MXPA01007218A - Detergent tablets comprising a pectate lyase - Google Patents

Abstract

The present invention relates to a laundry or automatic dishwashing composition in tablet form, comprising a pectate lyase, for improved cleaning performance.

Description

DETERGENT TABLETS THAT INCLUDE A PECTATO LIASA FIELD OF THE INVENTION The present invention relates to a composition for washing clothes or automatic dishwashing in the form of a tablet, comprising a pectate lyase.

BACKGROUND OF THE INVENTION The performance of a detergent product is judged by a number of factors, including the ability to remove dirt, and the ability to prevent the dirt from re-depositing, or the decomposition products of the soils in the laundry. Therefore, detergent compositions currently include a complex combination of active ingredients that meet certain specific needs. In particular, current detergent formulations generally include detergent enzymes that provide cleaning and fabric care benefits. The removal of stains from plants, wood, dirt based on clay for molding, muddy dirt, and fruit is one of the most difficult cleaning tasks of today; especially with the tendency towards low washing temperatures. These stains typically contain complex mixtures of fibrous material mainly based on carbohydrates and their derivatives: fibers and cell wall components. The plant-based soils are also accompanied by amylose, sugars and their derivatives. Food stains are often difficult to effectively remove from a dirty substrate. It is particularly challenging to remove colored or "dry" soils derived from fruit and / or vegetable juices. Specific examples of such spots would include orange juice, tomato juice, banana, mango or broccoli dirt. In reality, pectin polymers are important constituents of the cell walls of plants. Pectin is a hetero-polysaccharide with a base structure composed of alternating homogalacturonan (smooth regions) and rhamnogalacturonan (hairy regions). The smooth regions are linear polymers of 1, 4-linked alpha-D-galacturonic acid. The galacturonic acid residues can be esterified with methyl in the carboxyl group to a variable degree, usually in a non-random manner with blocks of polygalacturonic acid being completely esterified with methyl. Substrates in which stains containing pectin are commonly found may be fabrics, tableware or hard surfaces. In addition, the complex nature of everyday "bodily" soils typically found in pillow cases, t-shirts, collars and socks, provides a continuous challenge of complete cleaning for detergents. These soils are difficult to remove completely due in part to their interaction with the pectin components in the primary cell walls of the cotton fibers comprising cotton-containing fabrics, and waste often accumulates on said fabric leading to tarnish and yellowing. In addition, body fluid stains, such as blood and menstrual fluids, are often difficult to effectively remove from a soiled garment, especially when stains have remained for a long time. Daily body filths are also surfaces of toilets and kitchens such as bath tubs, toilet bowls and dishes. Accordingly, enzymes that degrade pectin are known to provide soil / stain removal benefits when used in washing and cleaning operations, specifically to provide for the removal of a wide range of plant, dirt, and fruit stains. and improving the cleaning profile of body dirt of the detergent compositions. By "enzyme that degrades pectin" is understood herein any enzyme that acts to decompose pectin substances and substances related to pectin. Enzymes that degrade pectin can be classified according to their preferential substrate, pectin highly esterified with methyl or pectin of low esterification with methyl and polygalacturonic acid (pectate), and its mechanism of reaction, beta elimination or hydrolysis. The enzymes that degrade the pectin can be mainly of endogenous action, cutting the polymer at random sites within the chain to give a mixture of oligomers, or they can be exogenously acting, attacking from one end of the polymer and producing monomers or dimers. Various activities of pectinase that act in the smooth regions of pectin are included in the classification of enzymes provided by the Enzyme Nomenclature (Enzyme Nomenclature) (1992) such as pectate lyase (EC 4.2.2.2), pectin lyase (EC 4.2. 2.10), polygalacturonase (EC 3.2.1.15), exo-polygalacturonase (EC 3.2.1.67), exo-polygalacturonate lyase (EC 4.2.2.9) and exo-poly-alpha-galacturonosidase (EC 3.2.1.82). Enzymes that degrade pectin are natural mixtures of the enzymatic activities mentioned above. Each type of enzyme that degrades pectin has a unique profile of substrate specificity, activity and stability under different hardness, pH, temperature, surfactant and other detergent ingredient matrix conditions. Enzymes that degrade pectin are specifically directed to degrade pectin substances and in particular cell walls of plants. In particular, pectate lyase enzymes are directed to the cleavage of α-D- (1, 4) glycosidic bonds in poly-D-galacturonans by the β-elimination mechanism. It is recognized in the art that many pectate lyases are dependent on metal ions, in particular calcium dependent. Accordingly, such enzymes may be unstable in a detergent matrix and may lose their activity when calcium is sequestered by builders also present in the detergent matrix. Also, it is also known that the enzymes lose their maximum activity at high pH in the presence of an oxidizing agent as a bleach and are degraded by proteases. In summary, when certain pectate lyases are formulated in a detergent matrix comprising high levels of builder, alkalinity, a bleach and protease system, their enzymatic activity can be significantly reduced unless specific measures are taken to stabilize them. This significantly limits the number of available pectate liases that can be used in detergent applications. It has been surprisingly found that the cleaning benefits of pectate lyase enzymes can be optimized and maximized with a controlled release technology over time. In particular, the technology controlled over time is a tablet wherein the pectate lyase is separated from the other detergent / inactivation detergent ingredients in a different product phase having a different solubility in washing. It has been surprisingly found that an optimum yield efficiency of the pectate lyase enzyme can be achieved when said enzyme is incorporated into a tablet and said system provides significant cleaning benefits of dirt and stains. It has also been found that such controlled release technology over time allows a wider range of pectate lyases to be used, including those that show a high degree of instability in standard detergent matrices. Detergent compositions in tablet form are known in the art. It is understood that detergent compositions in tablet form have several advantages over detergent compositions in the form of particles, such as ease of dosing, handling, transportation and storage. Detergent tablets are most commonly prepared by premixing components of a detergent composition and forming the premixed detergent components in a tablet using any suitable equipment, preferably a tablet press. The tablets are typically formed by compressing the components of the detergent composition so that the tablets produced are sufficiently robust to be able to withstand handling and transportation without sustained damage. In addition to being robust, the tablets should also be dissolved fast enough so that the detergent components are released into the wash water as soon as possible at the start of the wash cycle. The prior art addressed the problem of finding a balance between tablet robustness and tablet dissolution. One solution has been to design multi-phase tablets. The multi-phase detergent tablets described in the prior art are prepared by compressing a first composition in a tablet press to form a substantially flat first layer. Then another detergent composition is supplied to the tablet press at the top of the first layer. This second composition is then compressed to form another substantially flat second layer. Other multi-phase tablets exhibiting dissolution differences are prepared such that the second layer is compressed at a lower force than the first layer resulting in a faster dissolution of the second layer. The use of enzymes that degrade pectin in detergents has already been recognized in the art. The use of enzymes that degrade pectin is also recognized for the cleaning of contact lenses (US 4,710,313-J60196724). Enzymes having a pectinase activity are described in DE 36 35 427 to increase the detergent's ability to remove inorganic dirt, eg, mud, from clothes to be washed without damaging the fibers and without discoloration to allow the use of zeolites and polycarbonate builders that have a lower capacity to disperse inorganic materials than phosphates. The benefits of the use of enzymes that degrade pectin in detergent formulations, in particular those designed for use in laundry, dishwashing and home cleaning operations have been recognized in WO95 / 25790. JP 60226599 discloses detergent compositions comprising conventional detergent actives and a cellulase and hydrolase such as hemicellulase, pectinase, amylase or protease. It is said that the combination of cellulase and hydrolase provides a good washing effect in inorganic dirt together with enzymatic activity. WO95 / 09909 describes an enzyme preparation comprising modified enzymes selected from the group of amylase, lipase, oxidoreductase, pectinase or hemicellulase; modified enzymes having an improved yield due to an alkaline pH and / or increased surface activity obtained by chemical modification or amino acid substitution. Pectin and / or pectolytic and / or hemicellulotic and / or modified lipolytic enzymes are favorably applied in the papermaking industry and amylase and / or modified lipase in laundry and dishwashing. In particular, pectate lyases have been cloned from different genera of bacteria such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, Streptomyces, Penicillium, Baceriodes, Thermomonospora, Fusarium, and Aspergillus. Also from Bacillus subtilis (Nasser et al. (1993) FEBS 335: 319-326) and Bacillus sp. YA-14 (Kim et al. (1994) Biosci, Biotech, Biochem 58: 947-949) has described the cloning of a pectate lisase. The purification of pectate lyases with maximum activity on the scale of pH 8-10 produced by Bacillus pumilus (Dave and Vaughn (1971) J. Bacteriol. 108: 166-174), B. polymyxa (Nagel and Vaughn (1961) has been reported. ) 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). WO 98/45393 discloses detergent compositions containing protopectinase with remarkable detergency against muddy soils. However, never before has the formulation of a pectate lyase been recognized in a detergent tablet with controlled release over time, for superior cleaning performance.

BRIEF DESCRIPTION OF THE INVENTION The present invention relates to compositions for washing clothes or for automatic dish washing in the form of a tablet, comprising a pectate lyase for improved cleaning performance, especially in plant-based and body-based soils.

DETAILED DESCRIPTION OF THE INVENTION The detergent tablet of the present invention is not only robust enough to withstand handling and transportation, but also at least a portion of which dissolves rapidly in the wash water providing a rapid delivery of the pectate lyase enzyme. It is preferred that at least one phase of the tablet dissolves in the wash water within the first ten minutes, preferably five minutes, more preferably four minutes of the laundry cycle of a laundry washing machine or for the automatic washing of laundry. crockery Preferably, the washing machine is a laundry washing machine or for automatic dishwashing. The time within which the multi-phase tablet or a phase of the same or an active detergent component dissolves, is determined in accordance with DIN 44990 using a dishwashing machine available from Bosch in the normal wash program at 65 ° C. ° C with water hardness at 18 ° H, using a minimum of six replicates or a sufficient number to ensure that it is reproducible. Preferably, the pectate lyase and pH regulating materials are incorporated into the fast dissolving portion of the tablet. Without wishing to be bound by theory, it is believed that pectate lyase is released earlier than the other detergent / inactivation detergent ingredients and that optimum pectate lyase activity is obtained at the start of washing under regulated conditions at its pH, leaving the formulation in pectate detergent liases in the full scale of pectate liases available. Tablets are also contemplated wherein the pectate lyase is released at different stages of the washing process according to the needs of the pectate lyase application and matrix conditions.

Detergent Tablet The present invention includes the following different tablet modalities: (a) a tablet comprising a section 1 and a section 2 wherein section 2 comprises a higher level of pectate lyase. (b) the tablet described in (a) wherein the tensile strength of section 1 is larger, preferably at least 2% larger, most preferably 5%, still more preferably 10% and more preferably 30 %, than the tensile strength of section 2. (c) a tablet according to (a) or (b) wherein section 2 has an exposed surface larger than section 1. (d) a tablet according to (a), (b) or (c) wherein the section 2 has an exposed surface equal to the exposed surface of the tablet. (e) a tablet wherein section 2 is applied by a coating process. (f) a tablet according to (a) to (e) wherein section 1 is a slow dissolving section and section 2 is a rapid dissolving section. By "slow dissolution" is meant present a tablet that dissolves in more than 10 minutes according to the method DIN 44990 described. By "fast dissolution" is meant herein a tablet that dissolves within the first ten minutes, preferably five minutes, most preferably four minutes according to the method DIN 44990 described above. Single-phase and multi-phase detergent tablets are suitable for the purpose of the present invention for use in automatic dishwashing and laundry, having improved strength, especially in long-term storage and excellent dissolution characteristics as described in co-pending European application No. 9818716.4 filed on August 28, 1998. Said detergent tablet is not robust enough to resist handling and transportation, but also at least a portion of which dissolves rapidly in the wash water providing rapid supply of the enzyme pectate lyase and pH regulating materials. It is preferred that at least one phase, preferably the section, of the tablet is dissolved in the washing water within the first ten minutes, preferably five minutes, more preferably four minutes of the washing cycle of an automatic dishwashing machine or automatic washing machine in accordance with DIN 44990, previous. The detergent tablets of the present invention comprise a first phase and, in multi-phase tablet embodiments, also comprise a second phase and optional subsequent phases. The first phase is in the form of a body configured of detergent composition comprising one or more detergent components as described below. Preferred detergent components of the first phase include other builder components, bleach, enzymes and surfactant. The components of the detergent composition are mixed together, for example, by mixing dry components or by spraying liquid components. The components are then formed in a first phase using any suitable compression equipment, but preferably in a tablet press. In mold modalities, the first phase is prepared so as to compress at least one mold on the surface of the shaped body. In a preferred embodiment, the mold is formed using a specially designed tablet press, wherein the surface of the punch that comes in contact with the detergent composition is configured so that when it comes into contact and press the detergent composition, it presses a mold or molds multiple in the first phase of the multi-phase detergent tablet. Preferably, the mold will have an interiorly concave or generally concave surface to provide improved adhesion to the second phase. The tablets of the invention may also include one or more additional phases prepared from a composition or compositions comprising one or more detergent components as described below. At least one phase (hereinafter referred to as the second phase) preferably takes the form of a particulate solid (the term encompassing powders, granules, agglomerates and other particulate solids including mixtures thereof with liquid binders, meltable solids , sprinkles, etc.) compressed as a layer in / into one or more molds of the first phase of the detergent tablet, so that the second phase takes on itself the shape of a shaped body. Preferred detergent components include binders, colorants, detergency builders, surfactants, dissolving agents and enzymes, in particular pectate lyase enzymes. In another preferred aspect of the present invention, the second phase and the optionally subsequent phases comprise a dissolving agent that can be selected from a disintegrating agent or an effervescent agent. Suitable disintegrating agents include agents that swell upon contact with water or facilitate the entry and / or exit of water forming channels in the detergent tablet. Any known disintegrating or effervescing agent suitable for use in laundry or dishwashing applications is contemplated for use herein. Suitable disintegrating agents include starches, starch derivatives such as Arbocel (tradename), Vivapur (tradename), both available from Rettenmaier, Nymcel (tradename), available from Metsa-Serla, alginates, acetate trihydrate, burqueite, carbonate monohydrate of formula Na2C03.H20, carboxymethylcellulose (CMC), polymers based on CMC, sodium acetate and aluminum oxide. Suitable effervescent agents are those that produce a gas in contact with water. Suitable effervescent agents can be species that emit oxygen, nitrogen dioxide or carbon dioxide. Examples of preferred effervescent agents can be selected from the group consisting of perborate, percarbonate, carbonate, bicarbonate in combination with inorganic acids such as sulfamic and / or carboxylic acids such as citric, malic or maleic acid, and mixtures thereof. The components of the detergent composition are mixed together, for example, premixing dry components and mixing, or preferably spraying, liquid components. The components of the second phase and the optionally subsequent phases are then compressed to form one or more layers, or are fed and retained within the mold provided by the first phase. Preferred mold embodiments of the present invention comprise two phases: a first phase and a second phase. The first phase will normally comprise a mold, and the second phase will normally consist of an individual active detergent composition. However, it is envisioned that the first phase may comprise more than one mold, and that the second phase may be prepared from more than one active detergent composition. In addition, it is also envisaged that the second phase may comprise more than one active detergent composition contained within a mold. It is also envisioned that various active detergent compositions are contained in separate molds. In this way, potentially chemically sensitive detergent components can be separated to avoid any loss of performance caused by components that react together and potentially become inactive or deplete. In a preferred aspect of the present invention, the first and second phases and / or optionally subsequent phases, may comprise a binder. When present, the binder is selected from the group consisting of organic polymers, for example polyethylene and / or polypropylene glycols, having an average molecular weight of from about 1000 to about 12,000, especially those of molecular weight 4000, 6000 and 9000, polyvinylpyrrolidone. (PVP), especially molecular weight PVP 90,000, polyacrylates, sugars and sugar derivatives, starch and starch derivatives, for example hydroxypropylmethylcellulose (HPMC) and carboxymethylcellulose (CMC); and inorganic polymers such as hexametaphosphate. Polyethylene glycol binders are highly preferred herein.

In a preferred aspect of the present invention the first phase constitutes at least 50% of the total tablet weight. Most preferably the first phase comprises from 60 to 90%, still most preferably from 70 to 85% and most preferably from 80 to 85% of the total tablet weight. The second phase and optional later phases comprise less than 40% of the weight of the tablet. Most preferably, the second phase and / or optional subsequent steps comprise between 20 and 30%, most preferably between 8 and 15% of the total tablet weight. Detergent tablets are prepared using any suitable tableting equipment. Preferably, the multi-phase tablets of the present invention are prepared by compression in a tablet press capable of preparing a tablet comprising a mold. In a particularly preferred embodiment of the present invention, the first phase is prepared using a specially designed tablet press. The punches of this tablet press are modified, so that the surface of the punch that comes into contact with the detergent composition has a convex surface. A first detergent composition is supplied in the die of the tableting press, and the punch is brought down to come into contact and then compress the detergent composition to form a first phase. The first detergent composition is compressed using an applied pressure of at least 250 kg / cm2, preferably between 350 and 2000 kg / cm2, more preferably from 500 to 1500 kg / cm2, most preferably from 600 to 1200 kg / cm2. The punch is then raised, exposing the first phase that contains a mold. A second detergent composition and optionally subsequent detergent compositions comprising the pectate lyase, are then supplied in the mold. The punch of the specially designed tablet press is then lowered a second time to slightly compress the second detergent composition and the optionally subsequent detergent compositions to form the second phase and the optionally subsequent phases. In another embodiment of the present invention, wherein an optional subsequent phase is present, the optionally subsequent phase is prepared in an optionally subsequent compression step substantially similar to the second compression step described above. The second detergent composition and the optionally subsequent detergent compositions are compressed at a pressure preferably less than 350 kg / cm2, more preferably from 40 to 300 kg / cm2, most preferably from 70 to 270 kg / cm2. After compression of the second detergent composition, the punch is raised a second time, and the multi-phase detergent tablet is ejected from the tablet press. Single-ply and multi-ply tablets without molds can be prepared in a similar manner, except using a punch punch having a flat surface. The detergent tablets of the invention are prepared by compressing one or more compositions comprising active detergent components. Suitably, the compositions may include a variety of different detergent components including builders, surfactants, enzymes, bleaching agents, alkalinity sources, dyes, perfume, lime soap dispersants, organic polymeric compounds including agents polymeric dye transfer inhibitors, crystal growth inhibitors, heavy metal ions sequestrants, metal ion salts, enzyme stabilizers, corrosion inhibitors, suds suppressors, solvents, fabric softening agents, optical brighteners and hydrotropes . In the sequential, the proportions of these active components are given by weight of the corresponding composition of active detergent components, unless otherwise indicated. In multi-phase tablets, highly preferred detergent components of the first rapid dissolution phase include a builder, enzymes, specifically the pectate lyase, pH regulating agent and dissolving agent. The highly preferred detergent components of the second slower dissolution phase include a builder compound, a surfactant, an enzyme and a bleaching agent.

Detergency builders Detergency builders may optionally be included in the compositions herein to help control mineral hardness. Inorganic as well as organic builders can be used. Builders are typically used in fabric washing compositions to aid in the removal of particulate dirt. The level of builder can vary widely depending on the final use of the composition. Inorganic or P-containing detergent builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates (exemplified by tripolyphosphates, pyrophosphates, and vitreous polymeric metaphosphates), phosphonates, phytic acid, silicates, carbonates ( including bicarbonates and sesquicarbonates), sulphates, and aluminosilicates. However, non-phosphate builders are required in some places. Importantly, the compositions herein work surprisingly well even in the presence of so-called "weak" builders (comparatively with phosphates) such as citrate, or in the so-called "poor builder condition" which it can occur with stratified zeolite or silicate builders. Examples of silicate builders are alkali metal silicates, in particular those having a SiO2: Na2O in the scale 1.6: 1 to 3.2: 1 and layered silicates, such as the stratified sodium silicates described in the patent of US Pat. No. 4,664,839, issued May 12, 1987 to H. P. Rieck. NaSKS-6 is the brand of a crystalline layered silicate marketed by Hoechst (commonly abbreviated herein as "SKS-6"). Unlike zeolite builders, the Na SKS-6 silicate builder does not contain aluminum. NaSKS-6 has the form of laye-Na2SiOs morphology of stratified silicate. It can be prepared by methods such as those described in German DE-A-3,417,649 and DE-A-3,742,043. SKS-6 is a more preferred layered silicate for use herein, but other layered silicates, such as those having the general formula wherein M is sodium or hydrogen, x is a number from 1.9 to 4 may be used herein. , preferably 2, and y is a number from 0 to 20, preferably 0. Other stratified silicates of Hoechst include NaSKS-5, NaSKS-7 and NaSKS-11, such as the alpha, beta and gamma forms. As mentioned above, delta-Na2SiOs (NaSKS-6 form) is more preferred for use herein. Other silicates can also be useful, for example, magnesium silicate, which can serve as a tightening agent in granulated formulations, as a stabilizing agent for oxygen bleaches, and as a component of foam control systems. Examples of carbonate builders are alkaline earth metal and alkali metal carbonates which are described in German Patent Application No. 2,321,001 published November 15, 1973. Aluminosilicate builders are useful in the present invention. Aluminosilicate builders are of great importance in the heavy duty granular detergent compositions marketed today, and can also be a significant detergency builder ingredient in liquid detergent formulations. The aluminosilicate builders include those that have the empirical formula: Mz (zAI02) and] -xH20 where z and e are integers of at least 6, the mofar ratio of zay is on the scale of 1.0 to about 0.5, and x is an integer from about 15 to about 264. Useful aluminosilicate ion exchange materials are commercially available. These aluminosilicates may be of crystalline or amorphous structure and may be natural aluminosilicates or derivatives in a synthetic manner. A method for producing aluminosilicate ion exchange materials is described in the U.S.A. 3 patent., 985,669, Krummel, et al, issued October 12, 1976. Preferred synthetic crystalline aluminosilicate ion exchange materials useful herein are available under the designations Zeolite A, Zeolite P (B), Zeolite MAP and Zeolite X. In an especially preferred embodiment, the crystalline aluminosilicate ion exchange material has the formula: Na12 [(AI02) 12 (S02)? 2] -xH20 wherein x is from about 20 to about 30, especially about 27 This material is known as Zeolite A. Dehydrated zeolites (x = 0-10) can also be used herein. Preferably, the aluminosilicate has a particle size of about 0.1-10 microns in diameter. Organic detergency builders suitable for the purposes of the present invention include, but are not limited to, a wide variety of polycarboxylate compounds. As used herein, "polycarboxylate" refers to compounds having a plurality of carboxylate groups, preferably at least 3 carboxylates. The polycarboxylate builder in general can be added to the composition in acid form, but can also be added in the form of a neutralized salt. When used in salt form, alkali metal salts, such as sodium, potassium, and lithium, or alkanolammonium salts, are preferred. Polycarboxylate builders include a variety of categories of useful materials. An important category of polycarboxylate builders includes ether polycarboxylates, including oxydisuccinate, as described in Berg, US Patent 3,128,287, issued April 7, 1964, and Lamberti et al, US Patent 3,635,830, issued January 18. from 1972. See also detergent builders "TMS / TDS" of US Patent 4,663,071, issued to Bush et al, May 5, 1987. Suitable ether polycarboxylates also include cyclic compounds, particularly alicyclic compounds, such as those described in US Patents 3,923,679; 3,835,163; 4,158,635; 4,120,874 and 4,102,903.

Other useful detergency builders include the ether hydroxypolycarboxylates, maleic anhydride copolymers with ethylene or vinyl methyl ether, 1,3,5-trihydroxybenzene-2,4,6-trisulfonic acid, and carboxymethyloxysuccinic acid, the different alkali metal salts, ammonium, and substituted ammonium salts of polyacetic acids such as ethylenediaminetetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, oxydisuccinic acid, polymaleic acid, benzene-1, 3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts of the same. Citrate detergent builders, for example, citric acid, and soluble salts thereof (in particular sodium salt), are polycarboxylate builders of particular importance for liquid heavy duty detergent formulations because of their availability of renewable resources and their biodegradability The citrates can also be used in granular compositions, especially in combination with layered zeolite and / or silicate builders. Oxydisuccinates are also especially useful in said compositions and combinations. Also suitable in the detergent compositions of the present invention are 3,3-dicarboxy-4-oxa-1,6-hexanedioates and the related compounds described in the U.S.A. 4,566,984, Bush, issued January 28, 1986. Useful succinic acid builders include alkylsuccinic and alkenyl succinic acids of C5-C2o, and salts thereof. A particularly preferred compound of this type is dodecenylsuccinic acid. Specific examples of succinate builders include: laurylsuccinate, myristylsuccinate, palmitylsuccinate, 2-dodecenylsuccinate (preferred), 2-pentadecenylsuccinate, and the like. Lauryl succinates are the preferred builders of this group, and are described in European patent application 86200690.5 / 0,200,263, published on November 5, 1986. Other suitable polycarboxylates are described in US Pat. 4,144,226, Crutchfield et al., Issued March 13, 1979 and in the patent of E.U.A. 3,308,067, Diehl, issued March 7, 1967. See also Díehl patent of E.U.A. 3,723,322. Fatty acids, for example, C 2 -C 8 monocarboxylic acids, can also be incorporated into the compositions alone, or in combination with the aforementioned builders, especially citrate and / or succinate builders, to provide additional detergency builder activity. Said use of fatty acids will generally result in a decrease in foam production, which can be taken into account by the formulator. In situations where phosphorus-based detergency builders can be used, and especially the formulation of bars used for manual washing operations, the various alkali metal phosphates such as the well-known sodium tripolyphosphates, sodium pyrophosphate and the like can be used. sodium orthophosphate. Phosphonate detergency builders such as ethane-1-hydroxy-1,1-diphosphonate and other known phosphonates (see, for example, U.S. Patents 3,159,581, 3,213,030, 3,422,021, 3,400,148 and 3,422,137) can also be used. Suitable surfactants herein include anionic surfactants such as alkyl sulphates, alkyl ether sulphates, alkylbenzene sulphonates, alkyl glyceryl sulfonates, alkyl and alkenyl sulphonates, alkylethoxycarboxylates, N-acyl sarcosinates, N-acyltaurates and alkylsuccinates and sulfosuccinates, wherein the alkyl, alkenyl or acyl moiety is of C5-C20, preferably linear or branched C? oC? 8; cationic surfactants such as choline esters (see documents US-A-4228042, US-A-4239660 and US-A-4260529) and C-Ciß N-alkyl or alkenyl monoammonium surfactants, where the remaining N positions they are substituted by methyl, hydroxyethyl or hydroxypropyl groups; low and high cloud point nonionic surfactants, and mixtures thereof, including nonionic alkoxylated surfactants (especially ethoxylates derived from primary alcohols of C6-C18), ethoxylated-propoxylated alcohols (eg, Poly-Tergent® SLF18 from Olin Corporation), epoxy-blocked poly (oxyalkylated) alcohols (for example, Poly-Tergent® SLF18B from Olin Corporation - see WO-A-94/22800), poly (oxyalkylated) alcohol surfactants blocked with ether, and compounds polymeric polyoxyethylene-polyoxypropylene block such as PLURONIC®, REVERSED PLURONIC® and TETRONIC® by BASF-Wyandotte Corp., Wyandotte, Michigan; amphoteric surfactants such as amine oxides and alkyl amphocarboxylic surfactants such as Miranol ™ C2M; and zwitterionic surfactants such as betaines and sultaines; and mixtures thereof. Suitable surfactants herein are described, for example, in US-A-3,929,678, US-A-4,259,217, EP-A-0414 549, WO-A-93/08876 and WO-A-93/08874. Surfactants are typically present at a level of from about 0.2% to about 30% by weight, more preferably from about 0.5% to about 10% by weight, and most preferably from about 1% to about 5% by weight of the composition. Enzymes suitable for use in section 1 of the present include enzymes such as protease, amylase, lipase, cutinase and / or cellulase. Suitable proteases are the subtiiisins that are obtained from particular strains of B. subtilis and ß. licheniformis (subtilisin BPN and BPN '). A suitable protease is obtained from a strain of Bacillus, having a maximum activity on the entire pH scale of 8 to 12, developed and sold ® as ESPERASE by Novo Industries A / S of Denmark, hereinafter "Novo." The preparation of this enzyme and analogous enzymes is described in GB 1, 243,784, by Novo. Other suitable proteases include ALCALASE®, DURAZYM® and SAVINASE® from Novo and MAXATASE®, MAXACAL®, PROPERASE® and MAXAPEM® (Maxacal manipulated with proteins) by Gist-Brocades. Proteolytic enzymes also include modified bacterial serine proteases, such as those described in European Patent Application No. 87303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98) and which is herein called " Protease B ", and in the European patent application 199 404, Venegas, published on October 29, 1986, which refers to a modified bacterial serine proteolytic enzyme which is referred to herein as" Protease A ". The protease called "Protease C" is suitable, which is a variant of a Bacillus alkaline serine protease in which lysine replaces arginine in position 27, tyrosine replaces valine in position 104, serine replaces asparagine in position 123 and alanine replace threonine at position 274. Protease C is described in EP 90915958: 4, which corresponds to WO 91/06637, published May 16, 1991. Variants are also included herein genetically modified, particularly Protease C. A preferred protease referred to as "Protease D", is a variant of carbonyl hydrolase having an amino acid sequence that is not found in nature, which is derived from a precursor carbonyl hydrolase by substituting an amino acid different by a plurality of amino acid residues at a position in said carbonyl hydrolase equivalent to the +76 position, preferably also in combination Nation with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, + 128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and / or +274 according to the numeration of the subtilisin of Bacillus amyloliquefaciens as described in WO95 / 10591 and in the patent application of C. Ghosh, et al, "Bleaching Compositions Comprising Protease Enzymes", which has serial number US 08 / 322,677, issued on October 13, 1994. A carbonylhydrolase variant of the protease described in WO95 / 10591, having an amino acid sequence derived by replacing a plurality of amino acid residues replaced in the precursor enzyme corresponding to the position +210 in combination with one or more of the following residuals: +33, +62, +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, +218 and +222, where the numbered position corresponds to the subtilisin of Bacillus amyloliquefaciens that occurs naturally or to equivalent amino acid residues in other carbonylhydrolases or subtilisins, such as Bacillus lentus subtilisin (copending US patent application No. 60 / 048,550, filed June 4, 1997). Also suitable for the present invention are the proteases described in EP 251 446 and WO-A-91/06637 and the BLAP® protease described in WO91 / 02792 and its variants described in WO 95/23221. See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO93 / 18140 A to Novo. Enzymatic detergents comprising protease, one or more other different enzymes and a reversible protease inhibitor are described in WO 92/03529 A to Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter & Gamble. A recombinant trypsin-like protease for detergents suitable herein is described in WO 94/25583 to Novo. Other suitable proteases are described in EP 516 200 by Unilever. The proteolytic enzymes are incorporated in the detergent compositions of the present invention at a level of 0.0001% to 2%, preferably from 0.001% to 0.2%, most preferably from 0.005% to 0.1% pure enzyme by weight of the composition. Cellulases useful in the present invention include both bacterial and fungal cellulases. Preferably, they will have an optimum pH between 5 and 12 and an activity greater than 50 CEVU / mg (cellulose viscosity unit). Suitable cellulases are described in the US patent. No. 4,435,307, Barbesgoard et al, J61078384 and WO96 / 02653, which describes fungal cellulases produced respectively from Humicola insolens, Trichoderma, Thievalia and Sporotrichum. EP 739 982 describes cellulases isolated from novel species of Bacillus. Suitable cellulases are also described in GB-A-2,075,028; GB-A-2,095,275; DE-OS-2,247,832 and W095 / 26398. Examples of said cellulases are the cellulases produced by a strain of Humicola insolens (Humicola grísea var. Thermoidea), particularly the DSM 1800 strain of Humicola.

Other suitable cellulases are the cellulases originated from Humicola insolens which have a molecular weight of approximately 50 KDa, an isoelectric point of 5.5, and which contain 415 amino acids; and a ~ 43kD endoglucanase derived from Humicola insolens, DSM 1800, which exhibits cellulase activity; an endoglucanase component that is preferred has the amino acid sequence described in PCT patent application No. WO 91/17243. Also suitable cellulases are the EGIII celulases of Trichoderma longibrachiatum described in WO94 / 21801, Genencor, published on September 29, 1994. Particularly suitable cellulases are cellulases that have color care benefits. Examples of said cellulases are the cellulases described in the European patent application No. 91202879.2, filed on November 6, 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A / S) are especially useful. See also documents W091 / 17244 and WO91 / 21801. Other cellulases suitable for fabric care and / or cleaning properties are described in WO96 / 34092, W096 / 17994 and W095 / 24471. Said cellulases are normally incorporated in the detergent composition at levels of 0.0001% to 2% active enzyme by weight of the detergent composition. The peroxidase enzymes are used in combination with oxygen sources, for example, percarbonate, peroxide, persulfate, hydrogen peroxide, etc. and with a phenolic substrate as a bleach improving molecule. They are used for "bleaching in solution", that is, to avoid the transfer of dyes or pigments removed from substrates during washing operations, to other substrates in the washing solution. Peroxidase enzymes are known in the art and include, for example, horseradish peroxidase, ligninase, and haloperoxidase such as chloro- and bromoperoxidase. Peroxidase-containing detergent compositions are described, for example, in PCT International Application WO89 / 099813, WO89 / 09813 and European Patent Application EP No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, presented on February 20, 1996. Also suitable is the laccase enzyme. The improvers are generally comprised at a level of 0.1% to 5% by weight of the total composition. Preferred builders are substituted phenoxyzine and phenoxyzine, 10-phenothiazinopropionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazinopropionic acid (POP) and 10-methylphenoxazine (described in W094 / 12621). ) and substituted syringates (substituted C3-C5 alkylsalicylates) and phenols. Percarbonate or sodium perborate are preferred sources of hydrogen peroxide. Said peroxidases are normally incorporated in the detergent composition at levels of 0.0001% to 2% of active enzyme by weight of the detergent composition. Other preferred enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for detergent use include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, such as those described in British Patent 1, 372, 034. Suitable lipases include those that show a positive immunological cross-reaction with the lipase antibody, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the tradename Lipase P " Amano ", hereinafter referred to as" Amano-P ". Other suitable commercial lipases include Amano-CES, lipases ex Chromobacter viscosum, for example Chromobacter viscosum var. lipolyticum NRRLB 3673, from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp, E.U.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. Especially suitable lipases are the ® ® ® lipases such as M1 Lipase and Lipomax (Gist-Brocades) and Lipolase and ® Lipolase Ultra (Novo), which has been found to be very effective when used in combination with the compositions of the present invention. Also suitable are the lipolytic enzymes described in EP 258 068, WO92 / 05249, W095 / 22615 by Novo Nordisk, and in WO94 / 03578, W095 / 35381 and WO-A-96/00292 by Unilever. Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special type of lipase, namely lipases which do not require interfering activation. The addition of cutinases to detergent compositions has been described in for example, WO-A-88/09367 (Genencor); WO 90/09446 Plant Genetic System) and W094 / 14963 and WO-A-94/14964 (Unilever).

The lipases and / or cutinases are normally incorporated in the detergent composition at levels of 0.0001% to 2% active enzyme by weight of the detergent composition. Amylases (a and / or ß) can be included for the removal of carbohydrate-based stains. WO94 / 02597 discloses detergent compositions that incorporate mutant amylases. See also WO95 / 10603, Novo Nordisk A / S, published April 20, 1995. Other amylases for use in detergent compositions include α and β-amylases. A-amylases are known in the art and include those described in the U.S.A. No. 5,003,257; EP 252,666; WO / 91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and in the description of British Patent No. 1, 296,839 (Novo). Other suitable amylases are the amylases of improved stability described in WO94 / 18314, published on August 18, 1994 and WO96 / 05295, Genencor, published on February 22, 1996 and the amylase variants having additional modification in the immediate parent, available from Novo Nordisk A / S and described in WO95 / 10603, published April 1995. Also suitable are the amylases described in EP 277 216, W095 / 26397 and WO-A-96/23873 (all by Novo Nordisk). Examples of commercial a-amylases products are Purafect Ox Am® from Genencor and Termamyl®, Ban®, Fungamyl® and Duramyl®, Natalase® all available from Novo Nordisk A / S Denmark. W095 / 26397 describes other suitable amylases: α-amylases characterized by having a specific activity at least 25% greater than the specific activity of Termamyl® at a temperature range of 25 ° C to 55 ° C and at a pH value on the scale of 8 to 10, measured by the test ® Phadebas of α-amylase activity. Suitable are the variants of the above enzymes, described in W096 / 23873. Other amylolytic enzymes with improved properties with respect to the activity level and the combination of thermostability and higher activity level are described in W095 / 35382. The amylolytic enzymes are incorporated in the detergent compositions of the present invention at a level of from 0.0001% to 2%, preferably from 0.00018% to 0.06%, most preferably from 0.00024% to 0.048% pure enzyme by weight of the composition. The aforementioned enzymes may have any suitable origin, such as vegetable, animal, bacterial, fungal and yeast. The origin can also be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidic, halophilic, etc). The purified or non-purified forms of these enzymes can be used. At present, it is common practice to modify wild-type enzymes by means of protein / gene manipulation techniques in order to optimize their efficiency of performance in the detergent compositions of the invention. For example, the variants can be designed in such a way that the compatibility of the enzyme with commonly found ingredients of such compositions is increased. Alternatively, the variant can be designed such that the optimum pH, bleach or chelator stability, catalytic activity and the like, of the enzyme variant is adjusted to suit the particular cleaning application. In particular, attention should be focused on amino acids sensitive to oxidation in case of bleaching stability and on surface charges for compatibility with surfactant. The isoelectric point of such enzymes can be modified by the replacement of some charged amino acids, for example, an increase in the isoelectric point can help improve compatibility with anionic surfactants. The stability of the enzymes can be further enhanced by the creation of, for example, additional salt bridges and by reinforcing the calcium binding sites to increase the chelator stability. Special attention should be paid to cellulases, since most cellulases have separate binding domains (CBD). The properties of such enzymes can be altered by modifications in these domains. Said enzymes are normally incorporated in the detergent composition at levels of 0.0001% to 2% active enzyme by weight of the detergent composition. Enzymes can be added as separate individual ingredients (pellets, granules, stabilized liquids, etc. containing an enzyme) or as mixtures of two or more enzymes (eg cogranulated materials). Other suitable detergent ingredients that can be added are enzyme oxidation scavengers which are described in European patent application 92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation scavengers are ethoxylated tetraethylenepolyamines. A range of enzyme materials and means for their incorporation into synthetic detergent compositions are also disclosed in WO 9307263 A and WO 9307260 A to Genencor International, WO 8908694 A to Novo, and US Patent 3,553,139, January 5, 1971. to McCarty et al. In the patent of E.U.A. 4,101,457, Place et al, July 18, 1978, and in the patent of E.U.A. 4,507,219, Hughes, March 26, 1985, enzymes are also described. Useful enzyme materials for liquid detergent formulations, and their incorporation into such formulations, are described in the US patent. 4,261, 868, Hora et al, April 14, 1981. Enzymes for use in detergents can be stabilized by various techniques. Enzyme stabilization techniques are described and exemplified in the US patent. 3,600,319, August 17, 1971, to Gedge, et al, EP 199 405 and EP 200,586, October 29, 1986, Venegas. Enzyme stabilization systems are also described, for example, in the U.S. patent. 3,519,570. A Bacillus sp. AC13 useful and which gives proteases, xylanases and cellulases is described in WO 9401532 A to Novo, cellulases of bacteria and fungi such as Carezyme and Celluzyme (Novo Nordisk A / S); peroxidases; lipases such as Amano-P (Amano Pharmaceutical Co.), M1 Lipase® and Lipomax® (Gist-Brocades) and Lipolase® and Lipolase Ultra® (Novo); cutinases; proteases such as Esperasen Alcalase®, Durazym® and Savinase® (Novo) and Maxatase®, Maxacal®, Properase® and Maxapem® (Gist-Brocades); and α and β-amylases such as Purafect Ox AmR (Genencor) and Termamyl®, BanR, Fungamyl®, Duramyl® and Natalase® (Novo); and mixtures thereof. Enzymes are preferably added herein as pellets, granulates or cogranulates at levels typically in the range of about 0.0001% to about 2% by weight of pure enzyme of the composition. Suitable bleaching agents herein include chlorine and oxygen bleach, especially inorganic perhydrate salts such as sodium mono- and tetrahydrate perborate, and sodium percarbonate optionally coated to provide controlled release rate (see, for example, GB-A-1466799 on sulphate / carbonate coatings), preformed organic peroxyacids and mixtures thereof with organic peroxyacid bleach precursors and / or bleach catalysts containing transition metal (especially manganese or cobalt). The inorganic salts of perhydrate are typically incorporated at levels in the range of from about 1% to about 40% by weight, preferably from about 2% to about 30% by weight, and more preferably from about 5% to about 25% by weight. % by weight of the composition. Preferred peroxyacid bleach precursors for use herein include precursors of perbenzoic acid and substituted perbenzoic acid; cationic peroxyacid precursors; peracetic acid precursors such as TAED, sodium acetoxybenzenesulfonate and pentaacetylglucose; pemonanoic acid precursors such as 3,5,5-trimethylhexanoyloxybenzenesulfonate (iso-NOBS) of sodium and sodium nonanoyloxybenzenesulfonate (NOBS); N-nonanoyl-6-aminocaproic acid phenolsulfonate ester (NACA-OBS, described in WO94 / 28106), which are perhydrolyzed to form a peracid as the active bleaching species, producing an improved bleaching effect, substituted alkyl peroxyacid precursors with amide (see EP-A-0170386); and benzoxazine peroxyacid precursors (see EP-A-0332294 and EP-A-0482807). Bleach precursors are typically incorporated at levels in the range of about 0.5% to about 25%, preferably from about 1% to about 10% by weight of the composition, while the preformed organic peroxyacids are typically incorporated at in the range from 0.5% to 25% by weight, more preferably from 1% to 10% by weight of the composition. Preferred bleach catalysts for use herein include manganese triazacyclononane and related complexes (see US-A-4246612 and US-A-5227084); bispyridylamine Co, Cu, Mn and Fe and related complexes (see document US-A-5114611); and cobalt (III) pentaamine acetate and related complexes (see US-A-4810410). Other suitable components herein include organic polymers having dispersing, anti-redeposition, dirt release, and other detergency properties, at levels of from about 0.1% to about 30%, preferably about 0.5% a about 15%, more preferably from about 1% to about 10% by weight of the composition. Preferred anti-redeposition polymers herein include polymers containing acrylic acid such as Sokalan PA30, PA20, PA15, PA10 and Sokalan CP10 (BASF GmbH), Acusol 45N, 480N, 460N (Rohm and Haas), copolymers of acrylic acid / maleic acid such as Sokalan CP5 and copolymers of acrylic acid / methacrylic acid. Preferred dirt release polymers herein include alkyl and hydroxyalkyl celluloses (see US-A-4,000,093), polyoxyethylenes, polyoxypropylenes and copolymers thereof, and nonionic and anionic polymers based on esters of ethylene glycol terephthalate, propylene glycol, and mixtures thereof. Heavy metal sequestrants and crystal growth inhibitors are suitable for use herein at levels generally of from about 0.005% to about 20%, preferably from about 0.1% to about 10%, more preferably about 0.25% to about 7.5%, and most preferably from about 0.5% to about 5% by weight of the composition, for example diethylenetriamine penta (methylenephosphonate), ethylenediamine tetra (methylenephosphonate), hexamethylenediamine tetra- (methylenephosphonate), ethylene diphosphonate, hydroxyethylene-1 , 1-diphosphonate, nitrilotriacetate, ethylenediaminetetraacetate and ethylenediamine-N, N'-disuccinate, in their salt and free acid forms. The compositions herein, especially for use in dishwashing, may contain a corrosion inhibitor such as organic silver coating agents at levels of from about 0.05% to about 10%, preferably about 0.1% at about 5% by weight of the composition (especially paraffins such as Winog 70 marketed by Wintershall, Salzbergen, Germany), nitrogen-containing corrosion inhibiting compounds (for example, benzotriazole and benzimidazole - see GB-A-1137741) and compounds of Mn (ll), particularly Mn (ll) salts of organic ligands, at levels of from about 0.005% to about 5%, preferably from about 0.01% to about 1%, more preferably from about 0.02% to about 0.4 % by weight of the composition. Other suitable components herein include dyes, water-soluble bismuth compounds such as bismuth acetate and bismuth citrate at levels of from about 0.01% to about 5%, enzyme stabilizers such as calcium, boric acid, prapylene glycol and sweeteners. chlorine bleach at levels of from about 0.01% to about 6%, lime soap dispersants (see WO-A-93/08877), suds suppressors (see WO-A-93/08876 and EP-A- 0705324, polymeric dye transfer inhibiting agents, optical brighteners, perfumes, fillers, clay and cationic fabric softeners The detergent tablets herein are preferably not formulated to have an unduly high pH, preferably having a pH , measured as a 1% solution in distilled water, from 8.0 to 12.5, more preferred from 9.0 to 11.8, more preferred still from 9.5 to 11.5. intact will be the tablets described in co-pending European application No. 9815525.2 filed July 17, 1998. Said tablets are multi-phase detergent tablets for use in a washing machine, the tablet comprising: a) a slower dissolving phase in the form of a shaped body that has at least one mold therein (Section 1); and b) a second fast dissolving phase in the form of a particulate solid compressed within said mold (Section 1), comprising the pectate lyase enzyme of the present invention. In preferred embodiments, the first phase is a compressed shaped body prepared at an applied compression pressure of at least about 350 kg / cm2 (3.43 kN / cm2), preferably from about 400 to about 2000 kg / cm2, and especially from about 600 to about 1200 kg / cm2 (in the present, the compression pressure is the force applied divided between the cross-sectional area of the tablet in a plane transverse to the applied force - in effect, the cross-sectional area of the tablet. given of the rotary press). It is also preferred that the particulate solid of the second phase (whose terminology is intended to include the possibility of 'second' multiple phases, sometimes referred to herein as 'subsequent optional phases') is compressed in said mold at a lower compression pressure than which is applied to the first phase and preferably at a compression pressure less than about 350 kg / cm2, preferably in the range of about 40 kg / cm2 to about 300 kg / cm2, and more preferably around 70 to about 270 kg / cm2, such tablets being preferred herein from the viewpoint of providing optimal tablet integrity and strength (measured, for example, by the Child Bite Strength [CBS] test) and product dissolution characteristics. The tablets of the invention preferably have a CBS of at least 10 kg, preferably greater than 12 kg, most preferably greater than 14 kg, the CBS being measured in accordance with the Test Specification of the Product Safety Commission for the US Consumer. In addition, the compression pressures applied to the first and second phases will generally be at a ratio of at least about 2: 1, preferably at least about 4: 1. Thus, in accordance with a further aspect of the invention , a multi-phase detergent tablet is provided for use in a washing machine, the tablet comprising: a) a first slow dissolving phase in the form of a compressed shaped body having at least one mold therein, the body configured being prepared at a compression pressure of at least about 350 kg / cm2; and b) a second phase in the form of a particulate solid compressed within said mold, the second phase being compressed at a pressure of less than about 350 kg / cm2, the pectate lyase enzyme of the present invention comprising. In other preferred embodiments, the second phase is in the form of a compressed or shaped body contained in adhesive form, for example, by physical or chemical adhesion, within at least one mold of the first body. It is also preferred that the first and second phases are at a relatively high weight ratio to each other, for example, at least about 6: 1, preferably at least about 10: 1; and that the tablet composition contains one or more detergent active agents (eg, enzymes, bleaches, bleach activators, bleach catalysts, surface active agents, chelating agents, etc.) that are predominantly concentrated in the second phase, for example, that at least about 50%, preferably at least about 60%, especially about 80% by weight of the active agent (based on the total weight of the active agent in the tablet) is in the second phase of the tablet. In this case specifically, the preferred active is the pectate lyase enzyme. Again, said compositions are optimal for resistance, dissolution, cleaning and pH regulation characteristics of the tablet by providing, for example, tablet compositions capable of dissolving in the wash solution to supply at least 50%, preferably at least 60%, and more preferably at least 80% by weight of the pectate lyase to the washing solution within 10, 5, 4 or even 3 minutes of the start of the washing process. Thus, in accordance with a further aspect of the invention, a multi-phase detergent tablet is provided for use in a washing machine, the tablet comprising: a) a first slow dissolving phase in the form of a compressed shaped body having at least one mold therein (Section 1), and b) a second fast dissolving phase containing pectate lyase and in the form of a particulate solid compressed within said mold (section 2), and wherein the section 2 of the tablet comprises 70%, preferably at least 85%, more preferably at least 95% by weight of the pectate lyase that is supplied to the wash within the first 10 minutes, preferably within the first 5 minutes, and more preferably within of the first 3 minutes of the washing procedure. The following tablets, specifically designated for laundry purposes, are also suitable: Tablet Manufacturing Detergent tablets can be prepared by simply mixing the solid ingredients and compressing the mixture in a conventional tablet press as used, for example, in the pharmaceutical industry. Preferably, the main ingredients, in particular gelling surfactants, are used in the form of particles. Any liquid ingredients, for example, surfactant or foam suppressant, can be incorporated in a conventional manner into the ingredients into solid particles. In particular for laundry tablets, the ingredients such as builder and surfactant can be spray-dried in a conventional manner and then can be compacted at a suitable pressure. Preferably, the tablets according to the invention are compressed using a force of less than 100000 N, preferably less than 50000N, preferably less than 5000N and more preferably less than 3000N. In fact, the most preferred embodiment is a tablet suitable for washing compressed laundry using a force of less than 2500N, but tablets for automatic dishwashing can also be considered for example, wherein such tablets for automatic dishwashing usually They are more compressed than laundry tablets. The particulate material used to manufacture the tablet of this invention can be made by any process of particle formation or granulation. An example of such a process is spray drying (in a co-current or countercurrent spray drying tower) which typically gives low bulk densities of 600 g / L or lower. The higher density particulate materials can be prepared by granulation and densification in a batch mixer by high shear / granulator or by a continuous granulation and densification process (for example, using Lodige® CB and / or Lodige® KM mixers). ). Other suitable methods include fluidized bed processes, compacting methods (for example roll compaction), extrusion, as well as any particulate material made by any chemical method such as flocculation, crystallization, concretion, etc. The individual particles can also be any other particle, granule, sphere or grain. The components of the particulate material can be mixed together by any conventional means. The batch is suitable in, for example, a concrete mixer, Nauta mixer, ribbon mixer, or any other. Alternatively, the mixing process can be carried out continuously by measuring each component by weight in a moving band, and mixing them in one or more drum (s) or mixer (s). A non-gelling binder can be sprayed into the mixture of some or all of the components of the particulate material. Other liquid ingredients can also be sprayed into the mixture of components either separately or pre-mixed. For example, perfume and suspensions of optical brighteners can be sprayed. A finely divided flow aid (powdering agent such as zeolites, carbonates, silicas) can be added to the particulate material after spraying the binder, preferably towards the end of the process, to make the mixture less sticky. Tablets can be manufactured using any compaction process, such as tabletting, briquetting or extrusion, preferably tabletting. Suitable equipment includes a standard single goipe press or rotary press (such as Courtoy®, Korch®, Manesty®, or Bonals®). The tablets prepared according to this invention preferably have a diameter of between 20 mm and 60 mm, preferably of at least 35 and up to 55 mm, and a weight between 25 and 100 g. The ratio of height to diameter (or width) of the tablets is preferably greater than 1: 3, more preferably greater than 1: 2. The compaction pressure used to prepare these tablets needs not to exceed 100000 kN / m2, preferably not to exceed 30000 kN / m2, preferably not to exceed 5000 kN / m2, more preferably not to exceed 3000 kN / m2 and most preferably not to exceed 1000 kN / m2. In a preferred embodiment according to the invention, the tablet has a density of at least 0.9 g / cc, preferably of at least 1.0 g / cc, and preferably less than 2.0 g / cc, more preferably less than 1.5 g / cc, more preferably less than 1.25 g / cc and most preferably less than 1.1 g / cc.

Multilayer tablets are typically formed in rotary presses by placing the matrices of each layer, one after the other, in matrix force feed flasks. As the process continues, the matrix layers are then pressed into the precompression and compression stage stations to form the multilayer tablet. With some rotary presses, it is also possible to compress the first feed layer before compressing the entire tablet.

Hydrotrope Compound In a preferred embodiment of the invention, a highly soluble compound having a cohesive effect is integrated into the tablet of the invention, wherein this compound is also a hydrotrope compound. Said hydrotrope compound can generally be used to promote dissolution of the surfactant by preventing gelation, so that they can be, for example, usefully included in a faster, softer dissolution layer which also contains pectate lyase. A specific compound is defined as a hydrotrope in the following manner (see SE Friberg and M. Chiu, J. Dispersion Science and Technology, 9 (5 and 6), pages 443 to 457 (1988-1989)): 1. Prepare a solution comprising 25% by weight of the specific compound and 75% by weight of water. 2. Then octanoic acid is added to the solution in a ratio of 1.6 times the weight of the specific compound in solution, the solution being at a temperature of 20 ° Celcius. The solution is mixed in a Sotax beaker with an agitator with a marine propeller, the impeller being positioned about 5 mm above the bottom of the beaker, the mixer being adjusted at a rotation speed of 200 revolutions per minute. 3. The specific compound is hydrotrope if the octanoic acid is completely solubilized, that is, if the solution comprises only one phase, the phase being a liquid phase. It should be mentioned that in a preferred embodiment of the invention, the hydrotrope compound is a flowable material made of solid particles under operating conditions between 15 and 60 ° Celsius. Hydrotrope compounds include the listed compounds after: A list of commercial hydrotropes could be found in Emulsifiers and Detergents by McCutcheon published by the division McCutcheon of Manufacturing Confectioners Company. Composed of Interest also include: 1. Non-ionic hydrotrope with the following structure: R - O - (CH2CH20) x (CH-CH20) and H CH3 wherein R is an alkyl chain of C8-C10, x varies from 1 to 15, and from 3 to . 2. Anionic hydrotropes such as alkali metal arylsulfonates. This includes alkali metal salts of benzoic acid, salicylic acid, benzenesulfonic acid and its many derivatives, naphthoic acid and various hydro-aromatic acids. Examples of these are sodium, potassium salts and ammonium benzenesulfonate salts derived from toluenesulfonic acid, xylenesulfonic acid, cumenesulfonic acid, tetralinsulfonic acid, naphthalenesulfonic acid, methylnaphthalenesulfonic acid, dimethylnaphthalenesulfonic acid, trimethylnaphthalenesulfonic acid. Other examples include dialkylbenzenesulfonic acid salts such as salts of diisopropylbenzenesulfonic acid, ethylmethylbenzenesulfonic acid, alkylbenzenesulfonic acid with an alkyl chain length of 3 to 10, (preferably 4 to 9), linear or branched alkylsulfonates with an alkyl chain with 1 to 18 carbons. 3. Solvent hydrotropes such as alkoxylated glycerines and alkoxylated glycerides, alkoxylated glycerines of esters, alkoxylated fatty acids, glycerin esters, polyglycerol esters. The preferred alkoxylated glycerines have the following structure: wherein I, m, and n are each a number from 0 to about 20, with l + m + n = from about 2 to about 60, preferably from about 10 to about 45 and R represents H, CH3 or C2H5. Preferred alkoxylated glycerides have the following structure wherein R1 and R2 are each CnCOO or - (CH2CHR3-0) H where R3 = H, CH3 or C2H5 and I is a number from 1 to about 60, n is a number from about 6 to about 24. 4. Hydrotropes Polymers such as those described in EP636687: RR, - (CH2-C)? - (CH2-C), E R2 wherein E is a hydrophilic functional group, R is H or a C1-C10 alkyl group or is a hydrophilic functional group; R1 is H or a lower alkyl group or an aromatic group, R2 is H or a cyclic alkyl group or aromatic group. The polymer typically has a molecular weight of between about 1000 and 1000000.

. Hydrotropes of unusual structure such as 5-carboxy-4-hexyl-2-cyclohexane-1-yl octanoic acid (Diacid®). The use of said compounds in the invention would further increase the rate of dissolution of the tablet, since a hydrotrope compound facilitates the dissolution of surfactants, for example. Such a compound could be formed from a mixture or from a single compound.

Coating In another embodiment of the present invention, the strength of the tablet according to the invention can be further improved by making a coated tablet, the coating covering a non-coated tablet according to the invention and containing the enzyme pectate lyase, thereby improving additionally the mechanical characteristics of the tablet as it allows a rapid dissolution of the enzyme pectate lyase. This applies more advantageously to the multilayer tablets according to the invention, whereby the dissolution characteristics of the outer layer can be tailored to allow rapid release of the coating ingredients, thus combining the advantage of the coating with the advantage of the release time. In one embodiment of the present invention, the tablets may be coated such that the tablet does not absorb moisture, or absorb moisture only at a very slow rate. The coating is also resistant so that moderate mechanical shocks to which the tablets are subjected during handling, packing and shipping result in very low breaking or friction levels. Finally, the coating is preferably brittle so that the tablet decomposes when subjected to stronger mechanical shock. Furthermore, it is favorable if the coating material is dissolved under alkaline conditions, or is easily emulsified by surfactants, to allow the release of the pectate lyase. This helps to avoid the problem of visible residues in the window of a front loading washing machine during the washing cycle, and also avoids the deposition of undissolved particles or lumps of material in the laundry load. The solubility in water is measured following the test protocol of E1148-87 of ASTM entitled, "Standard test method for aqueous solubility measurements". Suitable coating materials which can be used in combination with the pectate lyase are dicarboxylic acids. Particularly suitable dicarboxylic acids are selected from the group consisting of oxalic acid, malonic acid, succinic acid, glutaric acid, adipic acid, pimelic acid, suberic acid, azelaic acid, sebacic acid, undecanedioic acid, dodecanedioic acid, tridecanedioic acid, and mixtures of the same. The coating material preferably has a melting point of 40 ° C to 200 ° C.

The coating can be applied in a number of ways. However, the preferred method when the pectate lyase is contained in the coating is to coat with a solution of the material. In this method, the coating is applied as a solution, the solvent being dry to leave a consistent coating. The substantially insoluble material can be applied to the tablet by, for example, sprinkling or immersing it. Clearly substantially insoluble materials having a melting point below 40 ° C are not sufficiently solid at ambient temperatures and it has been found that materials having a melting point above about 200 ° C are not viable to be used. Preferably, the materials are melted on the scale from 60 ° C to 160 ° C, more preferably from 70 ° C to 120 ° C. By "melting point" is meant the temperature at which the material to be heated slowly in, for example, a capillary tube becomes a transparent liquid. A coating of any desired thickness can be applied in accordance with the present invention. For most purposes, the coating forms from 1% to 10%, preferably from 1.5% to 5%, of the weight of the tablet. The tablet coatings of the present invention are very hard and provide extra resistance to the tablet, and allow easy release of the pectate lyase.

In a preferred embodiment of the present invention, the fracture of the coating in the wash is improved by adding a disintegrant to the coating. This disintegrant will swell once it is in contact with water and will break the coating into small pieces. This will improve the dissolution of the coating in the wash solution. The disintegrant is suspended in the molten coating at a level of up to 30%, preferably between 5% and 20%, more preferably between 5 and 10% by weight. Possible disintegrants are described in the Pharmaceutical Excipients Manual (1986). Examples of suitable disintegrants include starch: natural, modified or pregelatinized starch, sodium starch gluconate; gum: gum agar, guar gum, locust bean gum, karaya gum, pectin gum, gum tragacanth; croscarmilose-sodium, crospovidone, cellulose, carboxymethylcellulose, algenic acid and its salts including sodium alginate, silicon dioxide, clay, polyvinylpyrrolidone, soy polysaccharides, ion exchange resins, and mixtures thereof.

Resistance to stress For the purpose of measuring the tensile strength of a layer, the layer can be considered as a tablet itself. Depending on the composition of the starting material, and the shape of the tablets, the compaction force used can be adjusted so as not to affect the tensile strength, and the disintegration time in the washing machine. This method can be used to prepare homogeneous or stratified tablets of any size or shape. For a cylindrical tablet, the tensile strength corresponds to the diametral fracture stress (DFS) which is a way of expressing the strength of a tablet, and is determined by the following equation: Resistance to tension = 2F pDt where F is the maximum force (Newton) to cause voltage failure (fracture) measured by a tablet hardness tester VK 200 supplied by Van Kell Industries, Inc. D is the diameter of the tablet or layer, and t the thickness of the tablet or layer. For a non-round tablet, pD can be simply replaced by the perimeter of the tablet (see Method Pharmaceutical Dosage Forms: Tablets Volume 2 page 213 to 217). A tablet that has a lower diametral fracture effort than kPa is considered fragile and is likely to result in some tablets being delivered broken to the consumer. A diametral fracture stress of at least 25 kPa is preferred. This applies similarly to non-cylindrical tablets, to define the tensile strength, where the normal cross section at the height of the tablet is not round, and where the force is applied along a direction perpendicular to the direction of the height of the tablet and normal next to the tablet, the side being perpendicular to the non-round cross section.

Effervescent In another preferred embodiment of the present invention, the tablets further comprise an effervescent. "Effervescence" as defined herein means the formation of gas bubbles from a liquid, as a result of a chemical reaction between a soluble acid source and an alkali metal carbonate, to produce gaseous carbon dioxide, ie, C6H807 + 3NaHC03? Na3C6H507 + 3C02 t + 3H20 Additional examples of acid and carbonate sources and other effervescent systems can be found in: (Pharmaceutical Dosage Forms: Tablets Volume 1 page 287 to 291). An effervescent can be added to the tablet mix in addition to the detergent ingredients. The addition of this effervescent to the detergent tablet improves the disintegration time of the tablet. The amount will preferably be between 5 and 20% and more preferably between 10 and 20% by weight of the tablet. Preferably the effervescent should be added as an agglomerate of different particles or as a compact product, and not as separate particles. Due to the gas created by the effervescence in the tablet, the tablet can have a D.F.S. higher and still have the same disintegration time as a tablet without effervescence. When the D.F.S. of the tablet with effervescence remains the same as a tablet without effervescence, the disintegration of the tablet with effervescence will be faster. An additional dissolution aid could be provided using compounds such as sodium acetate or urea. A list of suitable dissolving aids can be found in Pharmaceutical Dosage Forms: Tablets, Volume 1, second edition, Edited by H.A. Lieberman et al, ISBN 0-8247-8044-2.

Other components The surfactant is comprised in the tablet according to the present invention. Suitable surfactants for the tablet herein are described hereinbefore.

Also suitable for the present tablet are detergency builders, bleaching agents, enzymes and enzymes such as those described herein.

Non-quenching detergent improvers Non-gelling detergent improvers can be integrated into the particles that make up the tablet to further facilitate dissolution. If non-gelling builders are used, suitable non-gelling builders include synthetic organic polymers such as polyethylene glycols, polyvinyl pyrrolidones, polyacrylates and water-soluble acrylate copolymers. The Pharmaceutical Excipients Second Edition manual has the following classification of detergency builders: acacia, alginic acid, carbomer, carboxymethylcellulose-sodium, dextrin, ethylcellulose, gelatin, guar gum, hydrogenated vegetable oil type I, hydroxyethylcellulose, hydroxypropylmethylcellulose, liquid glucose, magnesium-aluminum silicate, maltodextrin, methylcellulose, polymethacrylates, povidone, sodium alginate, starch and zein. Further preferred builders also have an active cleaning function in the laundry of clothes such as cationic polymers, ie, ethoxylated hexamethylenediamine quaternary compounds, bishexamethylene triamias, or others such as pentaamines, ethoxylated polyethylene amines, maleic acrylic polymers. The non-gelling builder materials are preferably sprayed and therefore have an appropriate melting point temperature below 90 ° C, preferably below 70 ° C and more preferably below 50 ° C so as not to damage or degrade the other active ingredients in the matrix. More non-aqueous liquid builders (that is, not in aqueous solution) are preferred which can be sprayed in molten form. However, they may also be solid builders built into the matrix by dry addition but having binding properties within the tablet.

Non-gelling builder materials are preferably used in an amount within the range of 0.1 to 15% of the composition, more preferably below 5% and especially if it is an active material that is not for laundry underneath of 2% by weight of the tablet. It is preferred to avoid gelling detergent builders, such as nonionic surfactants, in their liquid form or molten form. Nonionic surfactants and other gelling builders are not excluded from the compositions, but it is preferred that they be processed into detergent tablets as components of particulate materials, and not as liquids.

Pectate lyase enzyme An essential element of the detergent tablets of the present invention is a pectate lyase enzyme. Pectate lyase is classified within the classification of enzymes provided by the enzyme nomenclature (1992) as EC 4.2.2.2. Said enzyme is known to divide the α-1,4 bond, galacturonic acid glucoside found in the pectin substances, creating a double bond between C4 and C5 and is substantially free of other pectin degrading activities, ie, having less than 25%, preferably less than 15%, more preferably less than 5% by weight of the enzyme compound of other pectin-degrading enzyme activities. Pectate lyases have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, Streptomyces, Penicillium, Baceríodes, Thermomonospora, Fusarium, and Aspergillus It has also been described of the cloning of Bacillus subtilis (Nasser et al. (1993) FEBS 335: 319-326) and Bacillus sp. YA- 14 (Kim et al. (1994) Biosci. Biotech Biochem. 58: 947-949) of a pectate lyase. The purification of pectate lyases with a maximum activity on the pH scale 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 (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) has been reported. WO 98/45393 discloses detergent compositions containing protopectinase with remarkable detergency against dirt with sludge. Pectate lyases furthermore suitable for use in the present invention are protopectinases which have an optimum pH reaction of 7.0 or greater when the polygalacturonic acid is used as a substrate such as that described in W098 / 45393, and the lyase of pectic acid having the amino acid sequence SEQ No. 1 of EP 870 843 or having said amino acid sequence, with one or more amino acids deleted, added or substituted. Preferred are the pectate lyase enzymes described in co-pending international application PCT / DK98 / 00515, first issued in Denmark on November 24, 1997: - A pectate lyase comprises a first amino acid sequence consisting of seven (7) residues amino acids that have the following sequence: Asn Leu Asn Ser Arg Val Pro (NLNSRVP); - A pectate lyase that is: i) a polypeptide produced by Bacillus agaradhaerens, NCIMB 40482 or DSM 8721, or by a Bacillus species having a sequence homology of 16S rDNA to Bacillus agaradhaerens, DSM 8721, of at least 99%, or ii) a polypeptide comprising an amino acid sequence as shown in positions 27 -359 of SEQ ID NO: 2 of PCT / DK98 / 00515, or iii) an analogue of the polypeptide defined in i) or ii) which is at least 45% homologous with said polypeptide, or iv) is derived from said polypeptide by substitution, deletion or addition of one or more amino acids, provided that the arginine in position 240, and optionally also the arginine in position 245, is retained and the polypeptide derivative is at least 42% homologous with said polypeptide, or v) is immunologically reactive with a polyclonal antibody exposed to said polypeptide in purified form; A pectate lyase that is: i) a polypeptide produced by Bacillus licheniformis, ATCC, 14580, or by a Bacillus species having a sequence homology of 16S rDNA to Bacillus licheniformis, ATCC, 14580, of at least 99%, or ) a polypeptide comprising an amino acid sequence as shown in positions 28-341 of SEQ ID NO: 4 of PCT / DK98 / 00515, or iii) an analogue of the polypeptide defined in i) or ii) which is at least 45% homologue with said polypeptide, or v) is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, provided that the arginine at position 233, and optionally also the arginine at position 238, is retained and the polypeptide derivative is at least 42% homologous with said polypeptide, ov) is immunologically reactive with a polyclonal antibody exposed to said polypeptide in purified form; A pectate lyase that is: i) a polypeptide produced by a Bacillus species having the 16S rDNA sequence of SEQ ID NO: 14 or by a Bacillus species having a 16S rDNA sequence homology to SEQ ID NO: 14 greater than 97.3%; or ii) a polypeptide comprising an amino acid sequence as shown in positions 181-509 of SEQ ID NO: 6, or iii) an analog of the polypeptide defined in i) that is at least 50% homologous to said polypeptide, or iv) is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, provided that the arginine in position 390, and optionally also the arginine in position 395, is conserved and the derived polypeptide is at least 44% homologous with said polypeptide, or v) is immunologically reactive with a polyclonal antibody exposed to said polypeptide in purified form, - A pectate lyase that is: i) a polypeptide produced by the Bacillus halodurans species, or ii) a polypeptide comprising an amino acid sequence as shown in positions 42-348 of SEQ ID NO: 8 of PCT / DK98 / 00515, or iii) an analogue of the polypeptide defined in i) or ii) which is at least 45% homologous with said polypeptide, or iv) is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, provided that the arginine in position 240, and optionally also the arginine in position 245, is conserved and the polypeptide derivative is at least 40% homologous with said polypeptide, or v) is immunologically reactive with an anti-polyclonal antibody exposed to and said polypeptide in purified form, - A pectate lyase that is: i) a polypeptide produced by a Bacillus species having the 16S rDNA sequence of SEQ ID NO: 13 PCT / DK98 / 00515 or by a Bacillus species having a 16S rDNA sequence homology to SEQ ID NO: 13 of PCT / DK98 / 00515 greater than 98.1%; or ii) a polypeptide comprising an amino acid sequence as shown in positions 25-335 of SEQ ID NO: 10 of PCT / DK98 / 00515, or iii) an analog of the polypeptide defined in i) or that is at least 45% homologue with said polypeptide, or iv) is derived from said polypeptide by substitution, deletion or addition of one or more amino acids, provided that the arginine at position 227, and optionally also the arginine at position 232, is retained and the polypeptide derived at least 41% homologous with said polypeptide, or v) is immunologically reactive with a polyclonal antibody exposed to said polypeptide in purified form. Similarly preferred is the pectate lyase enzyme described in co-pending international application PCT / DK98 / 00514, first issued in Denmark on November 24, 1997, and which is: i) a polypeptide produced by Bacillus licheniformis, ATCC 14580, or ii) a polypeptide comprising an amino acid sequence as shown in positions 28-221 of SEQ ID NO: 4 of PCT / DK98 / 00514, or iii) an analogue of the polypeptide defined in i) or ii) which is at least 60% homologous with said polypeptide, or iv) is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, provided that the plants in positions 133 and 155 and the arginine at position 158 is retained and the polypeptide derivative is at least 66% homologous with positions 60-158 of SEQ ID NO: 4 of PCT / DK98 / 00514, or v) is immunologically reactive with a polyclonal antibody exposed to said polypeptide in purified form. The most preferred pectate lyases for the purpose of the present invention are those that have optimal activity at pH > 7.0 and are derived from Streptomyces fradiae, Streptomyces nitrosporeus, Erwinia carotovora, Bacillus spheroides, Thermomonospora fusca, Pseudomonas solanacearum, Bacteroides thetaiotaomicron, Fusarium solani, Xanthomonas campestris, Bacillus agaradhaerens, and / or Bacillus licheniformis. The most preferred pectate lyase for the purpose of the present invention is the pectate lyase of Bacillus agaradhaerens, NCIMB 40482 or DSM 8721. The pectate lyase is incorporated into the tablet of the invention preferably at a level of 0.0001% to 2%, more preferably from 0.0005% to 0.1%, more preferably from 0.001% to 0.02%, of the pure enzyme by weight of the composition. Preferably, more than 70%, more preferably more than 85%, more preferably more than 95% of the total amount of the pectate lyase enzyme will be understood in section 2 of the detergent tablet of the present invention. The pectate lyase of the invention, together with the enzyme core comprising the catalytically active domain, can also contain a cellulose binding domain (CBD), the cellulose binding domain and the enzyme core (the catalytically active domain) of the enzyme being operably linked. The cellulose binding domain (CBD) can exist as an integral part of the encoded enzyme, or a CBD from another source can be introduced into the enzyme in this way by creating an enzyme hybrid. In this context the term "cellulose binding domain" is understood as defined in Peter Tomme et al. "Cellulose-Binding Domains: Classification and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Míchael H. Penner (Eds.), ACS Symposium Series, No. 618, 1996. This definition classifies more 120 domains of cellulose binding in 10 families (lX), and demonstrates that CBDs are found in several enzymes such as celluloses, xylanases, mannanases, arabinofuranosidases, acetylesterases and citinases. CBD has also been found in algae, for example red alga Porphyra purpurea as a non-hydrolytic polysaccharide binding protein, see Tomme et al., Op.cit. However, most CBDs of celluloses and xylanases, CBDs are found in the N and C terminals of proteins or are internal. Enzyme hybrids are known in the art, see for example, WO 90/00609 and WO 95/16782, and can be prepared by transforming into host cells a DNA construct comprising at least one DNA fragment encoding the domain ligand binding to bound cellulose, with or without a linker, to a DNA sequence encoding the enzyme pectate lyase and growing the host cell to express the fused gene. The enzyme hybrids can be described by the following formula: CBD-MR-X wherein CBD is the N-terminal or the C-terminal region of an amino acid sequence corresponding to at least the cellulose binding domain; MR is the middle region (the linker), and may be a bond, a small linking group preferably about 2 to about 100 carbon atoms, more preferably 2 to 40 carbon atoms; or is preferably from about 2 to about 100 amino acids, more preferably from 2 to 40 amino acids; and X is an N-terminal or C-terminal region of the pectate lyase of the invention. The aforementioned enzymes can be of any suitable origin, such as of vegetable, animal, bacterial, fungal and yeast origin. The origin can also be mesophilic or extremophilic (psychrophilic, psychrotropic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). The purified or non-purified forms of these enzymes can be used. At present, it is common to modify the wild-type enzymes by means of protein / genetic engineering techniques to optimize their efficacy in terms of their performance in the detergent compositions of the invention. For example, the variants can be designed in such a way that the compatibility of the enzyme with ingredients commonly found in said compositions is increased. Alternatively, the variant can be designed so that the optimum pH, bleach or chelating stability, catalytic activity and the like, of the enzyme variant is characterized by being adapted to the particular cleaning application. In particular, attention should be paid to amino acids sensitive to oxidation in the case of bleaching stability in surface charges for compatibility of the surfactant. The isoelectric point of said enzymes can be modified by the replacement of some charged amino acids, for example, an increase in the isoelectric point can help improve compatibility with anionic surfactants. The stability of the enzymes can also be increased by the creation, for example, of additional salt bridges and reinforced metal binding sites to increase the chelating stability. Preferably, the detergent tablets of the present invention will comprise a pH regulating agent together with the enzyme pectate lyase. Said pH regulating agents may be required to generate the optimum pH for pectate lyase activity. Any standard pH regulating agent can be used. Those having an optimum pH-regulating capacity at pH where pectate lyase shows optimal activity are preferred. Examples include NaH2P04, NaHCO3, Na2CO3 and citric acid, tris (hydroxymethyl) amnomethane (Trizma (TM) from Sigma), triethanolamine, NN, bis (2-Hydroxyethyl) glycine, N-tris (Hydroxymethyl) methyl-3 acid. -aminopropane-sulfonic acid and / or mixtures thereof. Said pH regulating agent is typically present at 5% or less by weight of the fast dissolving phase containing pectate lyase.

Washing Method The compositions of the invention can be used in essentially any washing or cleaning method, including soaking methods, pretreatment methods and methods with rinsing steps for which a separate rinsing aid composition can be added. The process of the invention is conveniently carried out in the course of the cleaning process. The cleaning method is preferably carried out from 5 ° C to 95 ° C, especially between ° C and 60 ° C. The pH of the treatment solution is preferably from 7 to 12. A preferred machine dishwashing method comprises treating soiled articles selected from earthenware, vessels, silverware, metalware, cutlery and mixtures thereof, with liquid acuse which has a dissolved or dispersed effective amount of the compositions described herein. By an effective amount is meant from 8 g to 60 g of the product dissolved or dispersed in a solution for volume washing of 3 to 10 liters, as are the typical product doses and the volumes of washing solution commonly employed in methods for washing tableware in conventional machines. Preferably the detergent tablets are from 15 g to 40 g by weight, more preferably from 20 g to 35 g by weight. The methods for machine laundry in the present typically comprise treating soiled articles with an aqueous wash solution in a washing machine having an effective amount dissolved or dispersed therein of the compositions described herein. By an effective amount is meant 20 g to 300 g of the dissolved or dispersed product in a volume wash solution of 5 to 65 liters, as are typical product doses and volumes of wash solution commonly employed in conventional machine laundry methods .

EXAMPLES The following examples are intended to exemplify the compositions of the present invention, but are not necessarily intended to limit or otherwise define the scope of the invention.

EXAMPLES OF WASHING OF DISHES In Examples I-IV, the abbreviated component identifications in detergent compositions have the following meanings, and all levels are cited as parts by weight: STPP: Sodium tripolyphosphate: 50% hexahydrate, 6% phase I and 44% phase II Bicarbonate: Sodium bicarbonate. Citric acid: Anhydrous citric acid Carbonate: Anhydrous sodium carbonate Silicate: Amorphous sodium silicate (Si? 2 ratio: Na2? = 2.0) SKS-6: Crystalline layered silicate of the formula d-Na2Si2? 5 PB1: Anhydrous sodium perborate monohydrate Nonionic: C13-C? S ethoxylated / propoxylated fatty acid alcohol mixed with an average degree of ethoxylation of 3.8 and an average propoxylation grade of 4.5, sold under the trademark Plurafac by BASF. TAED: Tetra-acetylethylenediamine HEDP: 1-hydroxy-1,1-bisphosphonic acid ethane PAAC: Cobalt acetate pentaamine salt (lll) Paraffin: Paraffin oil sold under the trademark Winog 70 byWintershall. Protease Proteolytic enzyme sold under the tradename Savinase, Alcalase, Durazym by Novo Nordisk A / S, Maxacal, Maxapem sold by Gist-Brocades and proteases described in patents WO / 91/06637 and / or WO95 / 10591 and / or EP 251 446 Amylase: Amylolytic enzyme sold under the trade name Purafact Ox Am® described in WO 94/18314, WO 96/05295 sold by Genencor; Termamyl®, Fungamyl®, and Duramyl®, all available from Novo Nordisk A / S and those described in WO 95/26397 (sold under the trade name Natalase by Novo Nordisk) Pectate lyase: Pectate lyase from Bacillus agaradhaerens, NCIMB 40482 or DSM 8721 BTA: Benzotriazole Sulfate: Anhydrous sodium sulfate PEG 300: Polyethylene glycol of molecular weight of about 3000 available from Hoechst. PEG 6000: Polyethylene glycol of molecular weight of approximately 6000 available from Hoechst. The following examples illustrate detergent tablets of the present invention suitable for use in a dishwashing machine.

III IV V VI Phase 1 STPP 9.6 9.6 10.4 9.6 9.6 11.5 Silicate 0.5 0.7 1.6 1.0 1.0 2.4 SKS-6 1.5 1.5 - 2.3 2.25 - Carbonate 2.3 2.7 3.5 3.6 4.1 5.2 HEDP 0.2 0.2 0.2 0.3 0.3 0.3 PB1 2.4 2.4 2.4 3.7 3.7 3.7 PAAC 0.002 0.002 0.002 0.003 0.004 0.004 Amylase 0.1 0.1 0.11 0.2 0.2 0.2 Protease 0.06 0.06 0.06 0.09 0.09 0.09 Non-ionic 0.4 0.8 0.8 1.2 1.2 1.2 PEG 6000 0.4 0.26 0.26 0.4 0.4 0.4 BTA 0.04 0.04 0.04 - 0.06 0.06 Paraffin 0.1 0.10 0.10 0.1 0.1 0.15 Perfume 0.02 0.02 0.02 0.01 0.01 0.01 Sulfate - - - 0.5 0.05 2.8 Total 17.7 g 18.5 g 19.6 g 23.0 g 23.0 g 23.0 g Phase 2 Pectate lyase 0.005 0.50 0.001 0.002 0.02 0.001 Amylase 0.003 0.003 0.002 0.003 0.003 0.002 Protease 0.01 0.009 0.01 0.01 0.009 0.01 Citric acid 0.3 - 0.3 0.3 - 0.30 Sulfamic acid - 0.3 - - 0.3 - Bicarbonate 1.1 0.4 0.4 1.1 0.4 0.4 Carbonate - 0.5 - - 0.5 - Silicate - - 0.6 - - 0.6 CaCl2 - 0.07 - - 0.07 - PEG 3000 0.06 0.06 0.06 0.06 0.06 0.06 Total 2.05 g 2.50 g 2.1 g 2.20 g 2.02 g 2.15 g The tablet compositions are prepared as follows. The composition of the active detergent ingredients of phase 1 is prepared by mixing the liquid and granular components and then passed to the die of a rotating press. The press includes an appropriately modified punch to form the mold. The cross section of the die is approximately 30 x 38 mm. The composition is then subjected to a compression force of 940 Kg / cm 2 and the punch is raised to expose the first phase of the tablet containing the mold on its upper surface. The detergent active ingredient composition of phase 2 is prepared in a similar manner and passed to the die. The particulate active ingredient composition is then subjected to a compression force of 170 Kg / cm 2, the punch is raised and the multi-phase tablet is ejected from the press. The resulting tablets are dissolved or disintegrated in a washing machine as described above within a period of 12 minutes, phase 2 of the tablets being dissolved in a period of 5 minutes. The tablets provide improved strength, especially in prolonged storage, together with excellent dissolution characteristics.

EXAMPLES VII A XI The following illustrates examples of tablets for automatic dishwashing in accordance with the present invention (g of the raw material and enzymes are expressed in pure enzyme): VIII VIII IX X XI Body of the STPP table 10.3 9.5 10.6 10.6 10.1 Carbonate 5.2 5.2 2.8 3.5 3.5 Silicate 2.4 1.6 2.9 1.6 1.1 SKS-6 2.2 2.2 - 1.5 1.5 HEDP 0.3 0.3 0.2 0.2 0.2 Protease 0.003 0.003 0.002 0.002 0.002 Amylase 0.001 0.001 0.001 0.001 0.001 Perborate 3.7 3.7 2.8 2.4 2.4 EO / PO nonionic of C13-15 1.2 0.9 0.4 0.8 0.6 PEG4000 0.4 - - 0.3 - PEG6000 - 0.4 - - 0.3 BTA 0.09 0.09 0.06 0.06 0.06 Paraffin 0.1 0.1 0.1 0.1 0.1 Perfume - - 0.02 0.02 0.02 Total body tablet 26.4 24.5 20.1 21.3 20.1 Depression Protease 0.01 0.01 0.01 0.01 0.01 Amylase 0.003 0.003 0.004 0.003 0.003 Pectate lyase 0.2 0.05 0.2 0.3 0.3 Citrus 0.2 0.2 0.6 0.2 0.2 Bicarbonate 0.6 0.6 0.6 0.6 0.6 Triacetin - - 1.2 - - PEG400 0.02 0.02 - 0.02 0.02 PEG6000 0.08 0.08 - 0.08 0.08 PEG6000 - - 1.2 - - CaCI2 _ _ 0.1 _ _ Total depression 1.5 1.5 3.5 1.5 1.5 Total Tablet 27.9 26.0 23.6 22.8 21.6 The following illustrates examples of detergent tablets of the present invention suitable for use in a laundry machine. i) The detergent powder of compositions I-IV (see the tables below) was prepared as follows: all the particulate materials of the base composition were mixed in a mixing drum or sprinkling drum to form a mixture of homogeneous particles. During the mixing, the sprinkling of the builder system was carried out. After this stage, the matrix was separated into two samples. The sticky hydrotrope from DIBS was added to only one of the samples and subsequently processed independently in a Loedige KM 600®. The layer with DIBS was used for a harder lower layer and the non-DIBS layer was used for a smoother upper layer of a double-layer tablet. ii) Using a Bonals® rotary press, both matrices were filled in two separate force feeding flasks. The matrix with DIBS was filled first in a row in the stations, of turret, followed by the second matrix (without the DIBS matrix). Both layers were compressed in the pre-compression and compression stations to form a double layer tablet with a hard bottom layer. iii) In this particular example, the tablets have a rectangular cross section of 62.5 by 38.5 millimeters, a height of 20.5 millimeters and a weight of 48 grams. The height of the lower layer corresponding to 25% of the total weight of the tablet. If a round tablet is made in the lower layer matrix with the same density as with the rectangular tablet (983 g / l), the tensile strength of the layer is 7.8 kPa.

Using the same experiment (for a density of 991 g / l), the top layer of the tablet has an equivalent tensile strength of 5.1 kPa.

The elasticity measurements gave values of 1.8 J / kN for the upper layer and 3.3 J / kN for the lower layer. Below are examples for the composition of base particulate material for making laundry detergent tablets according to the invention, wherein a harder layer can be compressed in place of a softer layer, or in which different compositions can be used or adapt for each layer. Enzyme levels are expressed by pure enzymes by weight of the total composition and unless specified, the detergent ingredients are expressed by weight of the total compositions.

I II lll LV Anionic agglomerates 1 21.0 21.0 8.6 31.5 Anionic agglomerates 2 12.6 12.6 22.0 - Nonionic agglomerates - - 9.1 - Cationic agglomerates 5.4 5.4 4.6 5.0 Stratified silicate 10.8 10.8 9.7 11.5 Sodium percarbonate 14.2 14.2 12.2 16.2 Agglomerates of activator of 5.5 5.5 6.1 4.7 bleaching Sodium carbonate 13.8 12.6 7.3 3.3 Baking soda - - - 2.0 Sodium sulfate - - - 2.4 EDDS particle / sulfate 0.5 0.5 0.5 0.5 Tetrasodic acid salt 0.7 0.7 0.6 0.8 Hydroxyetho-diphosphonic 0.3 0.3 0.3 0.3 release polymer Drying agent 0.2 0.2 0.2 0.1 Phthalocyanine encapsulation 0.02 0.02 0.03 0.02 sulfonated zinc Soap powder 1.4 1.4 1.2 _ Foam suppressor 1.9 1.9 2.8 2.1 Citric acid 7.1 7.1 5.5 2.0 Pectate lyase 0.008 0.008 0.001 0.01 Protease 0.03 0.03 0.04 0.03 Lipasa 0.003 0.003 0.004 0.0003 Cellulase 0.0001 0.0001 0.0001 0.0001 Amylase 0.009 0.09 0.009 0.005 Sprinkler system 1.3 2.5 _ -cleaning detergent 1 3.05 sprinkler system detergent builder 2 Polymer particle - 3.0 Spray system non-5.2 ionic Zeolite - 6.2 Perfume spray 0.5 0.3 Perfume encapsulates - 0.2 Sodium Isoalkylbenzenesulfonate TOTAL 100.00 100.00 100.00 100.00 Anionic agglomerates 1 comprise 40% anionic surfactant, 27% zeolite and 33% carbonate. Anionic agglomerates 2 comprise 40% anionic surfactant, 28% zeolite and 32% carbonate. Nonionic agglomerate comprises 26% non-surface active agent Ionic, 6% Lutensit K-HD 96, 40% anhydrous sodium acetate, 20% carbonate and 8% zeolite. Cationic agglomerates comprise 20% cationic surfactant, 56% zeolite and 24% sulfate. Stratified silicate comprises 95% SKS 6 and 5% silicate. Agglomerates bleach activators comprise 81% TAED, 17% acrylic / maleic copolymer (acid form) and 2% water. The salt / sodium sulfate particle of ethylene diamine N, N-disuccinic acid comprises 58% sodium salt of ethylene diamine N, N-disuccinic acid, 23% sulfate and 19% water. Encapsulated sulfonated zinc phthalocyanine 10% active. Foam suppressor comprises 11.5% silicone oil (Dow Corning); 59% zeolite and 29.5% water. Sprinkler system 1 builder comprises 50% Lutensit K-HD 96 and 50% PEG (polyethylene glycol). Sprinkler builder system 2 comprises 0.5 parts of Lutensit K-HD 96 and 2.5 parts of PEG.

Encapsulates of perfume comprise 50% perfume and 50% starch. Polymer particle comprises 36%, 54% zeolite and 10% water. Non-ionic sprinkler system comprises 67% of C12-C15 AE5 (alcohol with an average of 5 ethoxy groups per molecule), 24% N-methyl glucosamide and 9% water. The protease is selected from the proteolytic enzyme sold under the tradename Savinase, Alcalase, Durazym by Novo Nordisk AS, Maxacal, Maxapem sold by Gist-Brocades and proteases described in patents WO01 / 06637 and / or WO95 / 10591 and / or EP 251 446 and / or mixtures thereof. The amylase is selected from: the amylolytic enzyme sold under the trade name Purafact Ox Am® described in WO 94/18314, WO96 / 05295 sold by Genencor; Termamyl®, Fungamyl® and Duramyl®, available from Novo Nordisk A / S and those described in W095 / 26397 (sold under the trade name Natalase by Novo Nordisk A S) and / or mixtures thereof. The lipase is selected from the lipolytic enzyme sold under the tradename Lipolase, Lipolase Ultra by Novo Nordisk A / S and Lipomax by Gist-Brocades, and / or mixtures thereof. The pectate lyase of Bacillus agaradhaerens, NCIMB 40482 or DSM 8721.

The cellulase is selected from: the cellulitic enzyme sold under the trade name Carezyme, Celluzyme and / or Endolase by Novo Nordisk A / S; and / or mixtures thereof.

Claims (10)

NOVELTY OF THE INVENTION CLAIMS

1. - A tablet comprising a section 1 and a section 2, wherein section 2 comprises a higher level of pectate lyase than section 1.

2. The tablet according to claim 1, further characterized in that the resistance to the The tension of section 1 is greater, preferably at least 2% greater, more preferably 5%, still more preferably 10% and more preferably 30%, than the tensile strength of section 2.

3.- The tablet in accordance with claims 1-2, further characterized in that section 2 has an exposed surface larger than section 1.

4. The tablet according to claims 1-3, further characterized in that section 2 has an exposed surface equal to Exposed surface of the tablet.

5. The tablet according to claims 1-4, further characterized in that the section 2 is applied by a coating process.

6. - A detergent tablet according to any of the preceding claims, further characterized in that section 1 is a slow dissolving section and section 2 is a rapid dissolving section.

7.- A detergent tablet in accordance with any of 5 the preceding claims, further characterized in that said pectate lyase is comprised at a level of 0.0001% to 2%, more preferably of

0. 0005% to 0.1%, more preferably from 0.001% to 0.02% pure enzyme in ** weight of the tablet.

8.- A detergent tablet in accordance with any of the 10 above claims, further characterized in that more than 70%, preferably more than 85%, more preferably more than 95% of the total amount of the enzyme pectate lyase, is comprised in section 2 of the detergent tablet.

9. A tablet detergent according to any of the preceding claims, further characterized in that said section 2 comprises a pH regulating material.

10. A method for cleaning a cloth or a dish with a tablet according to any of the preceding claims.