BRMU8903145Y1 - packed wash product - Google Patents

Description

Utility Model Patent Descriptive Report Packaged Wash Product Utility Model Field The present model relates to a viscous wash product and its packaging.

Utility Model Summary One object is to provide an improved pretreatment device for the precise pretreatment of washing stains.

Thus, in a first aspect, the present embodiment provides a packaged wash product comprising a fluid wash composition contained in a dispensing bottom package, wherein (i) the fluid wash composition has a minimum viscosity of at least 100 Pa. preferably at least 500 Pa.s when at rest or up to a shear stress of 10 Pa and formed by at least one surfactant and at least one hydrotrope and (ii) the dispensing bottom package comprising a container in which the fluid wash composition is stored and a dispensing device including a tissue pretreatment device, the dispensing device and a tissue pretreatment device being located at the bottom of the compressible container. The advantage of the above arrangement is that it offers greater control in applying a high viscosity face-to-face composition to dirty areas. Pretreatment with high viscosity fluids from handheld products is advantageous in terms of application accuracy to the dirty area. However, this can be difficult ergonomically and many users resort to applying an impact force to the device (tapping the base or tapping the side) where it interferes with exact dosing and often results in over dosing, spillage, etc.

This arrangement, as a consequence of the dispensing / pretreatment portion being positioned at the bottom of the reservoir, means that the user does not need to invert the package to dose / pretreat or wait until the viscous fluid flows from bottom to top ( where dispensing / pretreatment devices are usually located). With the present model, gravity keeps the pretreatment device loaded with the composition. While the propensity of high viscosity products to remain in place during pretreatment is advantageous, they can often remain throughout the wash process and leave their own mark on the fabric after the wash process has begun. This is especially prevalent in short washes or "environmentally friendly" low water washes. The presence of a hydrotope facilitates the solubilization of the composition applied to the stain and, consequently, the faster release in the wash.

Preferably, the tissue treatment container is closed by a metering cap device, providing a packaging support base. The advantage of this arrangement is that the dispensing device does not need to involve complicated and expensive seals / valves such as the metering closure cap, it includes the pretreatment device and provides the basis: it offers the advantage that any droplet composition. Fall from the pretreatment device after use, are collected on the support base which can be placed directly on the washing machine / container minimizing waste. The dispensing device may include a channel or duct providing fluid communication between the reservoir and the pretreater. The pretreater may include a device that allows mechanical cleaning, such as a multi-projection body. Projections can be flexible so that they move during cleaning, providing a light cleaning action. Alternatively, some or all projections may be semi-rigid or rigid to provide a harder mechanical cleaning action. The projections may be, for example, of thin bristles to provide a brush-like or thicker device to provide nozzles as projections. The packaging may have a curved top to make it impossible for users to store the bottle upside down. Thus, the package is more likely to be stored in the pretreater, ie loading position, with the gravity-accumulated fluid wash composition at the base of the package.

In one embodiment, the pretreater comprises a generally hemispherical body with multiple projections extending radially. The composition may include from 0.1% to 10% by weight of hydrotope, preferably 0.1% to 5%, preferably 0.1% to 2% and preferably 0.1% to 1% hydrotope.

Possible hydrotopes include toluene, urea, cumene sulfonate, xylene sulfonate and mixtures thereof. Salts include sodium, potassium, ammonium, monoethanolamine, triethanolamine and mixtures thereof. One combination is xylene sulfonate and urea. The composition is preferably a low shear gel type composition. The viscosity under shear stress may be less than 300 Pa.s, preferably less than 100 Pa.s and preferably less than 5 Pa.s, preferably 1 Pa.s and preferably 0.5 Pa.s.

Low shear compositions may comprise a polymer gum, for example, xanthan gum or another gum capable of forming stable continuous gum networks, which may suspend particles.

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

Another useful method is to alter an ungelled formulation to form an internal structure where the structure provides desired properties for the gel-like detergent thus formed. The composition may include a soap or fatty acid in combination with sodium sulfate and one or more surfactants may be used to form a gelled structure by the formation of lamellar phases. The composition may comprise a dispersion of a lamellar phase surfactant micellar systems and, additionally, a structuring agent for the establishment of the lamellar phase, wherein said structuring may be a fatty alcohol. The model composition contains one or more surfactants and / or other ingredients optionally that the composition is fully functional as a wash cleaning composition and / or a care composition. The composition of the model may be provided in solid or liquid state. If in solid form, the composition may be rehydrated and / or dissolved in a solvent, including water, before use. The composition may be presented in concentrated form to be diluted or may be ready to use (in use).

Brief Description of the Figures Figure 1 shows the packaging of the viscous wash product.

Detailed Description of the Utility Model The present model is suitable for use in household or industrial fabric wash compositions. The present model may also be applied to industrial or household non-detergents based on fabric care compositions.

Other contemplated ingredients including hydrotopes, preservatives, fillers, builders, complexing agents, polymers, stabilizers, perfumes themselves, other conventional detergent ingredients or combinations of one or more thereof are discussed below. Surfactants Fabric wash compositions according to the present invention comprise a fabric wash detergent material selected from soap-free anionic surfactants, nonionic surfactant, soap, amphoteric surfactants, zwitterionic surfactants and mixtures thereof.

Detergent compositions suitable for domestic or industrial automatic fabric washing machines generally contain non-soap anionic surfactant or nonionic surfactant or a combination of both in the appropriate proportion, as will be known to the person skilled in the art, optionally in conjunction with soap.

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

Suitable anionic surfactants include alkyl benzene sulfonate, primary and secondary alkyl sulfates, especially C 8 -C 15 primary alkyl sulfates; alkyl ether sulfates, olefin sulfonates; xylene alkyl sulfonates; dialkyl sulfosuccinates; ether carboxylates; isethionates; sarcosinates; fatty acid esters sulfonates and mixtures thereof. Sodium salts are generally preferred. When included, the composition usually contains about 1% to 50%, preferably 10% to 40% by weight based on the fabric treatment composition of an anionic surfactant such as linear alkyl benzene sulfonate, alpha olefin sulfonate, alkyl sulphate (fatty alcohol sulphate), ethoxy sulphate alcohol, secondary alkane sulphonate, alpha sulfo fatty acid methyl esters, alkyl or alkenyl succinic acid or soap. Preferred surfactants are alkyl ether sulfates and mixtures of nonionic alkoxylated alkyl surfactants with an alkyl sulfonates or alkyl ether sulfates.

Preferred alkyl ether sulfates are C8 -C15 alkyl and have from 2 to 10 moles of ethoxylation. Preferred alkyl sulfates are alkylbenzene sulfonates, particularly linear alkylbenzene sulfonates with a C8 -C15 alkyl chain length. The counterion of anionic surfactants is typically sodium, although other counterions such as tetraethylammonium (TEA) or ammonium may be used. Suitable anionic surfactants are commercially available as Clariant 'Genapol' ™ series.

Nonionic surfactants include primary and secondary alcohol ethoxylates, especially C8-C7 aliphatic alcohol ethoxylates with an average of 1 to 7 moles of ethylene oxide per mole of alcohol and especially C10-C15 primary and secondary aliphatic alcohol ethoxylates with an average of 1 to 10 moles of ethylene oxide per mole of alcohol. Non-ethoxylated nonionic surfactants include alkyl polyglycosides, glycerol monoethers and polyhydroxy starches (glucamide). Mixtures of nonionic surfactants may be used. When included the composition usually contains about 0.2% to 40%, preferably 1% to 7% by weight, preferably 5% to 15% by weight of a nonionic surfactant such as ethoxylated alcohol, ethoxylate. nonylphenol, alkyl polyglycoside, alkyl dimethyl amine oxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy fatty acid alkyl amide or glucosamine-N-acyl N-alkyl ("glucamides").

Nonionic surfactants that may be used include primary and secondary alcohol ethoxylates, in particular C8-C7 aliphatic alcohol ethoxylates with an average of 1 to 35 moles of ethylene oxide per mole of alcohol and especially of C10-C15 ethoxylates of primary and secondary aliphatic alcohols with an average of 1 to 10 moles of ethylene oxide per mole of alcohol. Enzymes One or more enzymes may be suitable. It is to be understood that variants of the enzyme (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 EP 251446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525610 (Solvay) and WO 94/02618 (Gist-Brocades NV).

The types of enzymes that should be incorporated into the model granules include oxidoreductasas, hydrolases, transferases, liases, isomerases and ligases, ie, respectively (EC 1 (EC 2.-.-.), (EC 3.-. -.-), (EC 4.-.-.-), (EC 5.-.-.-), (EC 6.-.-.-), of which the classification of this enzyme 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 enzymes include proteases, alpha-amylases, cellulases, lipases, peroxidases / oxidases, pectate liases and mannanases or mixtures thereof. Most preferred enzymes are proteases.

Suitable proteases include those of animal, plant or microbial origin. Microbial origin is preferred. Chemically modified or protein mutation engineering are included. The protease may be a serine protease or metal protease, preferably a microbial alkaline protease or a trypsin-like protease (trypsin). Examples of alkaline proteases are subtilisin, especially those derived from Bacillus, for example subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (described in WO 89/06279). Examples of trypsin-like proteases are trypsins (e.g. of bovine or porcine origin) and the Fusarium protease described in WO 89/06270 and WO 94/25583.

Examples of useful proteases are the variants described in WO 92/19729, WO 98/201 15, WO 98/20116 and WO 98/34946, especially variants with substitutions at 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 ™, 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 mutation engineering are included. Examples of useful lipases include Humicola (Termomices synonym), for example, H. lanuginosa (T. lanuginosus) lipases as described in EP 258 068 and EP 305 216 or H. insolens as described in WO 96/13580 , Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri (GB 1,372,034), P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012), Bacillus lipase, for example, from B. subtilisina (Dartois et al. (1993), Biochemica et Biophysica Acta, 1131, 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).

Other examples of lipase variants such as those described in WO 92/05249, WO 94/01541, EP 407 225, EP 260 105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578 , WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202.

Preferred commercially available lipase enzymes include Lipolase ™ and Lipolase Ultra ™, Lipex ™ (Novozymes A / S). The model method may be performed in the presence of cutinase, classified in EC 3.1.1.74. The cutinase used according to the invention may be of any origin. Preferred cutinases are of microbial origin, especially bacterial, fungal or yeast origin.

Cutinases are enzymes capable of degrading the cutin. In a preferred embodiment, the cutinase is derived from an Aspergillus strain, in particular Aspergillus oryzae, an Alternaria strain, in particular, Alternata brassiciola, a Fusarium strain, in particular, 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, Rhizoctonia, solani, a strain of Streptomyces, in particular Streptomyces scabies or a strain of Ulocladium, in particular, Ulocladium consortiale. In a preferred embodiment, the cutinase is derived from a strain of Humicola insolens, in particular the strain of Humicola insolens DSM 1800. Cutinase Humicola insolens is described in WO 96/13580, which is incorporated herein by reference. Cutinase may be a variant, as one of the variants disclosed in WO 00/34450 and WO 01/92502, which are incorporated by reference. Preferred cutinase variants include variants listed in Example 2 of WO 01/92502, which is specifically incorporated by reference.

Commercially preferred cutinases include NOVOZYM ™ 51032 (available from Novozymes A / S, Denmark). The model method may be performed in the presence of phospholipase classified as EC 3.1.1.4 and / or EC 3.1.1.32. As used herein, the term phospholipase is an enzyme that has activity towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, composed of glycerol esterified with two fatty acids in the outer position (sn-1) and in the middle (sn-2) and esterified with phosphoric acid in the third position; Phosphoric acid, in turn, can be esterified to an amino alcohol. Phospholipases are enzymes that participate in the hydrolysis of phospholipids. Several types of phospholipase activities can be distinguished, including phospholipases Ai and A2, which hydrolyze a fatty acyl group (at position sn-1 and sn-2, respectively) to form lysophospholipid and lysophospholipase (or phospholipase B), which can hydrolyze the remainder. fatty acyl group in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterase) release glycerol diacyl or phosphatidic acid, respectively. The term phospholipase includes enzymes with phospholipase activity, for example phospholipase A (A1 and A2), phospholipase B activity, phospholipase C activity or phospholipase D activity. The term "phospholipase A" used herein in connection with an enzyme of the phospholipase A The model is understood to be a phospholipase A1 enzyme and / or phospholipase A2 activity. Phospholipase activity may be provided by enzymes having other activities, as well as, for example, lipase with phospholipase activity. Phospholipase activity may be, for example, lipase with secondary phospholipase activity. In other embodiments of the model, phospholipase enzyme activity is provided by an enzyme with only phospholipase activity and where phospholipase enzyme activity is not a secondary activity. Phospholipase may be of any origin, for example animal origin (such as mammals), for example from the pancreas (e.g. cattle or pig pancreas) or snake venom or bee venom. Preferably, the phospholipase may be of microbial origin, for example from filamentous fungi, yeast or bacteria, such as the genus or species Aspergillus, for example A. niger, Dictyostelium, for example, D. discoideum, Mucor, for example. e.g. javanicus, M. mucedo, M. subtilissimus; Neurospora, for example, N. crassa; Rhizomucor, e.g. R. pusillus, Rhizopus, e.g. R. arrhizus, R. japonicus, R. stolonifer; Sclerotiorum, for example, S. libertiana; Trichophyton, for example, T. rubrum; Whetzelinia, for example, W. Sclerotinia; Bacillus, for example, B. megaterium, B. subtilis, Citrobacter, for example, C. freundii, Enterobacter, for example, E. aerogenes, E. cloacae Edwardsiella, E. tarda, Erwinia, for example, herbicola E .; coli, e.g. E. coli, Klebsiella, e.g. K. pneumoniae, Proteus, e.g. P. vulgaris, Providencia, e.g., P. stuartii; Salmonella, for example, S. typhimurium, Serratia, for example, liquefasciens S., S. marcescens, Shigella, for example, S. flexneri, Streptomyces, for example, violeceoruber S .; Yersinia, for example, Y. enterocolitica. Thus, the phospholipase may be fungi, for example, from the Pyrenomycetes class, such as the genus Fusarium, such as a strain of F. culmorum, heterosporum F., F. solani, or a strain of Fusarium oxysporum. Phospholipase may also be from a strain of filamentous fungi in the genus Aspergillus, such as a strain of Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger and Aspergillus oryzae.

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

In another preferred embodiment, the phospholipase is derived from a Fusarium strain, especially Fusarium oxysporum. Phospholipase may be disclosed in WO 98/026057 derived from Fusarium oxysporum DSM 2672, or variants thereof. In a preferred embodiment of the model, phospholipase is a phospholipase Ai (EC. 3.1.1.32). In another preferred embodiment of the model, phospholipase is a phospholipase A2 (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 mutation engineering are included. Amylases include, for example, alpha-amylases obtained from Bacillus, for example a special B. licheniformis ear, described in more detail in GB 1,296,839 or strains of Bacillus sp. disclosed in WO 95/026397 or WO 00/060060.

Examples of useful amylases are the variables described in 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 (where all references are incorporated by reference).

Commercially available amylases are Duramyl ™, Termamyl ™, Termamyl Ultra ™, Natalase ™, Stainzyme ™, Fungamyl ™ and BAN ™ (Novozymes A / S), Rapidase ™ and Purastar ™ (from Genencor International Inc.).

Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein mutation engineering are included. Suitable cellulases include cellulases of the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, for example, fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4,435,307, US 5,664,307. 263, US 5,691,178, US 5,776,757, WO 89/09259, WO 96/029397 and WO 98/012307.

Especially suitable cellulases are alkaline or neutral cellulases with color care benefits. Examples of such cellulases are cellulases as described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940. Other examples are cellulase variants as described in 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. 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 mutation engineering are included. Examples of useful peroxidases include Coprinus peroxidases, for example C. cinereus and variants thereof as 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 which have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as Bacillus subtilis (Nasser et al. (1993) FEBS Letts. 335: 319-326) and Bacillus sp. YA-14 (Kim et al. (1994) Biosci. Biotech. Biochem. 58: 947-949). Purification of pectate liases with maximum activity in the pH range 8 to 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 (1980) 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) have also been described. Some of the above, as well as divalent-independent and / or thermostable pectate liases, may be used in the practice of the model. In preferred embodiments, pectate lyase comprises the amino acid sequence of pectate lyase disclosed in Heffron et al. (1995) Mol. Plant-Microbe Interact. 8: 331-334 and Henrissat et al., Plant Physiol (1995). 107: 963-976. Specifically contemplated, pectatel liases are disclosed in WO 99/27083 and WO 99/27084. Others specifically contemplate Bacillus licheniformis-derived pectate liases being disclosed in US 6,284,524 (which is incorporated by reference). Specifically contemplated, variants of the pectate lyase are disclosed in WO 02/006442, especially the variants disclosed in Examples of WO 02/006442 (which is 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 mannanases of bacterial and fungal origin. In a specific embodiment, mannanase is derived from a strain of filamentous fungi of the genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus (WO 94/25576). WO 93/24622 describes a mannanase isolated from Trichoderma reseei. Mannanases have been isolated from various bacteria, including Bacillus organisms. For example, Talbotet al. Appl. Environ. Microbiol., Vol.56, No. 11, pp. 3505-3510 (1990) describes a beta-mannanase derived from Bacillus stearothermophilus. 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 describes a beta-mannanase derived from Bacillus sp. JP-A-63056289 describes the production of a thermostable alkaline beta-mannanase. JP-A-63036775 describes a microorganism Bacillus FERM P-8856, which produces beta-mannanase and beta-mannosidase. JP-A-08051975 describes alkaline beta-mannanases of Bacillus sp. AM-001. Mannanase purified from Bacillus amyloliquefaciens is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase as an active glucanase, xylanase or mannanase. Alkaline families contemplated are 5 and 26 mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp. and Humicola insolens disclosed in WO 99/64619. Especially contemplated are Bacillus sp. mannanases disclosed in Examples of WO 99/64619 where the document is incorporated herein by reference.

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

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

Hydrotropes: The term "hydrotrope" generally means a compound with the ability to increase solubility, preferably aqueous solubility of certain poorly soluble organic compounds. Examples of hydrotropes include xylene sodium 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 compositions.

Metal Chelating Agents: The composition may contain a metal chelating agent, such as carbonates, bicarbonates and sesquicarbonates. The metal chelating agent may be a bleach stabilizer (i.e. heavy metal scavenger). Suitable bleach stabilizers include ethylenediamine tetraacetate (EDTA), diethylenetriamine pentaacetate (DTPA), ethylene diamine disuccinic acid (EDDS) and polyphosphonates such as Dequests (trademark), ethylenediamine tetramethylene phosphonate (EDTMP) and DEPhenylamine phosphate diethylenediamine. In general, metal chelating agents were not present in part (a) of the composition so microbial function may be impaired if metal ions become unavailable.

Builders or Complexing Agents: Builders may be selected from 1) calcium sequestering materials, 2) precipitation materials, 3) ion exchange calcium materials and 4) mixtures thereof.

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

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

Examples of ion exchange calcium builder materials include the various types of crystalline or amorphous water-insoluble aluminosilicates, of which zeolites are the best known representatives, for example zeolite A, zeolite B (also known as zeolite P) , zeolite X, zeolite Y and also type P zeolite as described in EP-A-0.384.070. The composition may also contain from 0% to 65% of a builder or complexing agent such as ethylene diamino tetracetic acid, diethylene pentaacetic acid, alkyl or alkenyl succinic acid, nitrilotriacetic acid or other builders mentioned below. Many builders are stabilizing bleaching agents because of their ability to complex metal ions.

Where the builder is present, the compositions may suitably contain less than 7 wt%, preferably less than 10 wt%, preferably less than 10 wt% detergency builder. The composition may contain a crystalline aluminosilicate builder, preferably an alkaline aluminosilicate metal, preferably a sodium aluminosilicate. This is typically present at a level below 15% by weight.

Aluminosilicates are materials that have the general formula: 0.8-1.5 M20. Al203. 0.8-6 Si02 where M is a monovalent cation, preferably sodium. These materials contain some bound water and are required to have a calcium ion exchange capacity of at least 50 mg CaO / g. Preferred sodium aluminosilicates contain from 1.5 to 3.5 units of S1O2 of the above formula. They can be easily prepared by the reaction between sodium silicate and sodium aluminate, as widely described in the literature. The ratio of surfactants to alumuminosilicates (if present) is preferably greater than 5: 2, preferably greater than 3: 1.

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

For low cost carbonate formulations (including bicarbonate and sesquicarbonate) and / or citrate may be employed as builders. Polymers: The composition may include one or more polymers. Examples are carboxymethylcellulose, poly (vinylpyrrolidone), poly (ethylene glycol), polyvinyl alcohol, poly (vinylpyridine-N-oxide), poly (vinylimidazole), polycarboxylates such as polyacrylates, acrylic acid / lauryl methacrylate copolymers and polyacrylates .

Modern detergent compositions typically employ polymers called "dye transfer inhibitors". These prevent dye migration, especially during long immersion periods. All suitable dye transfer inhibiting agents may be used in accordance with the present model. Generally, such dye transfer inhibiting agents include polyvinyl pyrrolidone polymers, N-oxide polyamine polymers, N-vinylpyrrolidone and N-vinylimidazole copolymers, manganese phthalokinine, peroxidases and mixtures thereof.

Containing nitrogen, binding dye, DTI polymers are preferred. Of these polymers and copolymers of cyclic amines such as vinyl pyrrolidone and / or vinyl imidazole are preferred. Suitable N-oxide polyamine polymers for use herein contain units of the following structural formula: R-Ax-P; where P is a polymerizable unit wherein an N-0 group may be attached or the N-0 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 O or 1, and R is an aliphatic, aliphatic, aromatic, heterocyclic or alicyclic ethoxylate or combination wherein the nitrogen of the N-0 group can be attached or the N-0 group is part of these groups or the N- group. 0 can be connected to both units. Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyridine, pyrrol, imidazole, pyrrolidine, piperidine and derivatives thereof. The group N-0 may be represented by the general structures: N (O) (R ') o-3 or = N (0) (R') oi, where each R 'independently represents an aliphatic, aromatic, heterocyclic group or alicylic or a combination thereof; and the nitrogen of the N-0 group may be attached or be part of any of the above groups. The polyamine N-oxide amine oxide moiety has a pKa <10, preferably pKa <7, preferably pKa <6.

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

N-vinylpyrrolidone copolymers and N-vinylimidazole polymers (as a class, called "PVPVI") are also preferred. Preferably, PVPVI has an average molecular weight range of 5,000 to 1,000,000, preferably 5,000 to 70,000 and preferably 10,000 to 7,000 as determined by light scattering as described in Barth, et al. Chemical Analysis, Vol. 113. "Modern Methods of Characterization of Polymers". Typically preferred PVPVI copolymers have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1: 1 to 0.2: 1, preferably from 0.8: 1 to 0.3: 1, preferably from 0 to , 6: 1 to 0.4: 1. Such copolymers may be linear or branched. Suitable PVPVI polymers include Sokalan (TM) HP56, commercially available from BASF, in Ludwigshafen, Germany.

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

Suitable dye transfer inhibiting agents are of the modified polyethyleneimine polymer class, as disclosed, for example, in WO-A-0005334. Such modified polyethyleneimine polymers are water soluble or dispersible, modified polyamines. Modified polyamines are disclosed in US-A-4,548,744, US-A-4,597,898, US-A-4597898, US-A-4,877,896, 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-2,829,022 and JP-A-06,313,271.

Preferably, the composition according to the present invention comprises a dye transfer inhibiting agent selected from polyvinylpyrridine N-oxide (PVNO), polyvinyl pyrrolidone (PVP), polyvinyl imidazole, N-vinylpyrrolidone and N-vinylimidazole copolymers. (PVPVI), copolymers thereof and mixtures thereof. The amount of dye transfer inhibiting agent in the composition according to the present model will be from 0.01% to 10%, preferably 0.02% to 5%, preferably 0.03% to 2% by weight. weight of the composition.

Other Detergent Ingredients: The composition may also contain other conventional detergent ingredients, such as fabric softeners, including clays, foam boosters, anti-foam, anti-corrosion agents, soil suspending agents, soil anti-redeposition, dyes, antimicrobials, optical brighteners, inhibitors of stains or perfumes. Various non-limiting embodiments of the model will now be more specifically described with reference to the figure.

Referring to the drawing, a packaged wash product 1 is shown. Product 1 comprises a fluid wash composition 3 contained in a package 5 with the high viscosity wash composition 3 according to Example A or B, detailed below. The package comprises a compressible container, in this example a plastic bottle 7 stores the fluid, the high viscosity lavage gel 3 and a dispensing device 9 incorporating a tissue pretreatment device 11. The dispensing device 9 is located in the container base 13 of 7 and is closed by a metering cap device 13. Lid 13 comprises the support base 13 of package 5. Vial 7 and dispensing device 9 (incorporating pretreator 11) are connected to each other. another by threaded connection. The cap 13 is also placed on the bottle by a screw connection. (Threaded connections not shown). In a separate embodiment the cap 13 is connected to the vial 7 using a snap-on connection where there is no need to rotate the vial / cap to open while closed. The flask 7 is made of a flexible plastic material comprising polyethylene terephthalate.

The tops 21 of the bottle are shown horizontally, but in other embodiments, may be curved as shown in the dotted line 22 to encourage storage with the lid down. Lid 13 includes an enlarged flat surface (with respect to at least the neck region of the bottle), generally planar bottom surface 15. By providing an enlarged flat surface top 15, the surface allows lid 13 to function as a support base 13 of vial 7, in an inverted position, thus allowing the high viscosity gel of 3 to accumulate (by gravity) during storage in the dispensing device.

In addition, the lid 13 includes a reservoir portion 17 wherein the pretreater 11 is closed 26. The lid is taped externally toward the surface 15 to provide a stable base. The surface area 15 is larger than the top 21 of the device. Dispensing device 9 comprises a dispensing hole through which dispensing occurs. The orifice includes a valve 21 in fluid communication through the duct 23. The valve 21 comprises a membrane extending through an orifice 25 in the dispensing part 9.

In one embodiment, the membrane has an arcuate portion (not shown) facing container 7. The arcuate portion of the membrane is provided with a cross-cut to define a plurality of generally triangular blades. When the contents of the container are pressurized for dispensing, the triangular blades bend toward the open end of port 25 allowing the product to pass through port 25. When dispensing pressure is released, energy is triangulated back to its original position and acts to block product passage through orifice 25. Valve sheets are sufficiently sturdy, do not open unless applied pressure exceeds static pressure of generated hydraulic load when full of product. In use, the fluid is pressurized to flow and partially collect by the pretreatment part 11 ready for cleaning.

Any fluid remaining in the pretreater portion 11 may drip from the pretreater 11 during storage and is collected in the reservoir portion 17 for use in the next wash. This reduces product waste.

Wash Formulation Example A

The following gel wash detergent compositions were prepared, of which composition A is according to the invention. where: Borax: sodium tetraborate (10aq) Nonionic surfactant: ethoxylated alcohol with an average of 9 ethylene oxide groups. The gel detergent composition exemplified by composition A was found to be low shear and stable. In addition, typical detergent particles of density 0.8 to 0.9 g / cm3 and up to 5,000 micron diameter could be stable, suspended in this composition for more than two weeks without any observable movement in the particle liquid.

To obtain the values shown in the table above, all rheological measurements were performed at 25 ° C on a Carrimed CSL100 rheometer with a cone and specifically chopped laminar geometry to prevent slippage. Viscosity was measured at different shear rates from very low shear to a shear regime greater than 100 s'1. Two situations are presented: viscosity measured at relatively low shear (20 s'1) and measured at very shear. large (100 s'1). It can be seen that the viscosity of a high shear composition is much lower than that obtained at low shear, while composition B shows almost the same viscosity for high and low shear. In other words, a composition is clearly low shear whereas composition B is not.

In addition, the critical tension is shown. This parameter represents the stress at which the material leaves the upper Newtonian plateau and dilutes under increasing shear. In addition, "Eta 0" values are shown, referring to the zero shear viscosity calculated for from creep flow measurements.

Finally, "Tan delta" values are shown, referring to the reason for loss of more storage modules (G ”/ G ') and reflecting the predominance of viscosity over elastic properties such that materials giving very low values" Tan delta "(tending to zero, such composition A as in the table above) will be much more elastic than those values that give greater" Tan delta "(tending to 90).

Wash Formulation Example B

The following laundry detergent gel compositions have been prepared that composition C is according to the invention and composition D is a comparative composition according to the prior art: where: Borax: sodium tetraborate (10aq) Nonionic surfactant: alcohol ethoxylated with an average of 9 ethylene oxide groups Sodium alcohol sulfate EO: ethoxylated alcohol sulfate with on average 3 ethylene oxide groups. Composition B was stable, transparent, low pourable shear liquid capable of suspending typical stable detergent particles having a density between 0.8 and 0.9 g / cm3 and a diameter of up to 5,000 microns for more than two weeks without any observable movement in the particle liquid.

Rheological critical parameters for both compositions are shown below.

For clarification of the rheological values given in this table, reference is made to the description of the similar table shown in the above example A. Of course it is to be understood that the invention is not intended to be limited to the details of the above embodiment which are described above. by way of example only.

Packaged Wash Product Claim

Claims (1)

A packaged wash product comprising a fluid wash composition (3) contained in a dispensing bottom package (5), wherein: (i) the fluid wash composition (3) has a minimum viscosity of at least 100 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 dispensing bottom package (5) comprising a compressible container (7) in which the fluid wash composition (3) is stored and a dispensing device (9) including a tissue pretreatment device. (11), the dispensing device (9) being a fabric pretreatment device (11) being located at the bottom of the compressible container (7), characterized in that the compressible container (7) is capped by a dosing cap device ( 13) providing a support base (15) of the package (5), and the package having a curved top (21), wherein: - the dispensing device ¢ 9} comprises a channel or duct providing fluid communication between the container (7) and the pretreater (11); - the pretreater (11) comprises a device that allows mechanical cleaning, such as a body with multiple projections; - the projections are flexible so that they move during cleaning providing a light cleaning action, or some or all projections are semi-rigid or rigid to provide a harder mechanical cleaning action; and - the pretreater comprises a generally hemispherical body with multiple projections extending radially thereof.