ES2625487T3 - A viscous laundry product and packaging thereof - Google Patents

Abstract

A packaged laundry product comprising a fluid laundry composition contained in a package, in which (i) the fluid laundry composition has a viscosity of at least at least 100 Pa.s, preferably at least 500 Pa.s , when at rest or up to a shear stress of 10 Pa and comprises at least one surfactant and at least one enzyme; and (ii) the package comprises a compressible container in which the fluid laundry composition is stored and a dispensing device that incorporates a device for tissue pre-treatment and is located at the base of the compressible container and is enclosed by a device of closing of dosage that provides a base of support of the container, characterized in that the dispensing device comprises a channel or conduit that provides fluid communication between the reservoir and the pre-treater and because the pre-treater comprises a device that allows mechanical cleaning , which comprises a hemispherical body with multiple projections that extend radially therefrom.

Description

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DESCRIPTION

A product of viscous lavender and packaging thereof

The present invention relates to a viscous lavender product and packaging thereof.

One objective is to provide an improved pre-treatment device for the precise pre-treatment of stains on laundry clothes.

U.S. Pat. 6233771 discloses a cleaning device for cleaning tissue stains without causing damage to the fiber. The device is a portable device with a convex face comprising treatment means, such as fibers. During use, the stained fabric is moistened with a cleaning composition and the device is rolled or shaken on the stained area. The fibers mechanically detach the stain. The device is especially useful as a previous marker in a dry cleaning operation.

WO 2007/130563 discloses gel detergent compositions in dispensing containers at the bottom that can be used as pre-treaters.

Accordingly, in a first aspect, the present invention provides a packaged lavender product comprising a fluid lavender composition contained in a package, in which

(i) the fluid lavender composition has a viscosity of at least at least 100 Pa.s, preferably at least 500 Pa.s, when at rest or up to a shear stress of 10 Pa and comprises at least one surfactant and at least one enzyme; Y

(ii) the package comprises a compressible container in which the fluid lavender composition is stored and a dispensing device that incorporates a device for the pre-treatment of the tissue and is located at the base of the compressible container and is enclosed by a Dosing closure device that provides a support base of the container, characterized in that the dispensing device comprises a channel or conduit that provides fluid communication between the reservoir and the pre-treater and that the pre-treater comprises a device that allows cleaning mechanics, comprising a semi-spherical body with multiple projections that extend radially from it

The advantage of the above provision is that it offers greater control in the application of a highly viscous composition with respect to stained areas. The dispensing of controlled quantities of high viscosity fluids from portable products can be ergonomically difficult and many users resort to the application of a blow to the device (by hitting the base, or by slapping the sides), which interferes with precision of dosing and, frequently, results in overdosing, spills, etc.

The arrangement of the invention, as a consequence of the dispensing / pretreatment part being positioned at the base of the tank, implies that the user does not need to invert the container to dose / pretreat or wait until the viscous fluid flow from the base to the top (where the dispensing / pre-treatment devices are normally located). With the present invention, gravity keeps the pre-treatment device loaded with the composition. The dispensing device does not need to include complicated and expensive seals / valves, since the dosage closure encloses the pre-treatment device and provides the basis: this allows the advantage that no dripping of the composition that falls from the pre-device - treatment after use, is collected in the base of the support, which can then be placed directly in the washing machine / receptacle, which minimizes losses.

The dispensing device may comprise a channel or conduit that provides fluid communication between the reservoir and the pre-treater.

The pre-treater may comprise a device that allows mechanical cleaning, such as a body with multiple projections. The projections can be flexible so that they move during cleaning by providing a light cleaning action. As an alternative, some or all of the projections can be semi-rigid or nested in such a way as to provide a more rigorous mechanical cleaning action. The projections can be thin, for example, bristles to provide a brush type device, or thicker in order to provide finger type projections.

The container may have a curved upper part to deter users of head-down bottle storage. In this way the package is more likely to be stored in a pre-treater-loading position, that is, with the fluid-accumulated lavender composition accumulated by gravity at the base of the container.

In one embodiment, the pre-treater comprises a generally hemispherical body with multiple projections that extends radially therefrom.

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The composition is preferably a gel-like composition that fluidizes at shear. The viscosity under 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 it is, at most, 1 Pa.s and most preferably 0, 5 Pa.s.

Compositions that fluidize at shear may comprise a polymeric gum, for example, Xanthan gum or other gum capable of forming stable continuous gum networks that can suspend particles.

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

Another useful procedure is to change a non-gelled formulation in order to form an internal structure in which the structure provides the desired properties to the gel-type detergent thus formed. The composition may comprise a soap or fatty acid in combination with sodium sulfate and one or more surfactants can be used to form a gelled structure by forming lamellar phases.

The composition may comprise dispersions of lamellar phases from micellar surfactant systems, and additionally a structuring agent for establishing the lamellar phase, whereby said structure can be a fatty alcohol.

The composition of the invention contains one or more surfactants and / or optionally other ingredients, such that the composition is fully functional as a composition for the care and / or cleaning of lavender. A composition of the invention may be provided in solid or liquid form. If it is in a solid form, the composition can be rehydrated and / or dissolved in a solvent, including water, before use. The composition may be provided in a concentrated form to be diluted or it may be a ready-to-use (in use) composition.

The present invention is suitable for use in compositions for industrial or domestic fabric washing. Likewise, the present invention can be applied to compositions for the care of industrial or domestic non-detergent based fabrics.

Further on, other contemplated ingredients that include hydrotropes, preservatives, fillers, adjuvants, complexing agents, polymers, stabilizers, perfumes per se, other conventional detergent ingredients, or combinations of one or more thereof are set forth.

Surfactants:

The compositions for washing fabrics according to the present invention comprise a detergent material for washing fabrics selected from anionic non-soap surfactant, non-ionic surfactants, soap, amphoteric surfactants, zwitterionic surfactants and mixtures thereof.

Detergent compositions suitable for use in domestic or industrial automatic fabric washing machines generally contain anionic non-soap or non-ionic surfactant, or combinations of the two in suitable relation, as is known to the person skilled in the art, optionally in conjunction with soap.

Surfactants may be present in the composition in a proportion of from 0.1% to 60% by weight.

Suitable anionic surfactants include alkyl benzene sulphonate, primary and secondary alkyl sulfates, particularly C8-C15 primary alkyl sulfates; alkyl ether sulfates; olefin sulfonates; alkyl xylene sulfonates; dialkyl sulfosuccinates; ether carboxylates; isethionates; sarcosinates; fatty acid ester sulphonates and mixtures thereof. Sodium salts are generally preferred. When included in the present invention, the composition usually contains from about 1% to about 50%, preferably 10% by weight-40% by weight, based on the tissue treatment composition, of an anionic surfactant such as alkyl- linear benzene sulphonate, alpha-olefin sulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxy sulfate, secondary alkanesulfonate, methyl ester of fatty alpha-sulfo acid, alkyl- or alkenyl succinic acid or soap. Preferred surfactants are alkyl ether sulfates and mixtures of non-ionic alkyl alkoxylated surfactants with either alkyl sulphonates or alkyl ether sulfates.

Preferred alkyl ether sulfates are C8-C15 alkyl and have 2-10 moles of ethoxylation. Preferred alkyl sulfates are alkylbenzene sulphonates, particularly linear alkylbenzene sulphonates having an alkyl chain length of C8-C15. The counter ion for anionic surfactants is typically sodium, although other counterions such as TEA or ammonium can be used. Suitable anionic surfactant materials are available on the market as the "Genapol" range from Clariant.

Nonionic surfactants include primary and secondary alcohol ethoxylates, especially ethoxylated C8-C7 aliphatic alcohol with an average of from 1 to 7 moles of ethylene oxide per mole of alcohol, and more especially C10- primary and secondary aliphatic alcohols. C15 ethoxylates with an average of 1 to 10 moles of ethylene oxide per mole of alcohol. Non-ethoxylated nonionic surfactants include alkyl polyglucosides, glycerol monoethers and polyhydroxy amides (glucamide). Mixtures of non-ionic surfactant can be used. When

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When included in the present invention, the composition usually contains from about 0.2% to about 40%, preferably 1 to 7% by weight, more preferably 5 to 15% by weight of a non-ionic surfactant such as alcohol ethoxylate, Nonylphenol ethoxylate, alkyl polyglucoside, alkyldimethylamine oxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy fatty acid amide, or N-acyl derivatives N-alkyl glucosamine ("glucamides").

Non-ionic surfactants that can be used include primary and secondary alcohol ethoxylates, especially ethoxylated C8-C7 aliphatic alcohols with an average of from 1 to 36 moles of ethylene oxide per mole of alcohol, and more especially primary and aliphatic alcohols. of C10-C15 ethoxylates with an average of 1 to 10 moles of ethylene oxide per mole of alcohol.

Enzymes

Depending on the case, one or more enzymes may be suitable. It is understood that enzyme variants (produced, for example, by recombinant techniques) are included within the meaning of the term "enzyme." Examples of such enzyme variants are disclosed, for example, in Patents 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 appropriately incorporated into granules of the invention include oxidoreductases, hydrolase transferases, liases, isomerases and ligases, that is, respectively (EC 1.-.-.-), (EC 2.-. -.-), (EC 3.-.-.-), (EC 4.-.-.-), (EC 5.-.-.-), (EC 6.-.-.-), in which said classification of enzymes is in accordance with the Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Academic Press, Inc., 1992.

Especially contemplated are enzymes that include proteases, alpha-amylases, cellulases, lipases, peroxidase / oxidases, pectate liases, and mannanases, or mixtures thereof. The most preferred enzymes are proteases.

Suitable proteases include those of animal, plant or microbial origin. The one of microbial origin is preferred. They include genetically engineered or chemically modified mutants. The protease may be a serine protease or a metalloase protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases are subtilisins, especially those obtained from Bacillus, for example Novo subtilisin, Carlsberg subtilisin, 309 subtilisin, 141 subtilisin and 168 subtilisin (described in WO 89/06279). Examples of trypsin-like proteases are trypsin (for example, of porcine or bovine origin) and Fusarium protease described in WO 89/06270 and WO 94/25583.

Examples of useful proteases are the variants described in Patents WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially variants with substitutions in one or more 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 ™, Espe - raseTM, Everlase ™, Polirazyme ™, and KanaseTM, (Novozymes A / S), Maxatase ™, Maxacal ™, Maxapem ™, ProperaTM, Purafect ™, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).

Suitable lipases include those of bacterial or fungal origin. The genetically engineered or chemically modified mutants are included. Examples of useful lipases include lipases from Humicola (synonymous with Thermomyces), for example from H. lanuginosa (T. lanuginosus), as described in EP Patents 258 068 and EP 305 216, or from H insolens, as described in Patent WO 96/13580, a Pseudomonas lipase, for example, from P. alkalgenes or P. pseudoaligens (EP Patent 218 272), P. cepacia (EP Patent 331 376), P. stutzen (Patent GB 1,372,034), P. fluorescens, Pseudomonas sp. Strain sD 705 (Patents WO 95/06720 and wO 96/27002), P. wiscosinensis (Patent WO 96/12012), a Bacillus lipase, for example from B. subtilis (Dartois et al., Biochemica et Biophysica Acta, vol. 1131, pages 253-360, (1993)), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).

Other examples are lipase variants such as those described in WO 92/05249, WO 94/01541, EP 407 225, EP 260 105, WO 95/36381, WO 06/00292, WO 95/30744, WO 94/25578 , WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202.

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

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

Cutinases are enzymes that are capable of degrading cutin. In a preferred embodiment, the cutinase is obtained from an Aspergillius strain, in particular Aspergillus oryzae, an Alternaria strain, in particular Alternaria brassiciola, a Fussarium strain, in particular Fussarium Solani, Fussarium Solani pisi, Fussarium roseum culmo- rum, or Fossarium roseum sambucium, a strain of Helminthosporum, in particular Helminthosporum sativum, a

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strain of Humicola, in particular Humicola insolens, a strain of Pseudomonas, in particular Pseudomonas mendocin, 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 a most preferred embodiment, the cutinase is obtained from a strain of Humicola insolens, in particular the Humicola insolens DSM l800 strain. The Humicola insolens cutinase is described in WO 96/13580, which is thereby incorporated by reference The cutinase may be a variant, such as one of the variants disclosed in WO 00/34450 and WO 01/92502, which are therefore incorporated by reference. Preferred cutinase variants include variants listed in Example 2 of Patent 01/92502, which is therefore specifically incorporated by reference.

Commercially preferred cutinases include NOVOZYM ™ 51032 (available from Novozymes A / S, Denmark).

The process of the invention can be carried out in the presence of phospholipase classified as EC 3.1.1.4 and / or EC 3.1.1.32. As used in the present invention, the term phospholipase is an enzyme that has activity against phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in the outer (sn-1) and central (sn-2) positions and esterified with phosphoric acid in the third position; in turn, phosphoric acid can be esterified to an amino alcohol. Phospholipases are enzymes that participate in the hydrolysis of phospholipids. Various types of phospholipase activity can be distinguished, including phospholipases A1 and A2, which hydrolyse a fatty acyl group (in position sn-1 and sn-2, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B), which can hydrolyze the fatty acyl group remaining in lysophospholipid. Phospholipase C and phospholipase D (phosphodiestearases) release diacyl glycerol or phosphatidic acid, respectively.

The term phospholipase includes enzymes with phospholipase activity, for example, phospholipase A (A1 or A2), phospholipase B activity, phospholipase C activity or phospholipase D activity. The term "phospholipase A" as used herein in connection with a Enzyme of the invention is intended to encompass an enzyme with activity Phospholipase A1 and / or Phospholipase A2. The phospholipase activity can be provided by enzymes that also have other activities, such as, for example, a lipase with phospholipase activity. The phospholipase activity can proceed, for example, from a lipase with secondary phospholipase activity. In other embodiments of the invention, the phospholipase enzyme activity is provided by an enzyme that essentially has only phospholipase activity and in which the phospholipase enzyme activity is not a secondary activity.

The phospholipase can be of any origin, for example of animal origin (such as, for example, mairnfero), for example from pancreas (for example, pig or bovine pancreas), or of snake venom or bee venom. Preferably, the phospholipase may be of microbial origin, for example, from filamentous fungi, yeast or bacteria, such as of the genus or Aspergillus species, for example, A. niger; Dictyostelium, for example, D. discoideum; Mucor, for example, M. javanicus, M. mucedo, M. subtilissimus; Neurospora, for example, N. carasa; Rhizomucor, for example, R. pusillus; Rhizopus, for example, R. arrhizus, R. japonicus, R. stolonifer; Sclerosonia, for example, S. libertiana; Trychophyton, for example T. robrum; Whetzelinia, for example W. sclerotiorum; Bacillus, for example, B. megaterium, B. subtilis; Citrobacter, for example, C. freundii; Enterobacter, for example, E. aerogenes, E. cloacae; Edwardsiella, for example, E. takes; Erwinia, for example, E. herbicola; Escherichia, for example, E. coli; Klebsiella, for example, K. pneumoniae; Proteus, for example, P. vulgaris; Providence, for example, P. stuartii; Salmonella, for example, S. typhimurium; Serratia, for example, S. liquefaciens, S. marcescens; Shigella, for example, S. flexneri; Streptomyces, for example, S. violeceoruber; Yersinia, for example, Y. enterocolitica. Accordingly, the phospholipase can be fungic, for example, from the Pyrenemycete class, such as the genus Fusarium, such as a strain of F. culmorum, F. heterosporum, F. solani, or a strain of F oxysporum. The phospholipase can also come from a strain of filamentous fungus within the Aspergillus genus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or Aspergillus oryzae.

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

In another preferred embodiment, the phospholipse is obtained from a Fusarium strain, especially Fusarium oxysporum. The phospholipase may be one belonging to WO 98/027057 obtained from Fusarium oxysporum DSM 2672, or variants thereof.

In a preferred embodiment of the invention, the phospholipase is an A1 phospholipase (EC 3.1.1.32). In another preferred embodiment of the invention, the phospholipase is an A2 phospholipase (EC 3.1.1.4).

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

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Suitable amylases (alpha and / or beta) include those of bacterial or fungal origin. Genetically engineered or chemically modified mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, for example, a special strain of B. licheniformis, described in greater detail in GB 1,296,839, or Bacillus sp. disclosed in WO 95/026397 or WO 00/060060.

Examples of useful amylases are the variants described in Patents 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 (whose references are all incorporated by reference).

Commercially available amylases are Duramyl ™, Termamyl ™, Termamyl Ultra ™, Natalase ™, Stainzyme ™, Fungmyl ™ and BAN ™ (Novozymes A / S), Rapidase ™ and Purastar ™ (from Genencor International Inc.). Suitable cellulases include those of bacterial or fungal origin. Genetically engineered or chemically modified mutants are included. Suitable cellulases include cellulases from the Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium genera, for example, fungal cellulases produced from Humicola insolens ,, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum from the patents disclosed in the patents .UU. 4,435,307, USA 5,648,263, USA 5,691,178, USA 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307.

Especially suitable cellulases are alkaline or neutral cellulases that have the advantages of color care. Examples of such cellulases are the cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940. Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, USA. 5,457,046, USA 5,686,593, US 5,763,254, WO 95/24471, WO 97/12307 and PCT / DK98 / 00299.

Commercially available cellulases include Celluzime ™, Carezyme ™, Endolase ™, Renozyme ™ (Novozymes A / S), Clazinase ™ and Puradax Hatm (Genecol International Inc.), and KAC-500 (B) TM (Kao Corporation).

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

Examples of pectate liases include pectate liases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as from Bacillus subtilis (Nasser et al., FEBS Letts., Vol. 335, pags 319-326, (1993)) and Bacillus sp. YA-14 (Kim et al., Biosci. Biotech. Biochem., Vol. 58, pages 947-949, (1994)). The purification of pectate liases with maximum activity in the pH range of 8-10 produced by Bacillus pumilus (Dave and Vaughn, J. Bacteriol., Vol. 108, pages 166-174, (1971)), have also been described. B. polymyxa (Nagel and Vaugn, Arch. Biochem. Biophys., Vol. 93, pp. 344-362, (1961)), B. stearothermophilus (Karbassi and Vaugh, Can. J. Microbiol, vol. 26, pags. 377-384, (1980)), Bacillus sp. (Hasegawa and Nagel, J. Food Sci., Vol.31, pages 838-845, (1966)) and Bacillus sp. RK9 (Kelly and Fogarty, Can. J. Microbiol., Vol. 24, pp. 1164-1172, (1978). Any of the above, as well as pectate liases independent of the divalent and / or thermostable cation, can be used in the Implementation of the invention In preferred embodiments, the pectate lyase comprises the amino acid sequence of a pectate lyase disclosed by Heffron et al., in Mol. Plant-Microbe Interact., vol. 8, pp. 331-334, (1995) and by Henrissat et al., Plant Physiol., vol. 107, pp. 963-976, (1995). Specifically contemplated lyctae pectates are disclosed in WO 99/27083 and WO 99/27084 patents. of Bacillus licheniformis are disclosed in US Patent No. 6,284,524 (whose document is therefore incorporated herein by reference.) Specifically contemplated pectate liases variants are disclosed in WO 02/006442, specifically - especially the variants disclosed in the Examples in WO 02/006442 (whose document is therefore incorporated in the present invention by reference).

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

Examples of mannanases (EC 3.2.1.78) include mannanases of bacterial or fungal origin. In a specific embodiment, mannanase is obtained from a strain of the filamentous fungi of the Aspergillus genus, preferably Aspergillus niger or Aspergillus aculeatus (Patent WO 25576). WO 93/24622 discloses a mannanase isolate from Trichoderma reseei. Mannanases have also been isolated from various bacteria, including Bacillus organisms. For example, Talbot and others, Appl. Environ. Microbiol, vol. 56, No.11, pages. 3505-3510, (1990) describes a beta-mannanase derivative from Bacillus stearothermophilus. Mendoza et al., World J. Microbiol, Biotech., Vol. 10, No. 5, pages. 551-555, (1994) describes a beta.-mannanase obtained from Bacillus subtilis. JP-A-03047076 discloses a beta-mannanase obtained from Bacillus sp. JP-A-63056289 describes the production of a thermostable, alkaline beta-mannanase. JP-A-63036775 refers to the microorganism Bacillus FERM P-8856 that produces beta-mannanase and beta-mannosidase. JP-A-08051975 discloses alkaline beta-mannanases from Bacillus sp. AM-001 alkalophilic. In WO 97/11164 a purified mannanase from Bacillus amyloliquefaciens is disclosed. WO patent

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91/18974 describes a hemicellulase such as an active glucanase, xylanase or mannanase. The alkaline family of mannanases 5 and 26 obtained from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, bacillus clausii, Bacillus sp., And Humicola insolens disclosed in WO 99/64619 are contemplated. Especially contemplated are the Bacillus sp. concerned in the Examples in WO 99/64619, whose document is therefore incorporated herein by reference.

Examples of commercially available mannanasas include Mannaway ™ available from Novozymes A / S, Denmark.

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

Hydrotope

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

Solvents

The composition may comprise a solvent such as water or an organic solvent such as isopropyl alcohol or glycol ethers. Solvents may be present in liquid or gel-like compositions.

Metal chelating agents

The composition may contain a metal chelating agent such as carbonates, bicarbonates, and sesquicarbonates. The metal chelating agent can be a bleaching stabilizer (i.e. heavy metal sequestrant). Suitable bleaching stabilizers include ethylenediamine tetraacetate (EDTA), dielenedriamine pentaacetate (DTPA), ethylenediamine disuccinate (EDDS), and polyphosphonates such as Dequests (Trade Mark), ethylene diamine tetramethylene phosphonate (EDTMP) and pentamethylene diethylenetriamine phosphonate (DE-TPMP). In general, metal chelating agents will not be present in part (a) of the composition since microbial function can be impaired if metal ions become unavailable.

Adjuvants or complexing agents

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

Examples of calcium sequestering adjuvant materials include alkali metal polyphosphates, such as sodium tripolyphosphate and organic sequestrants, such as ethylene diamino tetraacetic acid.

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

Examples of calcium ion exchange adjuvant materials include the various types of water-insoluble amorphous or crystalline aluminosilicytes, of which zeolites are the best known representatives, for example, zeolite A, zeolite B (also known as zeolite P), zeolite C, zeolite X, zeolite Y and also zeolite type P, as described in Patent EP-A-0,384,070.

The composition may also contain 0-65% of an adjuvant or complexing agent such as ethylene diamino tetraacetic acid, alkyl- or alkenyl succinic acid, nitrilotriacetic acid or the other adjuvants mentioned below. Many adjuvants are bleaching stabilizing agents by virtue of their ability to complex metal ions.

When the adjuvant is present, the compositions may suitably contain less than 7% by weight, preferably less than 10% by weight, and most preferably less than 10% by weight of detergency aid.

The composition may contain as an adjuvant a crystalline aluminosilicate, preferably an alkali metal aluminosilicate, more preferably a sodium aluminosilicate. This is typically present in a proportion of less than 15% by weight. Aluminosilicates are materials that have the general formula

0.8-1.5 M2O.Al2Oa.0.8-6 SO

wherein M is a monovalent cation, preferably sodium. These materials contain some bound water and are required to have a calcium ion exchange capacity of at least 50 mg CaO / g. Preferred sodium aluminosilicates contain 1.5-3.5 units of SO in the above formula. They can be easily prepared by reaction between sodium silicate and sodium aluminate, as described extensively in the literature. The relationship of

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Aluminosilicate surfactants (if present) is preferably greater than 5: 2, more preferably greater than 3: 1.

Alternatively, or in addition to aluminosilicate adjuvants, phosphate adjuvants can be used. In this technique, the term "phosphate" encompasses diphosphate, triphosphate and phosphonate species. Other forms of adjuvants include silicates, such as soluble silicates, metasilicates, layered silicates (eg, Hoechst SKS-6).

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

Polymers

The composition may comprise one or more polymers. Examples are carboxymethyl cellulose, poly (vinyl pyrrolidone), poly (ethylene glycol), poly (vinyl alcohol), poly (vinyl pyridine-N-oxide), poly (vinylimidazole), polycarboxylates such as polyacrylates, maleic / acrylic acid copolymers and copolymers of lauryl methacrylate / acrylic acid.

Modern detergent compositions typically use polymers such as so-called "dye transfer inhibitors". These prevent the migration of dyes, especially during long soak times. Any suitable dye transfer inhibition agent may be used in accordance with the present invention. Generally, such dye transfer agents include polyvinyl pyrrolidone polymers, polyamine N-oxide polymers, N-vinyl pyrrolidone and N-vinylimidazole copolymers, manganese phthalocyanine, peroxidases, and mixtures thereof.

DTI, dye-binding polymers containing nitrogen are preferred. Of these, polymers and copolymers of cyllic amines, such as vinyl pyrrolidone and / or vinyl imidazole, are preferred.

Polyamine N-oxide polymers suitable for use in the present invention contain units having the following structural formula: R-Ax-P; wherein P is a polymerizable unit to which an N-O group can be attached or the N-O group can 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, aliphatic, ethoxylated, aromatic, heterocyclic or alicylic group or combination thereof, to which the nitrogen of the NO group may be attached, or the group is NOT part of these groups, or the group may NOT be attached to both units. Preferred polyamine N-oxides are those in which R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine and derivatives thereof. The group can NOT be represented by the following general structures: N (O) (r1) or -3, or = N (O) (R1) oi, in which each R1 independently represents an aliphatic, aromatic, heterocyclic or alid- click or combination thereof; and the nitrogen of the N-O group may be attached or be part of any of the aforementioned groups. The amine oxide unit of the polyamine N-oxides has a pKa <10, preferably pKa <7, more preferably pKa <6.

Any main polymer chain can be used, as long as the amine oxide polymer formed is water soluble and has dye transfer inhibitory properties. Examples of suitable polymeric main chains are polyvinyl, polyalkylene, polyester, polyether, polyamide, polyimide, polyacrylate and mixtures thereof. These polymers include random or block copolymers in which one type of monomer is an amine N-oxide and the other type of monomer is an N-oxide. The amine N-oxide polymers typically have an amine to amine N-oxide ratio of 10: 1 to 1: 1,000,000. However, the number of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymerization or by an appropriate degree of N-oxidation. 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 in the present invention as "PVNO". A preferred polyamine N-oxide is poly (4- vinyl pyridine-N-oxide), which has an average molecular weight of about 50,000 and an amine to N-oxide ratio of about 1: 4.

Copolymers of N-vinyl pyrrolidone and polymers of N-vinylimidazole (as a class, referred to as "PVPVI") are equally preferred. Preferably, the PVPVI has an average molecular weight range 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, determined by light diffusion, as described by Barth et al., in Chemical Analysis, vol. 113, "Modern Methods of Polymer Characterization." Preferred PVPVI copolymers typically have a molar ratio of N-vinylimidazole to N-vinyl pyrrolidone 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. Suitable PVPVI polymers include Sokalan ™ HP56, commercially available from BASF, Ludwigshafen, Germany.

Equally preferred as dye transfer inhibiting agents are polyvinylpyrrolidone polymers ("PVP") having an average molecular weight of from about 5,000 to 400,000, preferably from about 5,000 to about 700,000, and most preferably from about 5,000 to Approximately 50,000 PVPs are disclosed, for example, in Patents EP-A-262,897 and EP-A-256,696. Suitable PVP polymers include Sokalan ™ HP50, commercially available from

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BASF Compositions containing PVP may also contain polyethylene glycol ("PEG") with 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 on a ppm basis supplied 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 dye transfer inhibiting agents, are those from the class of modified polyethyleneimine polymers, as disclosed, for example, in WO-A-0005334. These modified polyethyleneimine polymers are modified, water soluble or dispersible polyamines. Modified polyamines are further disclosed 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.

Preferably, the composition according to the present invention comprises a dye transfer inhibitor selected from polyvinylpyridine N-oxide (PVNO), polyvinyl pyrrolidone (PVP), polyvinyl imidazole, N-vinyl pyrrolidone and N-vinylimidazole copolymers (PVPVI), copolymers thereof and mixtures thereof.

The amount of dye transfer inhibitor in the composition according to the present 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 such as, for example, fabric conditioners including clays, foam boosters, foam suppressants (anti-foams), anti-corrosion agents, dirt suspension agents, anti-redeposition agents of dirt, other dyes, anti-microbials, optical brighteners, patina inhibitors, or perfumes.

Next, several non-limiting embodiments of the invention will be described more particularly, with reference to the following figure, in which:

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

With reference to the drawing, a packaged lavender product 1 is shown. Product 1 comprises in a fluid lavender composition 3 contained in a package 5, the high viscosity lavender composition according to Example A or B detailed below.

The package comprises a compressible container, in this example a plastic bottle 7 that stores the high viscosity, fluid, lavender gel 3 and a dispensing device 9 incorporating a tissue pre-treatment device 11. The dispensing device 9 is located in the base 13 of the container 7 and is enclosed by a dosage closure device 13. The closure 13 comprises the support base 13 of the container 5.

The bottle 7 and the dispensing device 9 (which incorporates the pre-treater 11) are connected to each other by the threaded connection. The closure 13 is also attached to the bottle by means of a threaded connection. (Threaded connections are not shown). In a separate embodiment, the closure 13 is connected to the bottle 7 using a pressure connection, which does not require turning the bottle / closure to open the closure.

The bottle 7 is manufactured from a flexible plastic material comprising polyethylene terephthalate.

The upper part 21 of the bottle is shown flat but, in other embodiments, it can be curved, as shown in the dotted line 22, in order to avoid head-down storage.

The closure 13 includes a generally flat, smooth, elongated lower surface (with respect to at least the area of the neck of the bottle), 15. By having a surface in the elongated flat upper part 15, the surface allows the closure 13 function as a support base 13 with the bottle 7 in an inverted position, thus allowing the high viscosity gel 13 to accumulate (by gravity) during storage in the dispensing device 9.

In addition, the closure 13 includes a reservoir portion 17 in which the pre-treatment 11 is enclosed 26. The closure is held externally towards the surface 15 to provide a stable base. The area of the surface 15 is larger than that of the upper part 21 of the device.

The dispensing device 9 comprises a hole through which dispensing can occur. The orifice includes a valve 21 in fluid communication through the conduit 23. The valve 21 comprises a membrane that extends through an orifice 25 in the dispensing part 9.

In one embodiment, the membrane has an arcuate part (not shown) directed towards the container 7. The arcuate part of the membrane has intersection slits to define a plurality of sheets generally

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triangular tea When the contents of the container are pressed for dispensing, the triangular sheets are folded toward the open end of the hole 25, allowing the product to pass through the hole 25. When the dispenser is stopped pressing, the triangular sheets recede into position. original and operate by blocking the passage of the product through the hole 25. The leaves of the valve are resilient enough not to obtain the opening, unless the pressure applied exceeds the hydraulic static load pressure generated by one filled with product. During use, the fluid is pressed to flow and is partially collected on part 11 of the pre-treater ready for cleaning.

Any remaining fluid that remains on the pretreatment part 11, can drip from the pretreatment 11 during storage and be collected within the reservoir part 17 for use in the next wash. This reduces product losses.

Example of laundry formulation A

The following gel laundry detergent compositions were prepared, of which composition A is in accordance with the invention

 Component:

 % in weigh

 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

 Enzyme lipase

 0.5

 Fragrance

 0.2

 Water

 rest up to 100

in which:

Borax: sodium tetraborate (10 ac.)

Nonionic surfactant: ethoxylated alcohol with an average of 9 ethylene oxide groups.

The gel detergent composition exemplified by composition A was found to fluidize shear and stable. In addition, typical detergent particles of density between 0.8 and 0.9 g / cm3 and with a diameter of up to 5000 micrometres could be stably suspended in this composition for more than 2 weeks without any clear observable movement of the particles.

 Sample

 Viscosity / Pa.s Eta 0 Scientific Tension Tan Delta

 20 s-1 100 -1 Pa.s Pa at 1 Hz

 TO

 2.11 0.61 3.00E + 5 15 0.04

To obtain the values shown in the table above, all rheological measurements were carried out at 25 ° C using a Carrimed CSL100 reometer, with a cone geometry and plate roughly rough to avoid slippage.

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The viscosity was measured at variable shear rates, from very low shear to a shear rate greater than 100 s-1. Two situations are shown: the viscosity measured at relatively low shear (20 s-1) and the measure at much higher shear (100 s-1). It can be seen that the viscosity of composition A at high shear is much lower than that obtained at low shear, while composition B shows almost equal viscosities for high and low shear. In other words, composition A clearly fluidizes shearing, while composition B is not.

In addition, the critical tension is shown. This parameter represents the tension at which the material leaves the Newtonian plateau and is diluted under an increase in shear. Likewise, the “Eta 0” values are shown, which refer to the calculated viscosity at zero shear from the sliding flow measurements. Finally, the “Tan delta” values are shown, which refer to the ratio of loss during storage of the modules (G '' / G ') and reflect the viscosity domain over elastic properties, so that Materials that show very low “Tan delta” values (tending to zero, such as composition A in the table above), will be much more elastic than those that give higher “Tan delta” values (tending to 90).

Example of laundry formulation B

The following gel laundry detergent compositions were prepared, of which composition C is in accordance with the invention and composition D is a comparative composition according to the prior art:

 Component:

 % in weigh

 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 sulfate EO

 10.5

 Nonionic Surfactant

 6.6

 1-decanol

 6.0

 Protease Enzyme

 0.45

 Enzyme lipase

 0.25

 Fragrance

 0.2

 Water

 rest up to 100

in which:

Borax: sodium tetraborate (10 ac.)

Non-ionic surfactant: ethoxylated alcohol with an average of 9 ethylene oxide groups

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

Composition B is a liquid that fluidizes shear, pourable, transparent, stable, capable of stably suspending typical detergent particles with a density of between 0.8 and 0.9 g / cm3 and with a diameter of up to 5000 micrometres, for more than 2 weeks without any clear observable movement of the particles.

Next, the rheological parameters for the two compositions are shown.

 Sample

 Viscosity / Pa.s Eta 0 Scientific Tension Tan Delta

 20 s-1 100 -1 Pa.s Pa at 1 Hz

 B

 1.33 0.48 9.85E + 05 10 0.07

For clarification of the rheological values shown in this table, reference is made to the description concerning the similar table shown above in Example A.

Of course, it is understood that the invention is not intended to be restricted to the details of the previous embodiment, which are described by way of example only.

Claims (6)

5 10 fifteen twenty 25 1. A packaged lavender product comprising a fluid lavender composition contained in a package, in which (i) the fluid lavender composition has a viscosity of at least at least 100 Pa.s, preferably at least 500 Pa.s, when at rest or up to a shear stress of 10 Pa and comprises at least one surfactant and at least one enzyme; Y (ii) the package comprises a compressible container in which the fluid lavender composition is stored and a dispensing device that incorporates a device for the pre-treatment of the tissue and is located at the base of the compressible container and is enclosed by a Dosing closure device that provides a support base of the container, characterized in that the dispensing device comprises a channel or conduit that provides fluid communication between the reservoir and the pre-treater and because the pre-treater comprises a device that allows mechanical cleaning, which comprises a semi-spherical body with multiple projections that extend radially from it. 2. A packaged lavender product according to claim 1, wherein the projections are flexible such that they move during cleaning providing a light cleaning action. 3. A packaged lavender product according to claim 1 or 2, wherein some or all of the projections are semi-nigged or nested so as to provide a more rigorous mechanical cleaning action. 4. A packaged lavender product according to any preceding claim, wherein the package has a curved top. 5. A packaged lavender product according to any preceding claim, wherein the composition is a gel-like composition that fluidizes at shear, having a viscosity under shear stress less than 300 Pa.s, 6. A packaged lavender product according to claim 5, wherein the composition is fluidized at shear with viscosity under tension less than 100 Pa.s, preferably less than 5 Pa.s,