DE212009000119U1 - Dispenser and pretreatment agent for viscous liquids - Google Patents

Abstract

A packaged laundry product comprising a flowable detergent contained in a packaging dispensing at the bottom, wherein (i) the flowable detergent has a viscosity of at least 100 Pa · s, preferably at least 500 Pa · s when it is at rest or up to one Shear stress of 10 Pa., And comprises at least one surfactant and at least one hydrotrope, and (ii) the bottom-dispensing package comprises a compressible container in which the flowable detergent is stored and a dosing device which has incorporated a fabric treatment device, wherein the dosing device and tissue pretreatment device are located at the bottom of the compressible container, characterized in that the tissue treating container is enclosed by a dosage locking device which provides a supporting base of the package, and wherein the package has a curved top.

Description

The present invention relates to a viscous wash product and a package therefor.

It is an object to provide an improved pre-treatment device for the precise pretreatment of laundry stains.

• (i) das fließfähige Waschmittel eine Viskosität von wenigstens 100 Pa·s, vorzugsweise wenigstens 500 Pa·s hat, wenn es in Ruhe ist oder bis zu einer Scherspannung von 10 Pa, und das wenigstens ein Tensid und wenigstens ein Hydrotrop umfasst, und
• (ii) die am Boden abgebende Verpackung einen komprimierbaren Behälter, in welchem das fließfähige Waschmittel aufgenommen ist, und eine Spendervorrichtung, die eine Gewebevorbehandlungsvorrichtung eingebaut hat, umfasst, wobei die Spendervorrichtung und die Gewebevorbehandlungsvorrichtung am Boden des komprimierbaren Behälters lokalisiert sind.

Accordingly, in one aspect, the present invention provides a packaged laundry product comprising a flowable laundry detergent contained in a bottom-releasing package

• (i) the flowable detergent has a viscosity of at least 100 Pa · s, preferably at least 500 Pa · s, when at rest or up to a shear stress of 10 Pa and comprising at least one surfactant and at least one hydrotrope, and
• (ii) the bottom-dispensing package comprises a compressible container in which the flowable detergent is contained and a dispenser device incorporating a tissue pretreatment device, wherein the dispenser device and the tissue pretreatment device are located at the bottom of the compressible container.

The advantage of the above arrangement is that it provides greater control when applying a high viscosity composition to soiled areas. Pretreatment with high viscosity fluids from hand-held products is advantageous in terms of accuracy of application to the soiled area. However, this can be ergonomically difficult and many users apply impact force to the device (beating the base or tapping the side), which interferes with accurate dosing and often results in overdose, spillage, etc.

This arrangement, as a result of the positioning of the dispenser / pre-treatment part at the base of the container, means that the user does not need to invert the package in order to dose / pretreat or wait until the viscous liquid on the base flows to the top ( where dispensers / pre-treatment devices are normally attached). In the present invention, gravity keeps the pretreatment device loaded with the agent. While the propensity of high viscosity products to remain in place during a pretreatment is beneficial, it can often still persist through the washing process and leave its own mark on the fabric after the washing process has begun. This is often the case especially for short wash cycles or for "eco-friendly" washings with little water. The presence of a hydrotrope facilitates solubilization of the stain-applied agent and thereby faster release during washing.

Preferably, the tissue treatment container is closed by a dosage closure device which provides a bearing base of the packaging.

The advantage of this arrangement is that the dispensing device does not require complicated and expensive seals / valves since the dosing closure encloses the pretreatment device and provides the base: this offers the advantage that drops of the agent that fall out of the pretreatment device after use, in the bearing base, which can then be placed directly into the washing machine / receptacle, minimizing waste.

The dispensing device may include a channel or conduit that provides fluid communication between the reservoir and the pretreatment agent.

The pretreatment means may comprise a device which allows mechanical cleaning, for example a body with many projections.

The projections can be flexible so that they move during cleaning, providing a light cleaning process. Alternatively, some or all of the projections may be semi-rigid or rigid so as to provide a stronger mechanical cleaning process. The projections may be thin, for example bristles, to provide a brush-like device or may be thicker so as to provide finger-like projections.

The package may have a curved top to keep users from storing the bottle upside down. In this way, the packaging will most likely be in one Pre-treatment agent loading position stored, that is, with the flowable detergent by gravity accumulated in the base of the package.

In one embodiment, the pretreatment means comprises a generally hemispherical body having many projections extending radially therefrom.

The composition may comprise 0.1 to 10% by weight of hydrotrope, preferably 0.1 to 5%, more preferably 0.1 to 2%, and most preferably 0.1 to 1% of hydrotrope.

Possible hydrotropes include toluene, urea, cumenesulfonate, xylenesulfonate and mixtures thereof. Salts include sodium, potassium, ammonium, monoethanolamine, triethanolamine and mixtures thereof. One combination is xylene sulfonate and urea.

The agent is preferably a shear-thinning gel-type agent. The shear stress may be less than 300 Pa · s, preferably less than 100 Pa · s, and more preferably less than 5 Pa · s, even more preferably at most 1 Pa · s, and most preferably at most 0.5 Pa · s ,

Shear thinning agents may include a polymer gum, for example, xanthan gum or other gum capable of forming stable continuous gum networks that can suspend particles.

Other external structurants, for example hydrogenated castor oil, microcrystalline cellulose, may be used.

Another method useful for altering a non-gelled formulation to form an internal structure therein, which structure provides the desired properties of the gel-type detergent thus formed, can be used. The agent may comprise a soap or a fatty acid in combination with sodium sulfate, and it may be a surfactant or a plurality of surfactants may be used to form a gelled structure through the formation of lamellar phases.

The composition may comprise lamellar phase dispersions of a micellar surfactant system and additionally a structuring agent for the development of the lamellar phase, wherein the structurant may be a fatty alcohol.

The composition of the invention contains one or more surfactants and / or optional other ingredients such that the agent is fully functional as a laundry cleansing and / or conditioning composition. An agent of the invention may be provided in solid or liquid form. When provided in solid form, the agent may be rehydrated and / or dissolved in a solvent, including water, before use. The agent may be provided in a concentrated form for dilution or may be a ready-to-use agent.

The present invention is suitable for use in industrial or household fabric laundry detergents. The present invention may also be applied to industrial or household non-detergent based fabric care compositions.

Other contemplated ingredients, including hydrotropes, preservatives, fillers, images, chelants, polymers, stabilizers, perfumes per se, other conventional detergent ingredients, or combinations of one or more thereof, are discussed below.

surfactants:

Fabric laundry detergents according to the present invention comprise a fabric washing detergent material selected from anionic non-soap surfactants, nonionic surfactants, soap, amphoteric surfactants, zwitterionic surfactants, and mixtures thereof.

Detergent compositions suitable for use in household or industrial automatic fabric washing machines generally contain anionic non-soap surfactant or nonionic surfactant or combinations of the two in a suitable ratio, as will be known to those skilled in the art, optionally together with salts.

The surfactants may be present in the composition in a concentration of 0.1 to 60% by weight.

Suitable anionic surfactants include alkylbenzenesulfonate, primary and secondary alkyl sulfates, especially C ₈ -C ₁₅ primary alkyl sulfates; alkyl ether; olefin; Alkyl xylene sulfonates, dialkyl sulfursuccinates; carboxylates; isethionates; sarcosinates; Fatty acid ester sulfonates and mixtures thereof. The sodium salts are generally preferred. When included therein, the composition typically contains from about 1% to about 50%, preferably 10% to 40% by weight, based on the fabric treatment agent, of an anionic surfactant, for example, linear alkyl benzene sulfonate, alpha olefin sulfonate, alkyl sulfate ( Fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkali sulfonate, alpha-sulfofatty acid methyl ester, alkyl or alkenyl succinic acid or soap. Preferred surfactants are alkyl ether sulfates and mixtures of nonionic alkoxylated alkyl surfactants with either alkyl sulfonates or alkyl ether sulfates.

Preferred alkyl ether sulfates are C ₈ -C ₁₅ alkyl and have 2 to 10 moles of ethoxylation. Preferred alkyl sulfates are alkyl benzene sulfonates, especially linear alkyl benzene sulfonates having an alkyl chain length of C18 to C15. The counterion for anionic surfactants is typically sodium, although other counterions, for example TEA or ammonium may be used. Suitable anionic surfactant materials are available on the market, such as the "Genapol" ^™ series from Clariant.

Nonionic surfactants include primary and secondary alcohol ethoxylates, especially C ₈ -C ₇ aliphatic alcohols, ethoxylated with an average of 1 to 7 moles of ethylene oxide per mole of alcohol, and more particularly the C ₁₀ -C ₁₅ primary and secondary aliphatic alcohols ethoxylated with average 1 to 10 moles of ethylene oxide per mole of alcohol. Non-ethoxylated nonionic surfactants include alkylpolyglycosides, glycerol monoethers and polyhydroxyamides (glucamide). Mixtures of non-ionic surfactant can be used. When included, the composition will usually contain from about 0.2% to about 40%, preferably 1 to 7%, more preferably 5 to 15%, by weight of a nonionic surfactant, for example, alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside , Alkyldimethylaminoxid, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, Polyhydroxyalkylfettsäureamid or N-acyl-N-alkyl derivatives of glucosamine ("glucamides").

Nonionic surfactants that may be used include the primary and secondary alcohol ethoxylates, especially the C ₈ -C ₇ aliphatic alcohols ethoxylated with an average of 1 to 35 moles of ethylene oxide per mole of alcohol, and more particularly the primary and secondary aliphatic C ₁₀ - C ₁₅ -alcohols, ethoxylated with an average of 1 to 10 moles of ethylene oxide per mole of alcohol.

enzymes

The one or more enzymes may be any suitable ones. It will be appreciated that enzyme variants (produced, for example, by recombinant techniques) are included within the meaning of the term "enzyme". Examples of such enzyme variants are, for example, in EP 251,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV).

The types of enzymes that can be suitably incorporated into grains of the invention include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases, that is, (EC 1-.-.-), (EC 2-.-.-. ), (EC 3.-.-.-), (EC 4.-.-.-), (EC 5.-.-.-), (EC 6.-.-.-), wherein such an enzyme classification Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Academic Press, Inc., 1992.

Specifically contemplated enzymes include proteases, alpha-amylases, cellulases, ligases, peroxidases / oxidases, pectate lyases and mannanases, or mixtures thereof. Extremely preferred enzymes are proteases.

Suitable proteases include those of animal, vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. The protease may be a serine protease or a metalloprotease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those derived from Bacillus, e.g. Subtilisin Novo, Subtilisin Carlsberg, Subtilisin 309, Subtilisin 147 and Subtilisin 168 (described in US Pat WO 89/06279 ). Examples of trypsin-like proteases are trypsin (eg of porcine or bovine origin) and the Fusarium protease described in WO89 / 06270 and WO 94/25583 ,

Examples of useful proteases are the variants described in WO 92/19729 . WO 98/20115 . WO 98/20116 and WO 98/34946 Specifically, the variants with substitutions in one or more several of the following positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235 and 274. Preferred commercially available protease enzymes include Alcalase ^™ , Savinase, Primase ^™ , Duralase ^™ , Dyrazym ^™ , Esperase ^™ , Everlase ^™ , Polarzyme ^™ and Kannase ^™ , (Novozymes A / S), Maxatase ^™ , Maxacal ^™ , Maxapem ^™ , Properase ^™ , Purafect ^™ , Purafect OxP ^™ , FN2 ^™ and FN3 ^™ (Genencor International Inc.).

Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include Humicola lipases (Synonym Thermomyces), e.g. H. lanuginosa (T. lanuginosus), as in EP 258,068 and EP 305 216 described, or H. insolens, as in WO 96/13580 described a Pseudomonas lipase, z. 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. B. 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, for example, those described in U.S. Pat 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 are described.

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

The method of the invention may be carried out in the presence of cutinase, classified in EC 3.1.1.74. The cutinase used according to the invention may be of any origin. Preferably, cutinases are of microbial origin, in particular of bacterial, fungal or yeast origin.

Cutinases are enzymes that are able to break down cutin. In a preferred embodiment, the cutinase is derived from a strain of Aspergillus, in particular Aspergillus oryzae, a strain of Alternaria, in particular Alternaria brassiciola, a strain of Fusarium, in particular Fusarium solani, Fusarium solani pisi, Fusarium roseum culmorum or Fusarium roseum sambucium, a strain of Helminthosporum, in particular Helminthosporum sativum, a strain of Humicola, in particular Humicola insolens, a strain of Pseudomonas, in particular Pseudomonas mendocina or Pseudomonas putida, a strain of Rhizoctonia, in particular Rhizoctonia solani, a strain of Streptomyces, in particular Streptomyces scabies, or a strain of Ulocladium , in particular Ulocladium consortiale. In an extremely preferred embodiment, the cutinase is derived from a strain of Humicola insolens, in particular the strain Humicola insolens DSM 1800. Humicola insolens cutinase is obtained in WO 96/13580 which is incorporated herein by reference. The cutinase may be a variant, for example, one of the variants that in WO 00/34450 and WO 01/92502 which are incorporated herein by reference. Preferred cutinase variants include variants described in Example 2 of WO 01/92502 which is specifically incorporated herein by reference. Preferred commercially available cutinases include NOVOZYM ^™ 51032 (available from Novozymes A / S, Denmark).

The method of the invention may be carried out in the presence of phospholipase classified as EC 3.1.1.4 and / or EC 3.1.1.32. The term phospholipase used herein is an enzyme that has activity against phospholipids. Phospholipids, for example lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an external (sn-1) and middle (sn-2) position and esterified with phosphoric acid in the third position; in turn, the phosphoric acid may be esterified to an aminoalcohol. Phospholipases are enzymes involved in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases A ₁ and A ₂ , which hydrolyze a fatty acyl group (in the sn-1 and sn-2 positions, respectively) to form lysophospholipid, and lysophospholipase (or phospholipase B). which can hydrolyze the residual fatty acyl group in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterases) release diacylglycerol or phosphatidic acid.

The term phospholipase includes enzymes having phospholipase activity, e.g. As phospholipase A (A ₁ or A ₂ ), phospholipase B activity, phospholipase C activity or phospholipase D activity. The term "phospholipase A" used herein in connection with an enzyme of the invention is intended to cover an enzyme having phospholipase A ₁ and / or phospholipase A ₂ activity. The phospholipase activity can be provided by enzymes which also have other activities, for example a lipase with phospholipase activity. For example, the phospholipase activity can be derived from a lipase with phospholipase Secondary activity originate. In other embodiments of the invention, the phospholipase enzyme activity is provided by an enzyme that has substantially only phospholipase activity and in which the phospholipase enzyme activity is not a minor activity.

The phospholipase can be of any origin, for example of animal origin (eg from a mammal), e.g. From pancreas (eg, bovine or porcine pancreas) or snake venom or bee venom. Preferably, the phospholipase may be of microbial origin, e.g. B. from filamentous fungi, yeasts or bacteria, eg. B. the genus or species Aspergillus, z. B. A. niger; Dictyostelium, z. D. discoideum; Mucor, z. M. javanicus, M. mucedo, M. subtilissimus; Neurospora, z. B. crassa; Rhizomucor, e.g. B. pusillus; Rhizopus, z. R. arrhizus, R. japonicus, R. stolonifer; Sclerothinia, e.g. B. S. libertiana; Trichophyton, z. B. T. rubrum; Whetzelinia, z. B. sclerotiorum; Bacillus, e.g. B. megaterium, B. subtilis; Citrobacter, e.g. C. friendii; Enterobacter, e.g. B. E. aerogenes, E. cloacae; Edwardsiella, E. tarda; Erwinia, z. B. E. herbicola; Escherichia, z. B. E. coli; Klebsiella, z. B. K. pneumoniae; Proteus, z. P. vulgaris; Providencia, z. P. stuartii; Salmonella, z. S. typhimurium; Serratia, z. S. liquefasciens, S. marcescens; Shigella, z. B. S. flexneri; Strotomyces, e.g. B. S. violeceoruber; Yersinia, z. B. Y. enterocolitica. Thus, the phospholipase may be fungal, e.g. From the class Pyrenomycetes, for example the genus Fusarium, for example a strain of F. culmorum. F. heterosporum, F. solani or a strain of F. oxysporum. The phospholipase can also be derived from a filamentous fungus in the genus Aspergillus, z. A strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or Aspergillus oryzae.

Preferred phospholipases are from a strain of Humicola, especially Humicola lanuginosa. The phospholipase may be a variant, for example one of the variants described in WO 00/32758 disclosed herein by reference. Preferred phospholipase variants include variants described in Example 5 of WO 00/32758 which is specifically incorporated herein by reference. In another preferred embodiment, the phospholipase is one which in WO 04/111216 Specifically, the variants listed in the table in Example 1 are described.

In another preferred embodiment, the phospholipase is derived from a strain of Fusarium, especially Fusarium oxysporum. The phospholipase may be those that are in WO 98/026057 described in Fusarium oxysporum DSM 2672, or variants thereof. In a preferred embodiment of the invention, the phospholipase is a phospholipase A ₁ (EC 3.1.1.32). In another preferred embodiment of the invention, the phospholipase is a phospholipase A ₂ (EC.3.1.1.4.).

Examples of commercial phospholipases include LECITASE ^™ and LECITASE ^™ ULTRA, YIELSMAX or LIPOPAN F (available from Novozymes A / S, Denmark).

Suitable amylases (alpha and / or beta) include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include e.g. Alpha-amylases obtained from Bacillus, e.g. B. a special strain of B. licheniformis, described in more detail in GB 1,296,839 , or from the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060 , to be obtained.

Examples of useful amylases are the variants described in U.S. Pat WO 94/02597 . WO 94/18314 . WO 96/23873 . WO 97/43424 . WO 01/066712 . WO 02/010355 . WO 02/031124 and PCT / DK2005 / 000469 (all of which references are incorporated by reference).

Commercially available amylases are Duramyl ^™ , Termamyl ^™ , Termamyl Ultra ^™ , Natalase ^™ , Stainzyme ^™ , Fungamyl ^™ and BAN ^™ (Novozymes A / S), Rapidase ^™ and Purastar ^™ (ex 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 by Humicola insolens, Thielavia terrestris, Myceliophthora thermophila and Fusarium oxysporum, disclosed in U.S. Pat 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 ,

Especially suitable cellulases are the alkaline or neutral cellulases which have color care properties. Examples of such cellulases are cellulases which are present in EP 0 495 257 . EP 0 531 372 . WO 96/11262 . WO 96/29397 . WO 98/08940 are described. Other examples are cellulose variants, for example, those described in U.S. Pat WO 94/07998 . EP 0 531 315 . US 5,457,046 . US 5,686,593 . US 5,763,254 . WO 95/24471 . WO 98/12307 and PCT / DK98 / 00299 are described. Commercially available cellulases include Celluzyme ^™ , Carezyme ^™ , Endolase ^™ , Renozyme ^™ (Novozymes A / S), Clazinase ^™ and Puradax HA ^™ (Genencor International Inc.) and KAC-500 (B) ^™ (Kao Corporation).

Suitable peroxidases / oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include Coprinus peroxidases, e.g. From C. cinereus, and variants thereof, such as those found in WO 93/24618 . WO 95/10602 and WO 98/15257 are described. Commercially available peroxidases include Guardzyme ^™ and Novozym ^™ 51004 (Novozymes A / S).

Examples of pectate lyes include pectate lyases cloned from various bacterial genera, for example Erwinia, Pseudomonas, Klebsiella and Xanthomonas and Bacillus subtilis ( Nasser et al. (1003) FEBS Letts. 335: 319-326 ) and Bacillus sp. YA-14 ( Kim et al. (1994) Biosci. Biotech. Biochem. 58: 947-949 ). Purification of pectate lyases with maximum activity in the pH range of 8-10, produced by Bacillus pumilus ( Dave and Vaughn (1971) J. Bacteriol. 108: 166-174 ), B. polymyxa ( Nagel and Vaughn (1961) Arch. Biochem. Biophys. 93: 344-352 ), B. stearothermophilus ( Karbassi and Vaughn (1908) Can. J. Microbiol. 26: 377-384 ), Bacillus sp. ( Hasegawa and Nagel (1966) J. Food Sci. 31: 838-845 ) and Bacillus sp. RK9 ( Kelly and Fogarty (1978) Can. J. Microbiol. 24: 1164-1172 ), has also been described. Any of the above and divalent cation independent and / or thermostable pectate lyases can be used in the practice of the invention. In preferred embodiments, the pectate lyase comprises the amino acid sequence of a pectate lyase which in Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331-334 and Henrissat et al., (1995) Plant Physiol. 107: 963-976 is disclosed. Specifically contemplated pectate lyases are in WO 99/27083 and WO 99/27084 disclosed. Other specifically contemplated pectatlyases derived from Bacillus licheniformis are in the U.S. Patent No. 6,284,524 (this document being incorporated herein by reference). Specifically contemplated pectate lyase variants are in WO 02/006442 discloses, especially the variants which in the examples in WO 02/006442 are disclosed (this document is hereby incorporated by reference).

Examples of commercially available alkaline pectate lyases include BIOPREP ^™ and SCOURZYME ^™ L from Novozymes A / S, Denmark.

Examples of mannanases (EC 3.2.1.78) include mannases of bacterial and fungal origin. In a specific embodiment, the mannase is derived from a strain of the filamentous fungus of the genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus ( WO 94/25576 ). WO 93/24622 discloses a mannanase isolated from Trichoderma reseei. Mannanases have also been isolated from various bacteria, including Bacillus organisms. Talbot et al., Appl. Environ. Microbiol., Vol. 56, No. 11, pp. 3505-3510 (1990) For example, a beta-mannanase derived from Bacillus stearothermophilus describes. Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from Bacillus subtilis. JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp. comes. JP-A-63056289 describes the preparation of an alkaline, thermostable beta-mannanase. JP-A-63036775 refers to the Bacillus microorganism FERM P-8856, which produces beta-mannanase and beta-mannosidase. JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001. A purified mannanase from Bacillus amyloliquefaciens is in WO 97/11164 disclosed. WO 91/18974 describes a hemicellulase, for example a glucanase, xylanase or active mannanase. Families 5 and 26 of alkaline mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp. and Humicola insolens, disclosed in WO 99/64619 , come. Specifically contemplated are the Bacillus sp. Mannanases described in the examples in WO 99/64619 are described, this document being incorporated herein by reference.

Examples of commercially available mannanases include Mannaway ^™ available from Novozymes A / S Denmark.

Any enzyme present in the agent can be stabilized using conventional stabilizing agents, e.g. With a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid or a boric acid derivative, for example an aromatic borate ester, or a phenylboronic acid derivative, for example 4-formylphenylboronic acid, and the agent can be formulated as described e.g. In WO 92/19709 and WO 92/19708 is described.

hydrotropes:

The term "hydrotrope" generally means a compound having the ability to increase the solubilities, preferably solubilities in water, of certain sparingly soluble organic compounds. Examples of hydrotropes include sodium xylene sulfonate, SCM.

Solvent:

The composition may comprise a solvent, for example, water or an organic solvent, such as isopropyl alcohol or glycol ether. Solvents can be in liquid or gel compositions or agents.

Metal-chelating agent:

The composition or agent may contain a metal chelating agent, for example carbonates, bicarbonates and sesquicarbonates. The metal chelating agent may be a bleach stabilizer (i.e., a heavy metal sequestering agent). Suitable bleach stabilizers include ethylenediamine tetraacetate (EDTA), diethylenetriamine pentaacetate (DTPA), ethylenediamine disuccinate (EDDS) and the polyphosphonates, for example the Dequests (trademark), ethylenediamine tetramethylene phosphonate (EDTMP) and diethylenetriamine pentamethylene phosphate (DETPMP). In general, metal chelating agents will not be present in part (a) of the composition, as microbial function may be degraded if metal ions are not available.

Builder or complexing agent:

Builder materials can be selected from 1) calcium masking materials, 2) precipitating materials, 3) calcium ion exchange materials, and 4) mixtures thereof.

Examples of calcium masking builder materials include alkali metal polyphosphates, for example, sodium tripolyphosphate, and organic sequestrants, for example, ethylenediaminetetraacetic acid.

Examples of builder builders include sodium orthophosphate and sodium carbonate.

Examples of calcium ion exchange builder materials include the various types of water-soluble crystalline or amorphous aluminosilicates, of which zeolites are the best known representatives, e.g. Zeolite A, zeolite B (also known as zeolite P), zeolite C, zeolite X, zeolite Y and also the zeolite P type, as in EP-A-0,384,070 described. The agent may also contain 0-65% of a builder or complexing agent, for example, ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic acid, alkyl- or alkenylsuccinic acid, nitrilotriacetic acid, or the other builders mentioned below. Many builders are bleach-stabilizers because of their ability to complex metal ions.

When a builder is present, the agents may suitably contain less than 7% by weight, preferably less than 10% by weight, and most preferably less than 10% by weight of builder.

The agent may contain as builder a crystalline aluminosilicate, preferably an alkali metal aluminosilicate, more preferably a sodium aluminosilicate. This is typically present at a level of less than 15% by weight.

Aluminosilicates are materials that have the general formula: 0.8-1.5 M ₂ O, Al ₂ O ₃ , 0.8-6 SiO ₂ where M is a monovalent cation, preferably sodium. These materials contain some bound water and are required to have a calcium ion exchange capacity of at least 50 mg CaO / g. The preferred sodium aluminosilicates contain 1.5-3.5 SiO ₂ units in the above formula. They can be readily prepared by reaction between sodium silicate and sodium aluminate, as extensively described in the literature. The ratio of surfactants to aluminosilicate (if present) is preferably greater than 5: 2, more preferably greater than 3: 1.

Alternatively or in addition to the aluminosilicate builders, phosphate builders can be used. In this area, the term "phosphate" includes diphosphate, triphosphate, and phosphonate species. Other forms of builder include silicates, for example, soluble silicates, metasilicates, layered silicates (eg, SKS-6 from Hoechst).

For low cost formulations, carbonate (including bicarbonate and sesquicarbonate) and / or citrate may be used as builders.

polymers:

The agent may comprise one or more polymers. Examples are carboxymethylcellulose, poly (vinylpyrrolidone), poly (ethylene glycol), poly (vinyl alcohol), poly (vinylpyridine N-oxide), poly (vinylimidazole), polycarboxylates, for example polyacrylates, maleic / acrylic acid copolymers and lauryl methacrylate / acrylic acid copolymers ,

Modern detergents typically use polymers as so-called "dye transfer inhibitors." These prevent a migration of dyes, especially during long soaking times or exposure times. Any suitable dye transfer inhibiting agents can be used in accordance with the present invention. In general, such dye transfer inhibiting agents include polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, manganese phthalocyanine, peroxidases, and mixtures thereof.

Nitrogen-containing dye-binding DTI polymers are preferred. Of these, preferred are polymers and copolymers of cyclic amines, for example, vinylpyrrolidone and / or vinylimidazole. Polyamine N-oxide polymers suitable for use herein contain moieties having the following structural formula: RA _x -P, where P is a polymerizable moiety to which an NO group may be attached, or the NO- Group may be part of the polymerizable unit; A is one of the following structures: -NC (O) -, -C (O) O-, -S-, -O-, -N =; x is 0 or 1 and R is an aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic group or a combination thereof to which the nitrogen of the NO group may be attached, or the NO group is part of these groups or the NO group is Group can be bound to both units. Preferred polyamine N-oxides are those in which R is a heterocyclic group, for example pyridine, pyrrole, imidazole, pyrrolidine, piperidine and derivatives thereof. The NO group can be represented by the following general structures: N (O) (R ') _0-3 or = N (O) (R') _0-1 wherein each R 'is independently an aliphatic, aromatic, heterocyclic or alicyclic group or a combination thereof, and the nitrogen of the NO group may be bonded to or form part of any of the above groups. The amine oxide unit of the polyamine N-oxides has a pKa <10, preferably pKa <7, more preferably pKa <6.

A polymer backbone may be used provided the amine oxide polymer formed is water soluble and has dye transfer inhibiting properties. Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates, and mixtures thereof. These polymers include random or block copolymers wherein one monomer type is an amine N-oxide and the other monomer type is an N-oxide. The amine N-oxide polymers typically have an amine to amine N-oxide ratio of from 10: 1 to 1: 1,000,000. However, the number of amine oxide groups present in the polyamine oxide polymer can be altered by suitable copolymerization or by a suitable degree of N-oxidation. The polyamine oxides can be obtained in almost any degree of polymerization. Typically, the average molecular weight is in the range of 500 to 1,000,000, more preferably 1,000 to 500,000, most preferably 5,000 to 100,000. This preferred class of materials is referred to herein as "PVNO". A preferred polyamine N-oxide is poly (4-vinylpyridine-N-oxide), which has an average molecular weight of about 50,000 and an amine to amine N-oxide ratio of about 1: 4.

Copolymers of N-vinylpyrrolidone and N-vinylimidazole polymers (referred to as a class "PVPVI") are also preferred. Preferably, the PVPVI has a range of average molecular weight of from 5,000 to 1,000,000, more preferably from 5,000 to 70,000, and most preferably from 10,000 to 7,000, as determined by light scattering, as in U.S. Pat Barth et al., Chemical Analysis, Vol. 113, "Modern Methods of Polymer Characterization" is described. The preferred PVPVI copolymers typically have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone of from 1: 1 to 0.2: 1, more preferably from 0.8: 1 to 0.3: 1, most preferably from 0.6: 1 to 0 , 4: 1. These copolymers can be either linear or branched be. Suitable PVPVI polymers include Sokalan ^(TM) HP56, commercially available from BASF, Ludwigshafen, Germany.

Also, as dye transfer inhibiting agents, polyvinylpyrrolidone polymers ("PVP") having an average molecular weight of from about 5,000 to about 400,000, preferably from about 5,000 to about 700,000, and more preferably from about 5,000 to about 50,000 are also preferred. PVPs are for example in EP-A-262,897 and EP-A-256,696 disclosed. Suitable PVP polymers include Sokalan ^(TM) HP50, commercially available from BASF. Agents containing PVP may also contain polyethylene glycol ("PEG") having an average molecular weight of from about 500 to about 100,000, preferably from about 1,000 to about 10,000. Preferably, the ratio of PEG to PVP based on ppm delivered in wash solutions is from about 2: 1 to about 50: 1, and more preferably from about 3: 1 to about 10: 1.

Also suitable as inhibiting agents of dye transfer are those which are of the class of modified polyethylenimine polymers as described, for example, in U.S. Pat WO-A-0005334 are disclosed. These modified polyethyleneimine polymers are water-soluble or dispersible modified polyamines. Modified polyamines are also available in US-A-4,548,744 ; US-A-4,597,898 ; Us-A-4,877,896 ; US-A-4,891,160 ; US-A-4,976,879 ; US-A-5,415,807 ; GB-A-1,537,288 ; GB-A-1,498,57 ; DE-A-28 29022 and JP-A-06313271 disclosed.

Preferably, the agent according to the present invention comprises a dye transfer inhibiting agent consisting of polyvinylpyridine N-oxide (PVNO), polyvinylpyrrolidone (PVP), polyvinylimidazole, N-vinylpyrrolidone and N-vinylimidazole copolymers (PVPVI), copolymers thereof, and mixtures thereof is selected.

The amount of dye transfer inhibiting agent in the composition according to the invention will be from 0.01 to 10%, preferably from 0.02 to 5%, more preferably from 0.03 to 2% by weight of the composition.

Other detergent ingredients:

The composition may also contain other conventional detergent ingredients, e.g. As fabric conditioning agents, including clay, foam, foam suppressant (antifoaming agent), anti-corrosion agents, soil suspending agents, agents against re-deposition of dirt, other dyes, antimicrobial agents, optical brighteners, anti-fogging agents or perfumes included.

Various non-limiting embodiments of the invention will be described in more detail below with reference to the following figure, wherein:

1 shows a packaged laundry product according to an embodiment of the invention.

As far as the drawing is concerned, it becomes a packaged laundry product 1 shown. The product 1 includes a flowable detergent 3 in a packaging 5 wherein the high viscosity detergent 3 corresponds to Example A or B described in detail below.

The package comprises a compressible container, in this example a plastic bottle 7 containing the flowable wash gel 3 high viscosity, and a dispensing device 9 containing a fabric pre-treatment device 11 has installed. The dispenser device 9 is located at the base 13 of the container 7 and is from a dosing closure device 13 locked in. The closure 13 includes the supporting base 13 the packaging 5 ,

The bottle 7 and the dispenser device 9 (including pretreatment agents 11 ) are interconnected by screw connection. The closure 13 is also connected by a screw with the bottle (screw not shown). In a separate embodiment, the closure becomes 13 using a snap connection with the bottle 7 connected, this snap connection does not require turning the bottle / closure on / to.

The bottle 7 is made of a flexible plastic material comprising polyethylene terephthalate.

The top 21 the bottle is shown flat, but it may be curved in other embodiments, as is the dashed line 22 indicates to prevent upside down storage.

The closure 13 comprises an enlarged (with respect to at least the neck region of the bottle) flat, generally planar bottom surface 15 , By having an enlarged flat top 15 is provided, the surface allows the shutter 13 as a supporting base with the bottle 7 acting in reverse position to thereby the gel 3 high viscosity (under gravity) during storage on the dispenser 9 to collect.

In addition, the closure includes 13 a reservoir part 17 in which the pretreatment agent 11 is included, 26 , The shutter is outward towards the surface 15 glued to provide a stable base. The area of the surface 15 is bigger than the top 21 the device.

The dispenser device 9 includes an opening through which a discharge can take place. The opening comprises a valve 21 in fluid communication via line 23 , The valve 21 includes a membrane that extends through an opening 25 in the dispensing part or dispenser part 9 extends.

In one embodiment, the membrane has a bent portion (not shown) that faces the container 7 is directed. The bent portion of the membrane is equipped with intersecting slots to define a plurality of generally triangular blades. As contents of the container for dispensing are pressurized, the triangular blades flex toward the open end of the opening 25 , passing product through the opening 25 let go. As the dispensing pressure is released, the triangular blades spring back to their original position and act to block a product passageway through the opening 25 , The blades of the valve are sufficiently elastic that they will not flex open unless the applied pressure exceeds the hydraulic static head pressure created by a filling of seasoning. In use, the fluid is pressurized to pass and partially becomes the pretreatment agent 11 collected, ready for cleaning.

Some of the fluid in the pretreatment center part 11 may remain during storage from the pretreatment agent 11 drip and gets into the reservoir part 17 collected for use in the next wash. This reduces waste of the product.

Exemplary detergent formulation A

The following gel detergents were prepared, wherein agent A is according to the invention. component Wt .-% propylene glycol 8.0 sodium citrate 3.9 borax 3.0 NaOH (50%) 1.1 Monoethanolamine 1.0 LAS acid 4.4 coconut fatty acid 1.5 Nonionic surfactant 11.1 oleic acid 2.3 1-dodecanol 5.0 Protease enzyme 0.3 Lipase enzyme 0.5 Perfume 0.2 Water rest on 100 in which:
Borax: sodium tetraborate (10 aq)
nonionic surfactant: ethoxylated alcohol with an average of 9 ethylene oxide groups.

It has been found that the gel detergent, for which Agent A is an example, is shear thinning and stable. In addition, typical detergent particles with a density between 0.8 and 0.9 g / cm ³ and having a diameter of up to 5000 μm, be stably suspended in this medium for more than 2 weeks without any observable net movement of the particles. sample Viscosity / Pa.s Eta 0 critical tension Tan-Delta 20 s ^-1 100 s ^-1 Pa.s Pa at 1 Hz A 2.11 0.61 3.00 E + 05 15 0.04

To obtain the values shown in the above table, all rheological measurements were made using a Carrimed CSL 100 rheometer with a cone and plate geometry specially roughened to prevent slippage.

Viscosity was measured at varying shear rates from very slow shear to a shear plan in excess of 100 s ^-1 . Two situations are shown: viscosity measured at relatively low shear (20 s ^-1 ) and that measured at much higher shear (100 s ^-1 ). It can be seen that the viscosity of high shear agent A is much lower than that observed at low shear whereas high and low shear agent B shows almost the same viscosity. In other words, means A becomes thinner in shear, whereas means B does not.

In addition, the critical stress is shown. This parameter represents the stress at which the material leaves the upper Newtonian plateau and becomes thinner under increased shear. "Eta 0" values are also shown, referring to the viscosity calculated for shear from creepage measurements.

Finally, "tan-delta" values are given that relate to the loss ratio over storage moduli (G "/ G ') and reflect the dominance of viscous versus elastic properties, so that materials that are very low" tan-delta " Values (zero bias, e.g. mean A in the above table) will be much more elastic than those giving higher "tan delta" values (90 bias).

Exemplary detergent formulation B

The following gel detergents were prepared, wherein agent C is according to the invention and agent D is a comparison agent according to the prior art: component Wt .-% propylene glycol 4.75 sodium citrate 2.8 borax 2.3 NaOH (50%) 0.43 Monoethanolamine 0.23 LAS acid 6.0 coconut fatty acid 0.77 Sodium alcohol EO sulphate 10.5 Nonionic surfactant 6.6 1-decanol 6.0 Protease enzyme 0.45 Lipase enzyme 0.25 Perfume 0.2 Water rest too 100 in which:
Borax: sodium tetraborate (10 aq)
nonionic surfactant: ethoxylated alcohol with an average of 9 ethylene oxide groups

Sodium alcohol EO sulphate: ethoxylated alcohol sulphate with an average of 3 ethylene oxide groups.

Agent B is a stable, transparent, pourable, shear thinning liquid capable of containing typical detergent particles having a density of between 0.8 and 0.9 g / cm ³ and a diameter of up to 5000 μm for more than 2 Weeks without observable net movement of the particles stably suspend.

Critical rheological parameters for the two agents are given below. sample Viscosity / Pa.s Eta 0 critical tension Tan-Delta 20 s ^-1 100 s ^-1 Pa.s Pa at 1 Hz B 1.33 0.48 9.85 E + 05 10 0.07

For an explanation of the rheological values given in this table, reference is made to the description relating to the similar table given in Example A above.

It is to be understood that the invention is not to be limited to the details of the above embodiments, which are described by way of example only.

QUOTES INCLUDE IN THE DESCRIPTION

This list of the documents listed by the applicant has been generated automatically and is included solely for the better information of the reader. The list is not part of the German patent or utility model application. The DPMA assumes no liability for any errors or omissions.

Cited patent literature

• EP 251446 [0030]
• WO 91/00345 [0030]
• EP 525610 [0030]
• WO 94/02618 [0030]
• WO 89/06279 [0033]
• WO 89/06270 [0033]
• WO 94/25583 [0033]
• WO 92/19729 [0034]
• WO 98/20115 [0034]
• WO 98/20116 [0034]
• WO 98/34946 [0034]
• EP 258068 [0035]
• EP 305216 [0035]
• WO 96/13580 [0035, 0039]
• EP 218272 [0035]
• EP 331376 [0035]
• GB 1372034 [0035]
• WO 95/06720 [0035]
• WO 96/27002 [0035]
• WO 96/12012 [0035]
• JP 64/744992 [0035]
• WO 91/16422 [0035]
• WO 92/05249 [0036]
• WO 94/01541 [0036]
• EP 407225 [0036]
• EP 260105 [0036]
• WO 95/35381 [0036]
• WO 96/00292 [0036]
• WO 95/30744 [0036]
• WO 94/25578 [0036]
• WO 95/14783 [0036]
• WO 95/22615 [0036]
• WO 97/04079 [0036]
• WO 97/07202 [0036]
• WO 00/34450 [0039]
• WO 01/92502 [0039, 0039]
• WO 00/32758 [0043, 0043]
• WO 04/111216 [0043]
• WO 98/026057 [0044]
• GB 1296839 [0046]
• WO 95/026397 [0046]
• WO 00/060060 [0046]
• WO 94/02597 [0047]
• WO 94/18314 [0047]
• WO 96/23873 [0047]
• WO 97/43424 [0047]
• WO 01/066712 [0047]
• WO 02/010355 [0047]
• WO 02/031124 [0047]
• DK 2005/000469 [0047]
• US 4435307 [0049]
• US 5648263 [0049]
• US 5691178 [0049]
• US 5776757 [0049]
• WO 89/09259 [0049]
• WO 96/029397 [0049]
• WO 98/012307 [0049]
• EP 0495257 [0050]
• EP 0531372 [0050]
• WO 96/11262 [0050]
• WO 96/29397 [0050]
• WO 98/08940 [0050]
• WO 94/07998 [0050]
• EP 0531315 [0050]
• US 5457046 [0050]
• US 5686593 [0050]
• US Pat. No. 5,763,254 [0050]
• WO 95/24471 [0050]
• WO 98/12307 [0050]
• DK 98/00299 [0050]
• WO 93/24618 [0051]
• WO 95/10602 [0051]
• WO 98/15257 [0051]
• WO 99/27083 [0052]
• WO 99/27084 [0052]
• US 6284524 [0052]
• WO 02/006442 [0052, 0052]
• WO 94/25576 [0054]
• WO 93/24622 [0054]
• JP 03047076 A [0054]
• JP 63056289 A [0054]
• JP 63036775A [0054]
• JP 08051975A [0054]
• WO 97/11164 [0054]
• WO 91/18974 [0054]
• WO 99/64619 [0054, 0054]
• WO 92/19709 [0056]
• WO 92/19708 [0056]
• EP 0384070 A [0063]
• EP 262897A [0074]
• EP 256,696A [0074]
• WO 0005334 A [0075]
• US 4548744A [0075]
• US 4597898 A [0075]
• US 4877896A [0075]
• US 4891160 A [0075]
• US 4976879 A [0075]
• US 5415807 A [0075]
• GB 1537288A [0075]
• GB 149857A [0075]
• DE 2829022 A [0075]
• JP 06313271 A [0075]

Cited non-patent literature

• Dartois et al. (1993), Biochemica et Biophysica Acta, 1131, 253-360 [0035]
• Nasser et al. (1003) FEBS Letts. 335: 319-326 [0052]
• Kim et al. (1994) Biosci. Biotech. Biochem. 58: 947-949 [0052]
• Dave and Vaughn (1971) J. Bacteriol. 108: 166-174 [0052]
• Nagel and Vaughn (1961) Arch. Biochem. Biophys. 93: 344-352 [0052]
• Karbassi and Vaughn (1908) Can. J. Microbiol. 26: 377-384 [0052]
• Hasegawa and Nagel (1966) J. Food Sci. 31: 838-845 [0052]
• Kelly and Fogarty (1978) Can. J. Microbiol. 24: 1164-1172 [0052]
• Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331-334 [0052]
• Henrissat et al., (1995) Plant Physiol. 107: 963-976 [0052]
• Talbot et al., Appl. Environ. Microbiol., Vol. 56, No. 11, pp. 3505-3510 (1990) [0054]
• Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) [0054]
• Barth et al., Chemical Analysis, Vol. 113, "Modern Methods of Polymer Characterization" [0073]

Claims (8)

A packaged laundry product comprising a flowable detergent contained in a bottom-releasing package, wherein (i) the flowable detergent has a viscosity of at least 100 Pa · s, preferably at least 500 Pa · s when at rest or up to one Shear stress of 10 Pa., And comprising at least one surfactant and at least one hydrotrope; and (ii) the bottom-dispensing package comprises a compressible container in which the flowable detergent is stored and a metering device incorporating a fabric treatment device, wherein the metering device and the tissue pretreatment device are located at the bottom of the compressible container, characterized in that the tissue treatment container is enclosed by a dosage closure device that provides a bearing base of the packaging, and wherein the packaging has a curved top. A packaged laundry product according to claim 1, wherein the hydrotrope is present at 0.1 to 10% by weight of the total composition. A packaged laundry product according to any preceding claim, wherein the metering device comprises a channel or conduit providing fluid communication between the reservoir and the pretreatment means. A packaged laundry product according to any preceding claim, wherein the pretreatment means comprises a device allowing mechanical cleaning, for example a body having many projections. The packaged laundry product of claim 5, wherein the projections are flexible so that they move during cleaning, providing a lightweight cleaning process. A packaged laundry product according to claim 5 or 6, wherein some or all of the projections are semi-rigid or rigid so as to provide a stronger mechanical cleaning operation. A packaged laundry product according to any one of the preceding claims wherein the pretreatment means comprises a generally hemispherical body having many projections extending radially therefrom. A packaged laundry product according to any preceding claim, wherein the composition is a shear-thinning gel-type agent having a shear stress of less than 300 Pa · s.

Images