonate and diethylene triamine pentamethylene phosphonate or other appropriate organic phosphonate or salt thereof, such as the Dequest range hereinbefore described. These stabilisers can be used in acid or salt form which as the calcium, magnesium, zinc or aluminium salt form. The stabiliser may be present at a level of up to about 1% by weight, preferably between about 0.1% and about 0.5% by weight.

Since many bleaches and bleach systems are unstable in aqueous liquid detergents and/or other interact unfavourably will other components in the composition, e.g. enzymes, they may for example be protected, e.g. by encapsulation or by formulating a structured liquid composition, whereby they are suspended in solid form.

Other Optional Ingredients

The compositions herein can further comprise a variety of optional ingredients. A wide variety of other ingredients useful in detergent compositions can be included in the compositions herein, including other active ingredients, carriers, hydrotropes, processing aids, dyes or pigments, solvents for liquid formulations, solid fillers for bar compositions, etc. If high sudsing is desired, suds boosters such as the C10-C16 alkanolamides can be incorporated into the compositions, typically at 1%-10% levels. The C10-C14 monoethanol and diethanol amides illustrate a typical class of such suds boosters. Use of such suds boosters with high sudsing; adjunct surfactants such as the amine oxides, betaines and sultaines noted above is also advantageous. If desired, soluble magnesium salts such as MgCl2, MgSO4, and the like, can be added at levels of, typically, 0.1%-2%, to provide additional suds and to enhance grease removal performance.

Various detersive ingredients employed in the present compositions optionally can be further stabilized by absorbing said ingredients onto a porous hydrophobic substrate, then coating said substrate with a hydrophobic coating. Preferably, the detersive ingredient is admixed with a surfactant before being absorbed into the porous substrate. In use, the detersive ingredient is released from the substrate into the aqueous washing liquor, where it performs its intended detersive function.

By this means, ingredients such as the aforementioned, bleaches, bleach activators, bleach catalysts, photoactivators, dyes, fluorescers, fabric conditioners and hydrolyzable surfactants can be “protected” for use in detergents, including liquid laundry detergent compositions.

Liquid detergent compositions can contain water and other solvents as carriers.

Chelating Agents

The detergent compositions herein may also optionally contain one or more iron, copper and/or manganese chelating agents. Such chelating agents can be selected from the group consisting of amino carboxylates, amino phosphonates, polyfanctionally-substituted aromatic chelating agents and mixtures therein, all as hereinafter defined.

If utilized, these chelating agents will generally comprise from about 0.1% to about 10% by weight of the detergent compositions herein. More preferably, if utilized, the chelating agents will comprise from about 0.1% to about 3.0% by eight of such compositions.

Clay Soil Removal/Anti-Redeposition Agents

The compositions of the present invention can also optionally contain water-soluble ethoxylated amines having clay soil removal and antiredeposition properties.

Liquid detergent compositions typically contain about 0.0 1% to about 5% of these agents.

One preferred soil release and anti-redeposition agent is ethoxylated tetraethylenepentamine. Exemplary ethoxylated amines are further described in U.S. Pat. No. 4,597,898,

Another type of preferred antiredeposition agent includes the carboxy methyl cellulose (CMC) materials. These materials are well known in the art.

Brightener

Any optical brighteners or other brightening or whitening agents known in the art can be incorporated at levels typically from about 0.05% to about 1.2%, by weight, into the detergent compositions herein. Commercial optical brighteners which may be useful in the present invention can be classified into subgroups, which include, but are not necessarily limited to, derivatives of stilbene, pyrazoline, cournarin, carboxylic acid, methinecyanines, dibenzothiphene-5,5-dioxide, azoles, 5- and 6-membered-ring heterocycles, and other miscellaneous agents. Examples of such brighteners are disclosed in “The Production and Application of Fluorescent Brightening Agents”, M. Zahradnik, Published by John Wiley & Sons, New York (1982).

Suds Suppressors

Compounds for reducing or suppressing the formation of suds can be incorporated into the compositions of the present invention. Suds suppression can be of particular importance in the so-called “high concentration cleaning process” as described in U.S. Pat. Nos. 4,489,455 and 4,489,574 and infront-loading European-style washing machines.

A wide variety of materials may be used as suds suppressors, and suds suppressors are well known to those skilled in the art. See, for example, Kirk Othmer Encyclopedia of Chemical Technology, Third Edition, Volume 7, pages 430-447 (John Wiley & Sons, Inc., 1979). One category of suds suppressor of particular interest encompasses monocarboxylic fatty acid and soluble salts therein. See U.S. Pat. No. 2,954,347. The monocarboxylic fatty acids and salts thereof used as suds suppressor typically have hydrocarbyl chains of 10 to about 24 carbon atoms, preferably 12 to 18 carbon atoms. Suitable salts include the alkali metal salts such as sodium, potassium, and lithium salts, and ammonium and alkanolammonium salts.

The detergent compositions herein may also contain non-surfactant suds suppressors. These include, for example: high molecular weight hydrocarbons such as paraffin, fatty acid esters (e.g., fatty acid triglycerides), fatty acid esters of monovalent alcohols, aliphatic C 1 8-C40 ketones (e.g., stearone), etc.

The preferred category of non-surfactant suds suppressors comprises silicone suds suppressors. This category includes the use of polyorganosiloxane oils, suchas polydimethylsiloxane, dispersions or emulsions of polyorganosiloxane oils or resins, and combinations of polyorganosiloxane with silica particles wherein the polyorganosiloxane is chemisorbed or fused onto the silica. Silicone suds suppressors are well known in the art and are, for example, disclosed in U.S. Pat. No. 4,265,779.

For any detergent compositions to be used in automatic laundry washing machines, suds should not form to the extent that they overflow the washing machine.

Suds suppressors, when utilized, are preferably present in a “suds suppressing amount”.

By “suds suppressing amount” is meant that the formulator of the composition can select an amount of this suds controlling agent that will sufficiently control the suds to result in a low-sudsing laundry detergent for use in automatic laundry washing machines.

The compositions herein will generally comprise from 0.1% to about 5% of suds suppressor.

Fabric Softeners

Various through-the-wash fabric softeners, especially the impalpable smectite clays of U.S. Pat. No. 4,062,647 as well as other softener clays known in the art, can optionally be used typically at levels of from about 0.5% to about 10% by weight in the present compositions to provide fabric softener benefits concurrently with fabric cleaning. Clay softeners can be used in combination with amine and cationic softeners as disclosed, for example, in U.S. Pat. No. 4,375,416 and U.S. Pat. No. 4,291,071. Also useable are the amphiphilic carboxy containing polymers as disclosed in US-A-2005/0124528.

Dye Transfer Inhibiting Agents

The compositions of the present invention may also include one or more materials effective for inhibiting the transfer of dyes from one fabric to another during the cleaning process. Generally, such dye transfer inhibiting agents include polyvinyl pyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, manganese phthalocyanine, peroxidases, and mixtures thereof. If used, these agents typically comprise from about 0.01% to about 10% by weight of the composition, preferably from about 0.01% to about 5%, and more preferably from about 0.05% to about 2%.

The invention will now be further illustrated by way of the following non-limiting examples:

EXAMPLES Example I Method:

The additives A-D are post-dosed to liquids 1-4 and incorporated by mixing. All prepared liquids are physical stable and transparent at room temperature. A panel of experts examines the physical stability and transparency after 4 weeks of storage at 0 and 5° C. The observations are described in table 1-4 and the panel used the following terms to describe their observations.

Clear/no particles=transparent liquid without white particles, no difference with liquids stored at room temperature.

Clear/small particles=transparent liquid with white particles formed during storage. Hazy/no particles=during storage the liquid becomes not transparent but there are no particles formed.

Hazy/white particles=during storage the liquid becomes not transparent and there are white particles formed.

TABLE I The physical stability of liquid 1 with different levels additives determined by a panel of experts after 4 weeks of storage at 0 and 5° C. additive (see Physical stability Physical stability Table 7) level (%) (0° C.) (5° C.) None 0 hazy, small particles hazy, small particles A 0.5 hazy, small particles clear, small particles A 1 hazy, small particles clear, small particles A 2 hazy, small particles hazy, small particles B 0.5 hazy, small particles clear, small particles B 1 hazy, small particles clear, small particles B 2 hazy, small particles hazy, small particles C 0.5 clear, small particles clear, no particles C 1 clear, no particles clear, no particles C 2 clear, no particles clear, no particles D 0.5 hazy, small particles hazy, small particles D 1 Hazy, no particles hazy, small particles D 2 Hazy, no particles clear, no particles

TABLE 2 The physical stability of liquid 2 with different levels additives determined by a panel of experts after 4 weeks of storage at 0 and 5° C. Physical stability Physical stability additive level (%) (0° C.) (5° C.) None 0 Hazy, no particles clear, small particles A 0.5 Hazy, no particles clear, small particles A 1 Hazy, small particles clear, small particles A 2 Hazy, small particles clear, small particles B 0.5 Hazy, small particles clear, small particles B 1 Hazy, small particles clear, small particles B 2 Hazy, small particles clear, small particles C 0.5 clear, no particles clear, no particles C 1 clear, no particles clear, no particles C 2 clear, no particles clear, no particles D 0.5 Hazy, small particles clear, small particles D 1 Hazy, small particles clear, small particles D 2 Hazy, small particles clear, small particles

TABLE 3 The physical stability of liquid 3 with different levels additives determined by a panel of experts after 4 weeks of storage at 0 and 5° C. Physical stability Physical stability Additive level (%) (0° C.) (5° C.) None 0 hazy, no particles hazy, small particles A 0.5 Clear, small particles hazy, no particles A 1 Clear, small particles clear, small particles A 2 Clear, small particles clear, small particles B 0.5 Clear, small particles clear, small particles B 1 Clear, small particles clear, small particles B 2 Clear, small particles clear, small particles C 0.5 Clear, no particles clear, no particles C 1 Clear, no particles clear, no particles C 2 Clear, no particles clear, no particles D 0.5 Clear, small particles clear, small particles D 1 Clear, small particles clear, small particles D 2 Clear, small particles hazy, small particles

TABLE 4 The physical stability of liquid 4 with different levels additives determined by a panel of experts after 4 weeks of storage at 0 and 5° C. Physical stability Physical stability Additive level (%) (0° C.) (5° C.) None 0 Hazy, small particles hazy, small particles A 0.5 Hazy, small particles clear, small particles A 1 Hazy, small particles clear, small particles A 2 Hazy, small particles hazy, small particles B 0.5 Hazy, small particles hazy, small particles B 1 clear, small particles hazy, small particles B 2 Hazy, small particles hazy, small particles C 0.5 clear, no particles clear, no particles C 1 clear, no particles clear, no particles C 2 clear, no particles clear, no particles D 0.5 Hazy, small particles hazy, small particles D 1 Hazy, small particles hazy, small particles D 2 clear, small particles clear, small particles

Example 2 Method:

Additive C is post-dosed to liquid 5 and incorporated by mixing. All prepared liquids are physical stable and transparent at room temperature. A panel of experts examines the physical stability and transparency after 8 weeks of storage at 0 and 5° C.

The observations are described in table 5 and the panel used the following terms to describe theft observations.

Clear/no particles=transparent liquid without white particles, no difference with liquids stored at room temperature.

Clear/small particles=transparent liquid with white particles formed during storage. Hazy/no particles=during storage the liquid becomes not transparent but there are no particles formed.

Hazy/white particles=during storage the liquid becomes not transparent and there are white particles formed.

TABLE 5 The physical stability of liquid 5 w/wo addition of additive C determined by a panel of experts after 8 weeks of storage at 0 and 5° C. level Physical stability Physical stability Additive (%) (0° C.) (5° C.) None 0 hazy, small particles hazy, small particles C 1 clear, no particles clear no particles

TABLE 6 composition liquids (as 100%) Liquid Liquid Liquid Liquid 1 (%) 2 (%) 3 (%) 4 (%) Liquid 5 Monopropylene 1 1 1 1 0 glycol NaOH 1.49 1.17 1.64 1.53 1.45 Tinopal CBS-X 0.02 0.02 0.02 0.02 0.02 Citric acid 0.37 0 0.37 0 0.74 Dequest 2066 1 1 1 1 1 Nipacide BIT 20 LC 0.02 0.02 0.02 0.02 0.02 NeodoI25-7 E 7.18 7.17 8.18 8.16 7.66 Prifac 5908 1.70 1.70 1.70 1.70 1.69 LAS acid 7.18 7.18 8.18 8.16 7.66 SLES 3 EO 1.99 1.97 8.18 8.16 0 Relase 16 L ultra 0.38 0.38 0.38 0.38 0.38 Stainzyme 12 L 0.10 0.10 0.10 0.10 0.10 Perfume 0.4 0.4 0.4 0.4 0.4 pH 8.3 8.3 8.3 8.3 8.3 Liquid A Liquid 6 Liquid B Liquid 7 (%) (%) (%) (%) Monopropylene 2 2 10 10 glycol NaOH 1.37 1.37 3.44 3.44 MEA 2.23 2.23 0 0 TEA 0 0 3.39 3.39 Tinopal CBS-X 0.02 0.02 0.02 0.02 NaCl 0.25 0.25 0 0 Citric acid 0 0 1.31 1.31 Dequest 2066 1 1 0 0 Proxel GXL 0.02 0.02 0 0 NeodoI 25-7 E 4.45 4.45 14 14 Prifac 5908 8.00 8.00 5 5 LAS acid 9.0 9.0 21 21 SLES 2 EO 0 0 7 7 LR400 0.2 0.2 0.25 0.25 PVPK15 0.1 0.1 0 0 Additive C 0 1.0 0 1 Water To 100 To 100 To 100 To 100 pH(±0.1) 8.3 8.3 8.3 8.3 Stability 5° C. over Hazy Clear Hazy Clear 1 week

Materials:

LAS acid ═C10-C14 alkyl benzene sulphonic acid;

sLES 3 EO=sodium lauryl ether sulphate (with on average 3 oxide groups);

sLES 2 EO=sodium lauryl ether sulphate (with on average 2 oxide groups);

NI 7EO=C12-C13 fatty alcohol ethoxylated with an average of 7 ethylene oxide groups; MPG=monopropylene glycol;

Prifac 7908=palmkernel fatty acid;

Proxel GXL=trade name biocide Proxel GXL (20% active)

Dequest 2066=diethylenetriamino-penta-(methylenenephosphonic acid) DETPMP

MEA=monoethanolamine

TEA=triethanolamine

Tinopal CBA-X=4,4-bis(2-disulfonic acid styryl) biphenyl PVP K15=polyvinylpyrrolidone K15

NaOH=Sodium hydroxide

NaCl=Sodium chloride

Nipacide BIT 20 LC=trade name Nipacide BIT 20 LC 20% active

Relase 16 L ultra=protease (relase 16 L ultra)

Stainzyme 12 L=amylase (stainzyme 12 L)

citric acid

perfume: commercial detergent perfume

TABLE 7 tested additives (referring to Formula (I)): additive R1 and R2 M (av.) n (av.) A C12 alkenyl ca. 8 2 B C12 alkenyl ca. 12 2 C C18 alkenyl ca. 12 2 D C8 alkenyl ca. 12 2

Claims

1. An isotropic aqueous liquid detergent composition comprising:

a succinate dimer surfactant consisting of at least one compound of formula (I):
wherein in formula (I), each of R1 and R2 is independently selected from alkyl and alkenyl groups having from 8 to 18, preferably from 12 to 18, most preferably 18 carbon atoms; each of R3 and R4 is independently selected from hydrogen, groups M where M is a metal counter-cation, preferably an alkali metal such as sodium, C1-C6, preferably C1-C4 alkyl groups and groups of formula —NR6R7 where R6 and R7 are independently selected from hydrogen and C1-C6, preferably C1-C4 alkyl groups; and
R5 is selected from poly(alkyleneoxy) groups, preferably groups of formula —(CnH2n+1O)m—CnH2n+1— where m is from 0 to 12, preferably from 6 to 10, more preferably from 8 to 10, most preferably 10 wherein in each CnH2n+1 moiety n is independently from 2 to 4, more preferably 2 and preferably also, each n is the same;
one or more other surfactants; and water.

2. A composition according to claim 1, wherein R1 and R2 are independently selected from groups of formula CH3—(CH2)p—CH═CH—CH2— where p is preferably from 4 to 14, more preferably from 8 to 14 and most preferably is 14.

3. A composition according to claim 1, comprising from 0.1% to 5%, more preferably from 0.2% to 3%, most preferably from 0.5% to 2% by weight of the disuccinate dimer surfactant.

4. A composition according to claim 1, comprising from 5% to 60%, more preferably from 10% to 50%, most preferably from 12% to 45% by weight of the one or more other surfactants.

5. A composition according to claim 1, comprising from 30% to 90%, more preferably from 40% to 85%, most preferably from 50% to 80% by weight of the water.

6. A composition according to claim 1, further comprising soap.

7. A composition according to claim 1, further comprising an atmospheric oxygen bleach catalyst.

8. A method of preparing an isotropic liquid detergent composition, the method comprising admixture of a succinate dimer surfactant according to claim 1, one or more other surfactants, water and optionally, one or more other ingredients.

9. Use of a succinate dimer surfactant according to claim 1, as a stabiliser for an isotropic liquid detergent composition comprising water and one or more other surfactants.

Patent History
Publication number: 20070265182
Type: Application
Filed: May 11, 2007
Publication Date: Nov 15, 2007
Applicant:
Inventors: Olaf Cornelis P Beers (Vlaardingen), Lillimarlene Faucia Brouwn (Vlaardingen), Ian Charles Callaghan (Riding Mill), Maartje Ouwendijk-Vrijenhoek (Vlaardingen), Derdiyok Sonmezer (Vlaardingen), Simon Marinus Veerman (Vlaardingen)
Application Number: 11/803,056