MXPA99001620A - Detergent compositions comprising antibody controlled proteolytic activity - Google Patents

Abstract

The present invention relates to laundry detergent compositions comprising a protease and a protease-directed antibody in order to provide excellent cleaning performance and fabric care performance.

Description

DETERGENT COMPOSITIONS THAT INCLUDE PROTEOLIC ACTIVITY CONTROLLED BY ANTIBODIES FIELD OF THE INVENTION * «_ The present invention relates to laundry detergent compositions comprising a protease and an antibody directed against protease to provide excellent cleaning performance and fabric care performance. BACKGROUND OF THE INVENTION An important part of the system that protects vertebrates against infections by bacteria or viruses is the humoral immune system. The specialized cells present in the bone marrow, lymphoid tissues and the blood produce immunoglobulins (antibodies) that appear in response to the introduction of a micro- or macromolecule foreign to said body and join the structure foreign to the body, initiating so its destruction. This molecule, which is foreign to the body, is called an antigen. The antibody is directed against the antigenic determinant or aptene of the antigen, that is, an amino acid frequency, parts of oligosaccharides, polysaccharides, lipopolysaccharides, glycoproteins, lipopropteins, acids lipoteicoinics. The specific antibodies generated in this way can be combined with the antigen that produces their formation to form an antigen-antibody complex. The antibody molecules have binding sites that are very specific and complementary to the structural characteristics of the "- * 5 antigen inducing its formation Several applications of such recognition of highly specific antigen-antibody and binding have been discovered, such as the recognition agent, the binding agent or carrier agent in various domains such as the analytical chemistry, therapeutic treatment and health and aesthetic care. EP 479 600, EP 453 097 and EP 450 800 relate to the use of antibodies or fragments thereof to deliver the active ingredients to a target site. He EP 481 701 discloses treatment compositions for * the topical application containing microcapsules comprising a beneficial agent in a target location, the microcapsules having an antibody or specific antibody fragment in the target location or a lectin. WO92 / 04380 describes a newly formed human antibody or reshaped human antibody fragments having a specific character for the human polymorphic epithelial mucosa to be used in the treatment or diagnosis of cancer. The use of polypeptides specific for the Epstein-Barr virus for the production of antibodies and the diagnosis and treatment of said disease are described in WO94 / 06470. Oral compositions comprising antibodies as anti-caries or periodontal diseases are described extensively in documents O95 / 01155, • * s. 5 O95 / 00110, O95 / 10612, EP 140 498, GB 140 498, GB 2 151 923, GB 2 176 400, GB 2 167 299, DE 4324859, US 5 401 723 and EP 280 576. EP 673 683 and EP 542 309 describe cosmetic compositions for hair containing a antibody to the hair, or hair extract, obtained from the yolk of the egg or poultry immunized with the hair or hair extract of a polymer emulsion to provide reduced damage to the hair, softness, moisture sensation and smoothness; said composition is absorbed only in one specific part of the hair. * The compositions containing antagonists (tyrphostins or antibodies) against epidermal growth and transformation factors, suitable for use in the treatment of acne are described in W095 / 24896.

The use of antibodies in the context of detergency has been suggested in general in Unilever Researchprijs "Molecule zoekt parther" 1992, where modified antibodies directed to specific spots are proposed to be used in the bleaching process. The production of antibodies by hyperimmunization of mammals, such as a cow, with a vaccine derived from the E. coli bacterium is described in EP 102 831. EP 400 569 describes a method for preparing the vaccine composition for dental caries in nasal drops that comprise an antigen • a 5 produced by the integration of a protein antigen, expressed in the chromosomal gel of a GS-5 strain of Streptococcus mutant. W094 / 25591 describes the production of antibodies or functionalized fragments thereof derived from an immunoglobulin heavy chain of camelidae. Currently, detergent compositions include a complex combination of active ingredients that meet certain specific needs: a surfactant system, detergent enzymes, bleaching agents, a detergency builder system, foam suppressors, dirt suspending agents, dirt release agents, optical brighteners, softening agents, dispersants, dye transfer compound, abrasives, bactericides, perfumes and their development general has been improved over the years. In particular, current laundry detergent formulations generally include detergent enzymes, and more specifically proteases. However, excessive substrate exposure to The proteolytic activity and / or transfer of the proteolytic activity to the main post-wash portion of the wash cycle, such as the rinse, spin and / or drying steps, can result in undesirable effects. It is well known that proteolytic detergent enzymes can reduce, under certain circumstances, the tensile strength of the wool constituents of the fabrics. However, it should be noted that the loss of tensile strength of the fabric is also an inevitable result of the mechanical action due to wear / wear, and may also be the result of damage caused by a bleaching component in the washing process , especially if the fabric is contaminated with metal compounds. It has now surprisingly been found that the application of antibodies raised against the proteolytic enzyme prevents the occurrence of inconvenient residual proteolytic activity. The proteolytic activity can be totally controlled during the cleaning process, so that the negative effects due to excessive substrate exposure to the proteolytic enzyme can now be avoided. Therefore, an object of the present invention is to provide a laundry detergent composition containing protease that provides excellent cleaning benefits such as stain and / or dirt removal benefits, as well as cleaning and fabric care. The above need has been covered by specific laundry detergent compositions comprising a protease and an antibody directed against said proteolytic enzyme.

BRIEF DESCRIPTION OF THE INVENTION The present invention relates to laundry detergent compositions comprising a protease enzyme and an antibody produced against the proteolytic enzyme to provide excellent cleaning performance and fabric care performance.

DETAILED DESCRIPTION OF THE INVENTION Antibody An essential element of the detergent compositions of the present invention is an antibody. J Immunoglobulins are classified into 5 classes, respectively: IgA, IgD and IgE. Preferred types of immunoglobulin are IgG and IgA. The secretory slgA that has been discovered in the secreted fluids of the human body such as milk, saliva, respiratory and intestinal fluids, which are specially designed to survive in said secretions, have promoted binding characteristics and are resistant to proteolytic hydrolysis. The antibody that can be monoclonal or polyclonal or an antibody fragment can be generated by techniques conventional in the art, for example by using recombinant DNA techniques that allow the production of antibody variants with new properties: reduced immunogenicity, affinity driven, altered size, etc. You can also use the specific link. The monoclonal antibody is preferred for the purpose of the present inventionvery preferred is a fragment thereof. Such fragments can be generated similarly by conventional techniques such as enzymatic digestion by papain or pepsin, using recombinant DNA techniques. Antibody fragments can also be generated by conventional recombinant DNA techniques. The antibodies and antibody fragments can be humanized, as described in Meded.- Fac. Landbouwkd. Toegepast Biol. Wet. (Univ. Gent) (1995), 60 (4a, Forum for Applied Biotechnology, 1995, Part 1), 2057-63. Heavy and light chains are in fact made up of J constant and variable domains. The organisms that produce immunoglobulin in their natural state, the constant domains are very important for a number of fusions, but for several applications in industrial processes and products, their variable domains are sufficient. Consequently, many methods have been described to produce antibody fragments. The antibody fragments that are used can be a Fab, an Fv, a scFv or any other fragment that has similar link properties. The preferred fruits for antibody fragments are through recombinant DNA technology, so that the fragment is expressed by a genetically transformed organism. Antibodies and antibody fragments produced by recombinant DNA technology need not be identical to the antibody fragment produced in vertebrates, yet have the same binding properties evaluated by their Km, Ki and Kcat. For example they may include amino acid sequences and / or lycosylations that differ from those found in antibodies produced in other forms, especially sequences at the end of the fragments. Analogously, antibody fragments produced by recombinant DNA technology can include extra amino acid sequences at their terminal ends that have no counterpart in the antibodies produced in another way. A related possibility is that the binding agent for use in this invention is a natural or synthetic polymer that resembles the specific binding activity of a region complementary to the natural antibody. Said polymer is for example a polypeptide or a polymer fingerprint (Angew, Chem. Int. Ed. Engl, 1995, 34, 1812-1832). The usual method for the production of antibody can be adopted in the immunization of mammals or birds with the corresponding antigens. Since mammals will be immunized, mice, rabbits, goats, sheep, horses, cows, etc. can be used. The antibody (immunoglobulin fraction) can be separated from antiserum, milk or eggs in accordance with the ordinary antibody purification method including the purification method, Polson extraction, filtration chromatography, gel, ion exchange chromatography , affinity chromatography and the like, the purification method using ammonium sulfate to produce the precipitates, dialyzing the precipitates against the physiological saline solution to obtain the purified precipitates as the antibody. The plants are also capable of synthesizing and assembling all types of antibody molecules and allowing a large scale of antibody production as described in Tibtech. Dec 1995, Vol 13, pp 522-527; Plant Mol, Biol., 26, pp 1701-1710, 1994 and Biotechnol, proj, 1991, 7, pp. 455-461 and in the patent of E.U.A. 5,202,422. The antibodies can also be produced in microorganisms such as E. coli or 3. cerevisiae by the biofermentation process, as illustrated in the patent EP 667 394. The techniques for the production of antibody fragment are well known in the literature : Saiki et al. Science 230 1350-54 (1985); Orlani and other PNAS USA 86 3833-7 (1989); WO89 / 09825; EP 368 684; WO 91/08482 and W094 / 25591. The drawbacks due to the prolonged activity of the enzyme can be avoided by an effective control of the enzymatic activity through the introduction of the correspondingly corresponding body. Said antibodies can be polyclonal-directed to the whole structure of the enzyme- or monoclonal- directed to the specific hepitopes of the control regions of the enzyme activity of the structure of the enzyme. Antibodies raised against the specific enzyme can effectively inactivate the enzyme by binding the antibody-antigen in or very close to the active site. The formation of said complex leads to the deactivation of the enzyme and can be explained by the distortion of the 3-dimensional structure and / or steric hindrance in the slit of the substrate. The deactivation of the enzyme can also be achieved by precipitation of the antibody-antigen complex from the wash solution. Due to the very high specificity and efficiency of the antibody-antigen interaction, no other detergent active is affected in this way. Antibodies directed against protease are included - preferably in the detergent compositions of the present invention at a level of 10E-6% at 10E + 1% by weight of the total composition. In some cases, the antibodies produced against specific proteases have the ability to bind with other proteases of high structural similarity, providing cross-reactivity. Typically, a molecular ratio of antibody directed against protease: protease will be 100: 1 or less, preferably 50: 1 or less. For monoclonal antibodies or fragments thereof, the molecular ratio of antibody directed against protease: protease will generally be 50: 1 or less, preferably 20: 1 or less.

Antibodies raised against the protease are released into the wash solution after a period of delay that allows the protease to provide excellent performance benefits that will be achieved upon completion of the washing procedure. Therefore, antibodies are preferably incorporated in a release agent to control their time and rate of release in the wash solution. The physical form of the release agent containing antibodies is adapted to the physical form of the corresponding detergent or additive. For the granulated and powdered detergent and cleaning products, the antibodies and release agents can be contained in a granulate. Said antibody granulate may suitably contain various granulation aids, binders, fillers, plasticizers, lubricants, cores and the like. Examples thereof include cellulose (i.e. cellulosic fibers or in microcrystalline form), cellulose derivative (CMS, MC, HPC, HPMC), gelatin, starch, dextrins, sugars, polyvinylpyrrolidone, PVA, PEG, salts (i.e., sulfate of sodium, calcium sulfate), titanium dioxide, talc, clays (caolin or pentonite) and nonionic surfactants. Other materials of relevance for incorporation into the granulate are described in EP 304 331. The release agent can be, for example, a coating. Said coating protects said granules in the washing environment for a certain period. The coating is normally applied to said granulates in an amount in the range of 1% to 50% by weight (calculated on the weight basis of the uncoated, dry granules), preferably in the range of 5% to 40% by weight . The amount of coating to be applied to said granulates depends to a large extent on the nature of the composition of the desired coating, and on the kind of protection that said coating must offer to said granulates. For example, the thickness of said coating or a multilayer coating applied in any of the above granulates can determine the period in which the content of said granulates is released. A possible multiple layer coating can be a coating in which, for example, a quick release coating is applied in a slow release coating. Similarly, the cogranulates can be constructed by converting the detergent enzyme and a rapid release agent into the outer layer, and in the inner core, the antibody and a slow release agent. Suitable release coatings are the coatings that give rise to the release of the contents of the granules containing antibodies under the conditions prevailing during the use thereof. Thus, for example, when a preparation of the invention is to be introduced into a washing liquor containing a washing detergent (typically comprising, for example, one or more types of surfactants), the coating must be such that ensure the release of the contents of said granules from the release agent when it is introduced into the washing medium. The preferred release coating are coatings that are substantially insoluble in water. The release coatings which are suitable in the washing means may suitably comprise substances selected from the following: cellulose and cellulose derivatives, PVA, PVP, tallow; hydrogenated tallow; partially hydrolyzed tallow; fatty acids and fatty alcohols of natural and synthetic origin; long chain fatty acid mono- di- and glycerol triesters (ie, glycerol monostearate); ethoxylated fatty alcohols; latexes; hydrocarbon melting point in the 50-80 ° C scale; and waxes. Fusion coating agents are a preferred class of fast or slow release coating agents that can be used without dilution with water. Reference can be made to Controlled Relay Systems: Fabrication Technology, Vol. I, CRC Press, 1988, for more information on slow release coating. The coatings may further comprise - suitably substances such as clays (eg, kaolin), titanium dioxide, pigments, salts (such as calcium carbonate) and the like. The person skilled in the art is aware of other coating constituents of importance in the present invention. In liquid detergent compositions, the antibody can be incorporated as a particle dispersion containing, in addition to the antibody, a release agent. The antibody can be present in a liquid or solid form. Suitable particles consist of a porous hydrophobic material, ie, silica with an average pore diameter of 500 Angstroms or greater) containing the pores an antibody solution and a surfactant as described in EP 583 512 of Surutzidis A and others. The release agent can be a coating that protects said particles in the wash cycle for a certain period. The coating is preferably a hydrophobic coating material such as the liquid hydrophobic polymer. Said polymer can be an organo polysiloxane oil, alternatively a hydrocarbon of high molecular weight or water insoluble but with polymeric material permeable to water such as carboxymethyl cellulose, PVA, PVP. The polymer properties are selected to achieve a proper release profile of the antibody in the wash solution.

Enzyme protease The proteolytic enzymes are incorporated in the detergent compositions of the present invention at a level of from 0.0001% to 2%, preferably from 0.001% to 0.2%, more preferably from 0.005% to 0.1% by weight of pure enzyme of the composition. The proteolytic enzyme can be of various origins, for example, produced by mammals, plants or microorganisms. Its origin can also be mesophilic or extremophile (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Microorganisms are preferred producers of proteolytic enzymes. More preferred are serine proteases of bacterial origin. Purified or non-purified forms of these enzymes can be used. Also included by definition, they are mutants of native enzymes. Mutants can be obtained, for example, by protein engineering and / or genetic engineering, as well as by chemical and / or physical modifications of native enzymes. A common practice is also the expression of the enzyme by the host organism in which the genetic material responsible for the production of the enzyme has been cloned. Suitable proteases are the subtilisins that are obtained from particular strains of B. subtilis and B. licheniformis (subtilisins BPN and BPN '). A suitable protease is obtained from a strain of Bacillus, which has a maximum activity through the pH scale of 8-12, developed and sold as ESPERASER by Novo Industries A / S of Denmark, hereinafter "Novo". The preparation of said enzyme and analogous enzymes is described in GB 1,243,784 of Novo. Other suitable proteases include ALCALASER, DURAZYMR and SAVINASER from Novo and MAXATASER, MAXACALR, PROPERASER and MAXAPEMR (protein produced by Maxacal) from Gist-Brocades. The proteolytic enzymes also comprise modified bacterial serine proteases, such as those described in European Patent Application Serial No. 87303761.8, issued April 28, 1987 (particularly pages 17, 24 and 98), and which in the present are called "Protease B", and in the European patent application 199,404, Venegas, published on October 29, 1986, which refers to the modified bacterial serine proteolytic enzyme which is called "Protease A" in the present . Protease called in the present "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 aspargine at position 123, and alanine replaces trionine at position 274. Protease C is described in EP 90915958: 4, corresponding to WO 91/06637, published May 16, 1991. Genetically modified variants, particularly of protease C, are also included herein. The preferred protease, referred to as "Protease D", is a variant of a carbonyl hydrolase having an amino acid sequence but found in nature, which is derived from a carbonyl hydrolase precursor by substituting a different amino acid for a plurality of amino acids. amino acid residues at a position in said carbonyl and hydrolase equivalent at position +76, preferably also at * 5 combination with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +10, +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 number of 0 subtilisin of Bacillus amiloliquefaciens, as described in WO95 / 10591 and in the patent application C. Ghosh et al., "Bleaching Compositions Comprising Protease Enzymes" having the serial number of USA. 08 / 322,667, issued October 13, 1994. 5 Also suitable for the present invention are the proteases described in patent applications EP 251 446 and WO 91/06637, BLAPR protease described in WO91 / 02792 and its variant, described in W095 / 23221. See also a high pH protease from Bacillus sp. 0 NCIMB 40338 described in WO93 / 18140 A de Novo. Enzymatic detergents comprising protease, one or more enzymes, and a reversible protease inhibitor are described in WO 92/03529 A of Novo. When desired, a protease having reduced absorption and increased hydrolysis is available as described in WO 95/07791 to Procter & amp; amp; amp;; Gamble. A protease similar to the recombinant trypsin for detergent suitable herein is described in WO 94/25583 of Novo. Other suitable proteases are described in EP 516 200 by Unilever. * The composition of the present invention may also include protease enzymes which are variants of carbonyl hydrolase that do not occur naturally and which have proteolytic activity, stability, specific character of the substrate, pH profile and / or different performance characteristics, in comparison with the carbonyl hydrolase precursor of which the amino acid sequence of the variant is derived. As mentioned above, the protease enzymes are designed to have specific character similar to trypsin and also preferably be stable in bleach. The precursor carbonyl hydrolase can be a naturally occurring hydroxylase or hydroxylase hydroxylase. Specifically, said carbonyl hydrolase variants have an amino acid sequence not found in nature, which is derived by replacing a plurality of amino acid residues of a precursor carbonyl hydrolase with 0 different amino acids. The plurality of amino acid residues of the precursor enzyme correspond to the +210 position in combination with one or more of the following residues: +33, +62 +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, 5 +215, +217, +218 and + 222, wherein the numbered position corresponds to Bacillus amiloliquefaciens subtilisin occurring naturally or to equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin. * The sarbonyl hydrolase variants that are enzymes J5 proteases useful in the compositions of the present invention comprise the replacement of amino acid residue +210 in combination with one or more additional modifications. Although any combination of the above amino acid residue substitutions can be used, the preferred variant enzymes or proteases useful for the present invention comprise the substitution, deletion or insertion of amino acid residues in the following combinations 210/156; 210/166; 210/76; 210/103; 210/104; 210/217 210/156/166; 210/156/217; 210/166/217; 210/76/156; 210/76/166 5 210/76/217; 210/76/156/166; 210/76/156/217; 210/76/166/217 210/76/103/156; 210/76/103/166; 210/76/103/217; 210/76/104/156 210/76/104/166; 210/76/104/217; 210/76/103/104/156 210/76/103/104/166; 210/76/103/104/217; 210/76/103/104/156/166 210/76/103/104/156/217; 210/76/103/104/166/217 and / or 0 210/76/103/104/156/166/217; 210/76/103/104/166/222; 210/67/76/103/104/166/222; 210/67/76/103/104/166/218/222. More preferably, the variant enzymes useful for the present invention comprise the substitution, deletion or insertion of an amino acid residue in the following combination of 5 residues: 210/156; 210/166; 210/217; 210/15/166; 210/156/217; 210/166/217; 210/76/156/166; 210/76/103/156/166; and 210/76/103/104/156/166 of subtilisin from B. lentus, with 210/76/103/104/156/166 being the most preferred. The variant DNA sequences that code for * said carbonyl hydrolase or subtilisin variants are * 5 are derived from a precursor DNA sequence that codes for a recombinant or naturally occurring precursor enzyme. The variant DNA sequences are derived by modifying the precursor DNA sequence encoding the substitution of one or more specific amino acid residues encoded by the precursor DNA sequence corresponding to positions +210, +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 in Bacillus lentus or any combination thereof. Although the amino acid residues identified for modification herein are identified in accordance with the numbering applicable to B. amyloliquefaciens (which has been the conventional method for identifying residue positions in all subtilisins), the precursor DNA sequence useful for present invention 0 is the DNA sequence of Bacillus lentus. These recombinant DNA sequences encode carbonyl hydrolase variants having a novel amino acid sequence and, in general, at least one property that is substantially different from the same property of the enzyme encoded by the carbonyl hydrolase DNA precursor sequence. . Said properties include proteolytic activity, specific character of the substrate, stability, altered pH profile and / or improved performance characteristics. The protease enzymes useful herein encompass the substitution of any of the nineteen naturally occurring L-amino acids at the designated positions of amino acid residues. Said substitutions can be made in any precursor subtilisin (prokaryotic, eukaryotic, mammalian, etc.). Throughout this application, several amino acids are referred to by common one and three letter codes. These codes are identified in Dale, M.W. (1989). Molecular Genetics of Becteria, John Wiley & Sons, Ltd., Appendix B. Preferably, the substitution to be made at each of the identified positions of amino acid residues includes, but is not limited to, substitutions at position +210, including I, V, L and A , substitutions at positions +33, +62, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217 and +218 of D or E, substitutions at position 76, including D, H, E, G, F, K, P and N; substitutions at position 103, including Q, T, D, E, Y, K, G, R and S; and substitutions at position 104, including S, Y, I, L, M, A, W, D, T, G and V; and substitutions at position 222, including S, C and A. The specifically preferred amino acids that will be substituted at each position are designated below in Table I. Although specific amino acids are shown in Table I, it should be understood that any amino acid it can be replaced in the identified waste.

TABLE I * 5 Preferred Amino Acid amino acid residue to be replaced / inserted +210 I, V, L, A +33, +62, +100, +101, +107 D, E 0 +128, +129, +130, +135 +156, +158, +164, +166 +167, +170, +209, +215 +217 and +218 +76 D, H5. +103 A, Q, T, D, E, Y, K, G, R +104 I, Y, S, L, A, T, G +222 S, C, A A comparison of the preferred 0 amino acid residues identified herein for substitution against the preferred substitution for each of said positions is provided in Table II.

TABLE II +120 +156 +166 +217 +76 +103 +104 B. amyloliauefaciens P E G Y N Q Y (wild type) B. lentus P S S L N S V (wild type) Substitution plus I E / D E / D E / D D A I / Y preferred Detergent Components The detergent compositions of the invention may also contain additional detergent components. The precise nature of said additional components, and levels of incorporation thereof depend on the physical form of the composition, and the nature of the cleaning operation for which they are to be used. The detergent compositions according to the invention can be liquids, pastes, gels, sticks, tablets, powder and granular forms. The granulated compositions can also be found in the "compact" form, the liquid compositions can also be found in a "concentrated" form. The compositions of the invention can, for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the rinsing and / or pretreatment of soiled fabrics and in fabric softening compositions added during the rinse. Such compositions can provide fabric cleaning, stain removal, maintenance of whiteness, softness, color appearance and dye transfer inhibition benefits. When formulated as compositions suitable for use in a machine laundry method for laundry, the compositions of the invention preferably contain a surfactant and a builder compound and additionally one or more detergent components preferably selected from the polymeric compounds. organic, bleaching agents, additional enzymes, foam suppressants, dispersants, soap dispersants, soil sludge and anti-rejection agents and corrosion inhibitors. The laundry compositions may also contain softening agents as additional detergent components. The compositions of the present invention can also be used as detergent additive products comprising an antibody directed against protease, and will be added to conventional detergent-containing detergent compositions. The detergent additives may also comprise the protease and the antibody directed against it. Said additive products are intended to supplement or increase the performance of conventional detergent compositions, and preferably comprise up to 50% by weight of antibodies of the total composition.

If necessary, the density of the laundry detergent compositions herein ranges from 400 to 1,200 g / liter, preferably from 600 to 950 g / liter of the composition, measured at 20 ° C. The "compact" form of the granular laundry detergent compositions herein is best reflected by the density and, in terms of composition, by the amount of inorganic filler salt; the inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition. In compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, more preferably not exceeding 5% by weight of the composition. Inorganic filler salts, as referred to in the present compositions, are selected from alkali metal and alkaline earth metal salts of sulfates and chlorides. A preferred filler salt is sodium sulfate. The liquid detergent compositions according to the present invention can also be found in a "concentrated form", in which case, the liquid detergent compositions according to the present invention contain a lower amount of water, compared to conventional liquid detergents. Typically, the water content of the concentrated liquid detergent is preferably less than 40%, more preferably less than 30%, and most preferably less than 20% by weight of the detergent composition.

Surfactant System The detergent compositions according to the present invention comprise a surfactant system in which the surfactant can be selected from nonionic and / or anionic and / or cationic and / or ampholytic and / or zwitterionic surfactants and / or semi-polar. The surfactant is typically present at a level of 0.1% to 60% by weight. The most preferred levels of incorporation are 1% to 35% by weight, preferably 1% to 30% by weight of the detergent compositions according to the invention. The surfactant is preferably formulated to be compatible with the enzyme components present in the composition. In liquid or gel compositions, the surfactant is more preferably formulated in a manner that promotes, or at least does not degrade, the stability of any enzyme in these compositions. Preferred surfactant systems for use in accordance with the present invention comprise as the surfactant one or more of the nonionic and / or anionic surfactants described herein. The polyethylene oxide, polypropylene and polybutylene oxide condensates of alkylphenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being preferred. These compounds include the condensation products of alkylphenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, either in a straight chain or branched chain with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to about 2 to about 25 moles, preferably about 3 to about 15 moles of ethylene oxide per mole of alkylphenol. Commercially available nonionic surfactants of this type include Igepal CO-630, marketed by GAF Corporation; and Triton ™ X-45, X-114, X-100 and X-102, all sold by Rohm & Haas Company. These surfactants are commonly known as alkylphenol alkoxylates (for example, alkylphenol ethoxylates). The condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant system of the present invention. The alkyl chain of the aliphatic alcohol may be either straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide. per mole of alcohol. About 2 to about 7 moles of ethylene oxide are present, and more preferably 2 to 5 moles of ethylene oxide per mole of alcohol in said condensation products. Examples of commercially available nonionic surfactants of this type include Tergitol ™ 15-S-9 (the linear alcohol condensation product of Cn-C] _5 with 9 moles of ethylene oxide), Tergitol ™ 24 -L-6 NMW (the primary alcohol condensation product of C12-C1 with 6 moles of ethylene oxide with a limited molecular weight distribution), both marketed by Union Carbide Corporation; Neodol TM 45-9 (the condensation product of linear alcohol of c14 ~ c15 with 9 moles of ethylene oxide), Neodol 23-3 (the linear condensation product of C] _2 ~ i3 with 3.0 moles of ethylene), Neodol "PM 45-5 (the condensation product of linear C14-C15 alcohol with 7 moles of rpi ethylene oxide), Neodol 45-5 (the linear alcohol condensation product of C ^ -C ^ with 5 moles of ethylene oxide), marketed by Shell Chemical Company, Kyro EOB (the condensation product of C13-C15 alcohol with 9 moles of ethylene oxide), marketed by The Procter & amp; amp;; Gamble Company, and Genapol LA 050 (the alcohol condensation product of Ci2 ~ c1 with 5 moles of ethylene oxide), marketed by Hoechst. The preferred scale of HLB in these products is 8-11, and most preferred is 8-10. Also useful as the nonionic surfactant of the surfactant systems of the present invention are the alkylpolysaccharides described in the U.S.A. No. 4,565,647, Filling, issued January 21, 1986, having a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms, and a polysaccharide, per example, a polyglycoside, a hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, more preferably from about 1.3 to about 2.7 units of saccharide. Any reducing saccharide containing 5 or 6 carbon atoms can be used, for example, the glucose, galactose and galactosyl moieties can replace the glucosyl moieties (optionally the hydrophobic moiety is attached in the 2-, 3-, 4- positions). , etc., thus giving a glucose or galactose as opposed to a glucoside or galactoside). The intersaccharide bonds can be, for example, between position one of the additional saccharide units and positions 2-, 3-, 4- and / or 6- of the preceding saccharide units. Preferred alkyl polyglycosides have the formula ^ 5 R ^ O (CnH2n0) t (glycosyl) or wherein R is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof, wherein the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, atoms of carbon; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, more preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alkylpolyethoxylated alcohol or alcohol is first formed, and then reacted with glucose or a source of glucose to form the glucoside (linkage at position 1). The additional glycosyl units can then be linked between their position 1 and the preceding glycosyl units in the 2-, 3-, 4- and / or 6- position, preferably predominantly in the 2-position. ethylene with a hydrophobic base, formed by the condensation of propylene oxide with propylene glycol, are also suitable for use as the additional nonionic surfactant system of the present invention. The hydrophobic portion of these compounds will preferably have a molecular weight of -I 5 about 1500 to about 1800, and will exhibit insolubility in water. The addition of polyoxethylene portions to this hydrophobic portion tends to increase the water solubility of the molecule in general, and the liquid character of the product is retained to the point where the polyoxethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include some Plurafac ™ LF404 and Pluronic ™ surfactants commercially available from BASF. Also suitable for use as the nonionic surfactant of the nonionic surfactant system of the present invention, are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine. The hydrophobic portion of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of about 2500 to about 3000. This hydrophobic portion is condensed with ethylene oxide to the extent that the The condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5000 to about 11,000. Examples of this type of nonionic surfactant include some of the Tetronic ™ compounds, commercially available from BASF. Preferred to be used as the nonionic surfactant of the surfactant systems of the present invention are the polyethylene oxide condensates of alkylphenols, the condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides and mixtures thereof. Preferred are Cg-C ^ alkylphenol ethoxylates having from 3 to 15 ethoxy groups and the C3-C18 alcohol ethoxylates (preferably from average C) having from 2 to 10 ethoxy groups, and mixtures thereof. thereof. The highly preferred nonionic surfactants are the polyhydroxy fatty acid amide surfactants of the formula R ^ C - N - Z, O RJ wherein R 1 is H, or R 1 is C 1 -C 4 hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl or a mixture thereof, R is C5-31 hydrocarbyl and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly attached to the chain, or an alkoxylated derivative thereof. Preferably, R is methyl, R is an alkyl chain of Cn-C ^ or alkyl or alkenyl of straight C ^ gC ^ s, such as cocoalkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose and lactose, in a reductive amination reaction. Suitable anionic surfactants that are used are the alkyl ether sulfonate surfactants that include linear esters of C3-C20 carboxylic acids (ie, fatty acids) that are sulfonated with gaseous SO3 according to "The Journal of the American Oil Chemists Society ", 52 (1975), p. 323-329. Suitable starting materials would include natural fatty substances such as those derived from tallow, palm oil, etc. The preferred alkyl ether sulphonate surfactant, especially for laundry applications, comprises alkyl ether sulphonate surfactants of the structural formula: OR R- CH C OR- SO3M wherein R is a C8-C20 hydrocarbyl preferably an alkyl, or combination thereof, R is a hydrocarbyl of C ^ -Cg, preferably an alkyl or a combination thereof, and M is a cation that forms a soluble salt in water with the alkyl ether sulfonate. Suitable salt-forming cations include metals such as sodium, potassium and lithium, and substituted or unsubstituted ammonium cations such as monoethanolamine, diethanolamine and triethanolamine. Preferably, R is C ^ g-C ^ g alkyl and R is methyl, ethyl or isopropyl. Methyl-ethersulphon-methyl-tetra-sulfonates in alkyl are especially preferred. Other suitable anionic surfactants include the alkyl sulfate surfactants which are salts or water-soluble acids of the formula ROSO3M, wherein R is preferably a C10-C24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having an alkyl component of (-.10 ~ c20 'more preferably an alkyl or hydroxyalkyl of C] _2"Ci8 and M is H or a cation, for example, an alkali metal cation (e.g. sodium, potassium, lithium), or substituted ammonium or * ammonium (for example, methyl-, dimethyl-, and trimethylammonium cations and quaternary ammonium cations such as tetramethylammonium and dimethylpiperidinium cations, and quaternary ammonium cations derived from alkylamines such as 0 ethylamine, diethylamine, triethylamine and mixtures thereof, and the like.) Typically, the C cadenas-ig alkyl chains are preferred for temperatures lower washings (for example, below about 50 ° C) and alkyl chains of C] _g _] _ 3 are preferred for higher wash temperatures (for example, about 50 ° C). Other anionic surfactants useful for detersive purposes may also be included in the detergent compositions of the present invention. These may include salts (including, for example, sodium, potassium, ammonium and substituted ammonium salts such as salts of -5 mono-, di- and triethanolamine) of soap, primary or secondary alkanesulfonates of Cg-C22. C8-C24 olefin sulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, for example, as described in the description of British Patent No. 1,082,179, Cg-C24 alkyl polyglycol ether sulphates (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, fatty alkyl glycerol sulfonates, alkyl phenol ethers sulfates of ethylene oxide, paraffinsulfonates, alkyl phosphates, 5-isethionates, such as acyl isethionates, N-acyltaurates, * Alkylsuccinamates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C ^ -C ^ monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated Cg-C? _2 diesters), acyl sarcosinates, or sulphates of alkylpolysaccharides such as sulfates of alkyl polyglucoside (non-sulphonated nonionic compounds are described below), branched primary alkyl sulphates and alkyl polyethoxy carboxylates such as those of the formula RO (CH 2 CH 2?) k-CH 2 COO-M +, wherein R is a C 8 -C 22 alkyl is an integer from 1 to 10, and M is a soluble salt forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin and rosin acids, as well as hydrogenated rosin acids present in, or derived from, oil from - tallow tree. * 5 Additional examples are described in "Surface Active Agents and Detergents "(Vol.I and II of Schwartz, Perry and Berch.) A variety of such surfactants are also generally described in U.S. Patent No. 3,929,678, issued December 30, 1975 to Laughiin and 0 others, in Column 23, line 58 to Column 29, line 23 (incorporated herein by reference.) When included herein, the laundry detergent compositions of the present invention typically comprise from about 1% to about 40%, preferably from about 3% to about 20% by weight of said agents * anionic surfactants. Highly preferred anionic surfactants include alkoxylated alkylsulfate surfactants which are salts or water-soluble acids of the formula 0 RO (A) mS03M, wherein R is an unsubstituted C10-C24 alkyl or hydroxyalkyl group having an alkyl component of C_Q - C24, preferably an alkyl or hydroxyalkyl of C] _2 ~ C20 / more preferably alkyl or hydroxyalkyl of A is an ethoxy or propoxy unit, m is greater than zero, typically between 0.5 and about 6, more preferably between 0.5 and 0.5; about 3, and M is H or a cation which may be, for example, a metal cation (eg, sodium, potassium, lithium, calcium, magnesium, etc.) or an ammonium or substituted ammonium cation. The ethoxylated alkyl sulphates, as well as the propoxylated alkyl sulphates, are also contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl-, and trimethylammonium cations, and quaternary ammonium cations such as tetramethylammonium and dimethylpiperidinium cations, and those derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof and Similar. Exemplary surfactants are polyethoxylated alkyl sulfate (1.0) of Ct_2 ~ ci8 (C1-C18E (1.0) M), polyethoxylated alkyl sulfate (2.25) of C ^ -C ^ (C12-C18E (2.25) M), polyethoxylated alkyl sulfate (3.0) of C ^ -C ^ (C12-C18E (3.0) M), and polyethoxylated alkyl sulfate (4.0) of C12- C18 (C:? _ 2-C18E (4.0) M), in which M is conveniently selected from sodium and potassium . The detergent compositions of the present invention may also contain cationic, ampholytic, zwitterionic and semipolar surfactants, as well as other nonionic and / or anionic surfactants than those already described herein. Suitable cationic detersive surfactants for use in the detergent compositions of the present invention are those having a long chain hydrocarbyl group. Examples of such cationic surfactants include ammonium surfactants such as alkyltrimethylammonium halides and surfactants having the formula: [R2 (OR3) and] [R4 (0R3) and] 2R5N + X- p wherein R is an alkyl or alkylbenzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R is selected from a group consisting of -CH2CH2-, -CH2CH (CH3) -, -CH2CH (CH2OH) -, -CH2CH2CH2-, and mixtures thereof; each R is selected from the group consisting of C1-C4 alkyl, C1-C4 hydroxyalkyl, benzyl ring structures formed by joining the two groups R4, -CH2CHOH-, -CHOHCOR6CHOHCH2OH, wherein R6 is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when and not 0; R is the same as R or is an alkyl chain wherein p rr the total number of carbon atoms of R plus R is not greater than about 18; each y is from 0 to approximately 10 and the sum of the values of y is from 0 to approximately 15; and X is any compatible anion. The quaternary ammonium surfactants suitable for the present invention have the formula: x- wherein R 1 is a short chain alkyl (Cg-Ct_o- ° alkylamidoalkyl of formula (II): wherein y is 2-4, preferably 3, whereby R2 is H or a C1-C3 alkyl; whereby x is 0-4, preferably 0-2, very preferably 0; whereby R3, R4 and R5 are the same or different and may be a short chain alkyl (C1-C3) or alkoxylated alkyl of formula III; whereby X "is a counterion, preferably a halide, for example, chloride, or methyl sulfate, R6 is C1-C4 and z is 1 or 2. Preferred quaternary ammonium surfactants are those defined in formula I with wherein R ^ is Cg, C ^ o ° mixtures thereof, x = 0, R3, R4 = CH3 and R5 = CH2CH2OH Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition, which have the formula: 1R2R3R4N + X (i wherein R? _ is Cg-C alkyl? _g, each of R 2, R 3 and R 4 is independently C 1 -C 4 alkyl, hydroxyalkyl of C 1 -C 4. benzyl and - (C2H4Q)? H, where x has a value of 2 to 5 and x is an anion. No more than one of R2, R3 or R4 must be benzyl. The preferred length of the alkyl chain for R] _ is C 12 -C 15, particularly when the alkyl group is a mixture of chain lengths derived from palm or coconut seed fat, ie synthetically derived by olefin formation or synthesis of alcohols 0X0. Preferred groups for R2, R3 and 4 are methyl and hydroxyethyl groups, and the anion X can be selected from halide, methosulfate, acetate and phosphate ions. Examples of quaternary ammonium compounds of the formula (i) suitable for use herein are: cocotrimethylammonium chloride or bromide; cocomethyldihydroxyethylammonium chloride or bromide; decyltriethylammonium chloride; decildimethylhydroxyethylammonium chloride or bromide; dimethylhydroxyethylammonium chloride or bromide of C12-c15 '* cocodimethylhydroxyethylammonium chloride or bromide, • myristyltrimethylammonium methylsulfate; lauryl dimethylbenzylammonium chloride or bromide; lauryldimethyl (ethenoxy) 4 ammonium chloride or bromide; choline esters (compounds of formula (i) wherein R] _ is CH2-CH2-O-C-C12-14 alkyl and R2R3R4 are methyl). Or di-alkylimidazolines [compounds of formula (i)]. Other cationic surfactants useful herein are also described in the U.S.A. No. 4,228, 044, Cambre, issued October 14, 1980, and in the European Patent Application EP 000,224. When included, the detergent compositions of the present invention typically comprise from 0.2% to about 25%, preferably from about 1% to about 8% by weight of said cationic surfactants. The ampholytic surfactants are also suitable for use in the detergent compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or as aliphatic derivatives of heterocyclic secondary or tertiary amines in which the aliphatic radical can be a straight or branched chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water solubilization group, for example, carboxy, sulfate, sulfonate. See the patent of E.U.A. No. 3,929,678 to Laughiin et al., Issued December 30, 1975, column 19, lines 18-35, for examples of ampholytic surfactants. When included, the detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of said ampholytic surfactants. Zwitterionic surfactants are also suitable for use in detergent compositions. These "Surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines or derivatives of quaternary ammonium compounds, quaternary phosphonium or tertiary sulfonium. See the patent of E.U.A. No. 3,929,678 to Laughiin et al., Issued December 30, 1975, in column 19 line 38, to column 22 line 48, for examples of zwitterionic surfactants. When included, the detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of said zwitterionic surfactants. Semi-polar nonionic surfactants are a special category of nonionic surfactants that include water-soluble amine oxides containing an alkyl portion of from about 10 to about 18 carbon atoms and 2 portions selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-soluble phosphine oxides containing an alkyl portion of from about 10 to about 18 carbon atoms and two portions selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing an alkyl portion of about * 10 to about 18 carbon atoms, and a portion selected from the group consisting of alkyl and hydroxyalkyl portions of from about 1 to about 3 carbon atoms. Semi-polar nonionic surfactants include the amine oxide surfactants having the formula: 0 t R3 (0R4) xN (R5) 2 wherein R is an alkyl, hydroxyalkyl or alkylphenyl group, or mixtures thereof, containing from about 8 to about 22 carbon atoms; R is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms, or mixtures thereof; x is from 0 to about 3; and each R is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms, or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R groups may be linked to each other, for example, through an oxygen or nitrogen atom to form a ring structure. These amine oxide surfactants include in particular alkydimethylamine oxides of C.sub.1-8 and alkoxyethyldihydroxyethylamine oxides of C.sub.Q -Cl.sub.2 - When included, the detergent compositions of the present invention typically comprise from about 0.2% to about 15%. , preferably from about 1% to about 10% by weight of said semi-polar nonionic surfactants. The detergent composition of the present invention may further preferably comprise a co-surfactant selected from the group of primary or tertiary amines. Primary amines suitable for use herein include amines according to the formula R] _ NH2, wherein R ^ is an alkyl chain of C -Ciß. preferably C -CiQ. ° R4X (CH2) n 'X is -0 -, - C (0) NH- or -NH-, R4 is an alkyl chain of C -C ^. n is between 1 to 5, preferably 3. The alkyl chains of R_ may be straight or branched and may be interrupted with up to 12, preferably less than 5, portions of ethylene oxide. Preferred amines according to the above formula are the n-alkylamines. Amines suitable for use herein may be selected from 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary amines include Cß-Cig oxypropylamine, octyloxypropylamine, 2-ethylexyl-oxypropylamine, laurylamido-propylamine and amidopropylamine. Tertiary amines suitable for use herein include tertiary amines having the formula R1R2 3N, wherein R] _ and R2 are Ci-Cg alkyl chains or i 5 (CH2-CH-0) xH R3 is an alkyl chain of C -C ^ * - preferably Cg-C10, or R3 is R4X (CH2) n, where X is -0 -, - C (0) NH- or -NH-, R4 is a C4 -C12 / n is between 1 to 5, preferably 2-3. R5 is H or C -C2 alkyl and x is between 1 to 6. R3 and R4 can be linear or branched; the alkyl chains of R3 can be interrupted with up to 12, preferably less than 5, portions of ethylene oxide. The preferred tertiary amines are R1R2 3N where Rl is an alkyl chain of Cg-Ci2, R2 and R3 are C? -C3 alkyl, or (CH2-CH-0)? H where R5 is H or CH3 and x = 1-2. Amidoamines of the formula are also preferred: OR II R! - C-NH- (CH2) n-N- (R2) 2 wherein R] _ is alkyl of -Ci2; n is 2-4, preferably n is 3; R2 and R3 is C -C4. The most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, oxy-propylamine of CS-CIQ. N-COCO-1-3-diaminopropane, cocoalkyldimethylamine, lauryldimethylamine, laurylbis (hydroxyethyl) amine, coco-bis (hydroxyethyl) amine, lauryl amine propoxylated with 2 moles, propoxylated octylamine with 2 moles, laurylamidopropyldimethylamine, C8-C10 amidopropyldimethylamine and amidopropyldimethylamine CT_Q- The most preferred amines for use in the compositions herein are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Particularly suitable are n-dodecyldimethylamine and bishydroxyethylcocoalkylamine and 7-fold ethoxylated oleylamine, laurylamidopropylamine and cocoamidopropylamine.

Conventional detergent enzymes The detergent compositions may also contain one or more enzymes that provide cleansing action and / or fabric care benefits. Said enzymes include selected enzymes of hemicellulases, peroxidases, glucoamylases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tanases, pentosanas, malanases, β-glucanases, arabinosidases , hyaluronidase, chondroitinase, laccase or mixtures thereof. A preferred combination is a detergent composition having a cocktail of conventional applicable enzymes such as protease, amylase, lipase, cutinase and / or cellulase, in conjunction with one or more plant cell wall degrading enzymes. Cellulases useful in the present invention include both bacterial and fungal cellulase.

Preferably, they will have an optimum pH of between 5 and 9.5.

Suitable cellulases are described in the US patent. Do not. 4,435,307, Bargesgoard et al., Which describe a fungal cellulase produced from Humicola insolens. Suitable cellulases are also described in GB-A-2,075,028; GB-A-2,095,275 and DE-OS-2,247,832. Examples of these cellulases are those produced by a strain of Humicola insolens (Humicola grisea var. Thermoidea), particularly the DSM 1800 strain of Humicola. Other suitable cellulases are the cellulases originated from Humicola insolens that have a molecular weight of approximately 50 KDa, an isoelectric point of 5.5 and contain 415 amino acids; and a ~ 43 kD endoglucanase derived from Humicola insolens DSM 1800, which exhibits cellulase activity; a preferred component of endoglucanase has the amino acid sequence described in PCT patent application No. WO 91/17243. Other suitable cellulases are the EGIII cellulases of Trichoderma longibrachiatum described in WO 94/21801, Genencor, published September 29, 1994. Especially suitable cellulases are cellulases which have color care benefits. Examples of these cellulases are the cellulases described in European Patent Application No. 9122879.2, filed on November 6, 1991 (Novo). Peroxidase enzymes are used in combination with oxygen sources, for example, percarbonate, perborate, »Persulfate, hydrogen peroxide, etc. They are used for "bleached solution", that is, to avoid the transfer of dyes or pigments removed from the substrates during the 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 the PCT International Application WO89 / 099813, and in European Patent Application No. 91202882.6, filed on November 6, 1991.

Other suitable oxidases are the laccase enzyme, which uses oxygen or hydrogen peroxide as the primary substrate. Said cellulases and / or peroxidases are normally incorporated in the detergent composition at levels of 0.0001% to 2% 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 trade name Lipasa P "Amano", hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, Chromobacter viscosum lipases, for example, Chromobacter viscosum var. lipolyticum NRRLB 3673 by Toyo Jozo Co. , Japan Tagata; Chromobacter viscosum lipases from U.S. Biochemical Corp. E.U.A. and Disoynth Co., The Netherlands, and lipases, for example, from Pseudomonas gladioli. Especially suitable lipases are lipases such as Ml Lipase and Lipomax (Gist-Brocades) and Lipolase (Novo), which have been found most effective when used in combination with the compositions of the present invention.

Also suitable are cutinases [EC 3.1.1.50], which can be considered as a special type of lipase, namely, lipases that do not require interfacial activation. Suitable cutinases are described in WO 94/14963 and WO / 94/14964. The addition of cutinases to detergent compositions has been described, for example, in WO-A-88/09367 (Genencor). 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 (Ó and / or ß) can be included for the removal of carbohydrate-based spots. The document WO94 / 02597, Novo Nordisk A / S, published on February 3, 1994, describe cleaning compositions that incorporate mutant amylases. See also WO / 94/18314, Genencor, published on August 18, 1994 and WO / 95/10603, Novo Nordisk.

A / S, published April 20, 1995. Other amylases to be used in cleaning compositions include O- and β-amylases.

The O-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; RF 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 amylases of improved stability including Purafact Ox Am described in W094 / 18314, published August 18, 1994 and amylase variants having further modification in the immediate parent, available from Novo Nordisk A / S and described in WO95 / 10603, published April 1995. Examples of commercial O-amylases products are Purafact Ox Am from Genencor, and * Termamyl, Ban, Fungamyl® and Duramyl®, all available from * 5 Novo Nordisk A / S Denmark. Document W095 / 26397 describes other suitable amylases: Ó-amylases characterized by having a specific activity at least 25% higher than the specific activity of Termamyl at a temperature range of 25 ° C to 55 ° C and a pH value in the scale from 8 to 10, 0 measured by the Phadebas Ó-amylase activity test. 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 aforementioned enzymes can be of any suitable origin, such as of vegetable, animal, bacterial, fungal and yeast origin. Said enzymes are normally incorporated in the detergent composition at levels of 0.0001% to 2% active enzyme by weight of the detergent composition. They can be added as separate ingredients 0 (pellets, granulates, stabilized liquids, etc., containing an enzyme), or as mixtures of two or more enzymes (for example, cogranulates). Other suitable detergent ingredients that can be added are enzyme oxidation scavengers that are described in European Copending Patent Application No. 92870018.6, filed January 31, 1992. Examples of these enzyme oxidation scavengers are the ethoxylated tetraethylene polyamines. A variety of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A for Genencor International, WO 8908694 A for Novo, and US Pat. No. 3,553,139, January 5, 1971 for McCarty et al. Enzymes are also described in U.S. Pat. No. 4,101,457, Place et al., July 18, 1978, and in the US Patent. No. 4,507,219, Hughes, March 26, 1985. Enzyme materials useful for liquid detergent formulations, and their incorporation into these formulations, are described in US Pat. No. 4,261,868, Hora et al., April 14, 1981. Enzymes to be used in detergents can be stabilized by * medium of several techniques. Enzyme stabilization techniques are described and are exemplified in U.S. Pat. No. 3,600,319, of August 17, 1971, Gedge et al., EP 199,405 and EP 200,586, of October 29, 1986, for Venegas. Enzyme stabilization systems are also described, for example, in the U.S. Patent. No. 3,519,570. A Bacillus, sp. AC13 useful for giving proteases, xylanases and cellulases in WO 9401532 A for Novo.

Benefits for color care Technologies that provide a type of benefit for color care can also be included. Examples of these technologies are metallocatalysts for color maintenance. Metallocatalysts are also described in European Patent Application No. 92870181.2. The Blanching Agent The detergent compositions of the present invention may further include bleaching agents such as hydrogen peroxide, PB1, PB4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components may include one or more oxygen bleaching agents and, depending on the bleaching agent chosen, one or more bleach activators. When present, oxygen bleach compounds will typically be present at levels of about 1% to about 25%.

* The bleaching agent component for use herein may be any of the bleaching agents useful for detergent compositions including oxygen bleaching as well as others known in the art. The bleaching agent suitable for the present invention can be an activated or non-activated bleaching agent. A category of oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include in magnesium monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloroperbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxydecanedioic acid. Such bleaching examples are set forth in U.S. Patent 4,483,781, the patent application of E.U.A. 740,446, European patent application 0,133,354 and US patent 4,412,934. Highly preferred bleaching agents include 6-nonylamino-6-oxoperoxycaproic acid as described in the U.S.A. 4,634,551. Another category of bleaching agents that can be used encompasses halogen bleaching agents. Examples of hypohalogenite bleaching agents, for example, include isocyanuric acid and dichloroisocyanurates and sodium and potassium N-chloro- and N-bromoalkanesulfonamides. Such materials are usually added to 0.5-10% by weight of the finished product, preferably, 1-5% by weight. Peroxide-releasing agents can be used * hydrogen in combination with bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934), 3,5, -trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or pentaacetylglucose (PAG) or phenolsulfonate-ether of N-nonanoyl-6-aminocaproic acid (NACA-OBS, described in WO94 / 28106), which are perhydrolyzed to form a peracid as the active bleaching species, producing an improved bleaching effect. Acylated citrate esters such as are disclosed in European Patent Application No. 91870207.7 are also suitable activators.

Useful bleaching agents, including peroxyacids comprising bleach activators and peroxygen bleach compounds are disclosed for use in detergent compositions according to the invention, in applications USSN 08 / 136,626, PCT / US95 / 07823, W095 / 27772, W095 / 27773, W095 / 27774 and W096 / 27775. The hydrogen peroxide may also be present by adding an enzyme system (ie, an enzyme and therefore a substrate) which is capable of generating hydrogen peroxide at the beginning and where the washing and / or rinsing process is carried out. Such enzymatic systems are set forth in patent application EP 91202655.6 filed on October 9, 1991. Catalysts containing metal for use bleaching compositions, include catalysts including cobalt such as cobalt (III) salts of pentamine-acetate * and manganese containing catalysts such as described in EPA 549 271; EPA 549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US 5,114,644. A bleaching composition comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent is described in patent application No. 948702206.3. Bleaching agents other than oxygen bleaching agents and which can be used herein are also known in the art. One type of oxygen free bleaching agent of particular interest includes photoactivated bleaching agents such as zinc phthalocycins and / or sulfonated aluminum. These materials can be deposited on the substrate during the washing process. By irradiation with light, in the presence of oxygen, for example by hanging clothes outside to dry in daylight, the suftenated zinc phthalocyanine is activated and, consequently, the substrate is bleached. The preferred zinc phthalocyanine and a photoactivated bleaching process are described in the U.S.A. 4,033,718. Typically, the detergent compositions will contain from about 0.025% to about 1.25%, by weight, of the sulfonated zinc phthalocyanine.

Builder System The compositions of the present invention may further comprise a builder system. Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxilicates, alkylalkenyl succinic acid and fatty acids, materials such as ethylenediaminetetraacetate, diethylenetriaminpentamethylenacetate, metal ion sequestrants such as aminophosphonates, particularly ethylenediaminetetramethylenephosphonic acid and acid. diethylenetriaminpentamethylenephosphonic. Phosphate builders can also be used herein. Suitable builders may be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as zeolite A, X, B, HS or hydrated MAP. Another suitable inorganic builder material is layered silicate, for example SKS-6 (Hoechst). SK-6 is a crystalline statified silicate consisting of sodium silicate (Na2Si2? _5). Suitable polycarboxylates containing a carboxy group include lactic acid, glycolic acid and ether derivatives thereof as set forth in Belgian patents Nos. 831,368, 821,369 and 821,370. Carboxylates containing two carboxy groups include the water-soluble salts of succinic acid, malonic acid, ethylenedioxydiacetic acid, maleic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid, as well as other ether carboxylates described in German Patents 2,446,686, and 2,446,687 and the patent of * E.U.A. No. 3,935,257, and the sulfonyl caboxylates described in Belgian Patent No. 3,935,257. The carboxylates containing three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconates as well as succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1,379,241, the lactoxysuccinates described in Dutch Application 7205873 and the oxypolycarboxylate materials such as 2-oxa-l, 1, 3-polypanadricarboxylates described in British Patent No. 1,387,447. Polycarboxylates containing four carboxy groups include the oxydisuccinates described in British Patent No. 1,261,829,1,1,2,2-ethanetenetecorboxylates. 1, 1, 3, 3-propanotetraorboxylates and 1, 2, 1, 3-propanotetracarboxylates. Polycarboxylates containing sulfo substituents including sulfosuccinate derivatives described in British Patent Nos. 1,398,421 and 1,398,422 and in the US patent. No. 3,936,448, and the sulfonated pyrolysed sulfonates described in British Patent No. 1, 082,179, while exposing the caboxylates containing phosphone substituents of British Patent No. 1,439,000. The alicyclic and heterocyclic polycarboxylates include cyclopentane-cis, cis, cis-tetracarbocylates, cyclopentadiene-pentacarboxylates, 2,3,4,5-tetrahydrofuran-cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan-cis- dicarboxylates, 2,2,5,5-tetrahydrofuran-tetracarboxylates, 1, 2, 3, 4, 5, 6-hexanohexacarboxylates and carboxymethyl derivatives of 'polyhydric alcohols such as sorbitol, mannitol and xylitol.

Aromatic polycarboxylates include the melitic acid, pyromellitic acid and phthalic acid derivatives set forth in British Patent No. 1,425,343. Of the above, the preferred polycarboxylates are hydroxycarboxylates containing up to three carboxy groups per molecule, more particularly citrates. Preferred builder systems for use in the present compositions include a mixture of a water insoluble aluminosilicate builder such as zeolite A or a layered silicate (SKS-6) and a water soluble carboxylate chelating agent such as acid citric. Preferred builders systems for use in liquid detergent compositions of the present invention are soaps and polycarboxylates. A suitable chelating agent for inclusion in the detergent compositions according to the invention is ethylenediamine-N, N 'disuccinic acid or salts of alkali metals, alkaline earth metals, ammonium or substituted ammonium thereof or mixtures thereof. The preferred EDDS compounds are the free acid form and the sodium or magnesium salt thereof. Examples of such preferred sodium salts of EDDS include Na2EDDS and Na4EDDS. Examples of such preferred magnesium salts of EDDS include MgEDDS and Mg2EDDS. Magnesium salts are most preferred for inclusion in the compositions according to the invention. * Preferred builder systems include a mixture of a water insoluble aluminosilicate builder such as zeolite A and a water soluble carboxylate chelating agent such as citric acid. Other detergency builder materials that can be part of the builder system for use in granular compositions include inorganic materials such as carbonates, bicarbonates, silicates, and organic materials such as phosphonates, aminopoly-alkylene-phosphonates, and aminopolycarboxylates.

Other suitable water-soluble organic salts are homo- or copolymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from one another by not more than two carbon atoms. The polymer of this type is exposed in GB-A-1, 596, 756. Examples of such salts are polyacrylates with MW of 2000-5000 and their copolymers with maleic anhydride, such as copolymers having a molecular weight of 20,000 to 70,000, especially about 40,000. The best detergent salts are usually included in amounts of 5% to 80% by weight of the composition, preferably 10% to 70% and most usually 30% to 60% by weight.

Foam suppressor Another optional ingredient is a foam suppressant, exemplified by silicones and silica / silicone blends. Silicones can be represented generally by alkylated polysiloxane materials while silicas are normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. These materials can be incorporated as particulate materials in which the foam suppressor is advantageously incorporated in a releasable manner in a water-soluble or water-dispersible detergent vehicle, substantially non-surfactant.

Alternatively, the foam suppressant can be dissolved or dispersed in a liquid vehicle and applied by spraying on one or more of the other components. A preferred silicone foaming agent is disclosed, in Bartollota et al., U.S. Pat. 3 933 672. Other particularly useful foam suppressors are self-emulsifying silicone foam suppressors, described in the German patent application DTOS 2 646 126 published April 28, 1977. An example of such a compound is DC-544, commercially available from Dow Corning, which is a siloxane-glycol copolymer. The especially preferred foaming agent is the foam suppressor system comprising a mixture of silicone oil and 2-alkylalkanols. The suitable 2-alkylalcanol is 2-butyloctanol which is commercially available under the factory name of Isofol 12 R. Such a foam suppressor system is described in European Patent Application No. 92870174.7, filed on November 10, 1992. Particularly preferred silicone foam controlling agents are described in European Patent Application No. 92201649.8. Such compositions may comprise a mixture of silicone / silica in combination with fumed non-porous silica such as Aerosil. The foam suppressors described above are usually employed at levels from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight.

Other components Other components used in the detergent compositions may be employed, such as soil suspending agents, soil release agents, optical brighteners, abrasives, bactericides, bleaching inhibitors, coloring agents and / or encapsulated or unencapsulated perfumes. Particularly suitable encapsulating materials are water-soluble capsules consisting of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1,464,616. Other suitable water-soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid-esters of substituted dicarboxylic acids such as are described in US 3,455,838. These are prepared * acid-ester dextrins, preferably, from starches such as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of such encapsulating materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified corn starch and glucose. The starch is modified by adding polyfunctional substituted groups such as octenylsuccinic acid anhydride. Suitable antiredeposition and soil suspending agents herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or copolymeric polycarboxylic acids or salts thereof. Polymers of this type include the polyacrylates and the maleic anhydride-acrylic acid copolymers previously mentioned as detergency builders, as well as copolymers of maleic anhydride with ethylene, methyl vinyl ether or methacrylic acid, constituting maleic anhydride at least 20% by weight. mol of the copolymer. These materials are normally used at levels of 0.5% to 10% by weight, more preferably 0.75% to 8%, more preferably still 1% to 6% by weight of the composition. Preferred optical brighteners are of anionic character, examples of which are 4,4'-bis- (2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate disodium, , 4'-bis- (2-mofolino-4-anilino-s-triazin-6-ylamino-stilbene-2, 2'-disodium disodium 4,4'-bis- (2,4-dianilino-s-triazin) -6-ylamino) stilbene-2, 2 '- * monosodium disulfonate, 4', 4"-bis- (2,4-dianilino-s-tri-azin-6-ylamino) stilbene-2-sulfonate disodium , 4,4'-bis- (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylamino) -stilbene-2,2'-disodium disulfonate, 4.4 '-bis- (4-phenyl-2, 1, 3-triazol-2-yl) -stilbene-2, 2'-disodium disulfonate, 4,4' bis (2-anilino-4- (1-methyl- 2-hydroxyethylamino) -s-triazin-6-ylamino) -stilbene-2,2'-disodium disulfonate, 2 (stilbil-4"- (naphtho- 1 ', 2': 4,5) -l, 2, 3-triazole-2 • '-sulfonate sodium and 4,4'-bis (2-sulfostyril) biphenyl The highly preferred brighteners are the brighteners specific to the European patent application No. 95201943.8.

Other useful polymeric materials are polyethylene glycols, particularly those with a molecular weight of 1,000-10,000, more particularly from 2,000 to 8,000, and most preferably about 4,000. These are used at levels of 0.20% to 5%, more preferably 0.25% to 2.5% by weight. These polymers and the homo- or copolymeric polycarboxylate salts mentioned above are valuable for improving the maintenance of whiteness, the deposition of ash in the fabric and the cleaning performance on clay, protein and oxidisable soils in the presence of metal impurities of transition. The soil release agents useful in the compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and / or propylene glycol units in various distributions. Examples of such polymers are set forth in the U.S.A. Nos. 4116885 and 4711730, commonly assigned, and published European patent application No. 0 272 033. A particular preferred polymer in accordance with EP-A-0 272 033 has the formula (CH3 (PEG) 43) 0.75 (pOH) or .25 - (T-PO) 2.8 (T-PEG) -0.4] T (PO- H) 0.25 ((PEG) 43CH-3) 0.75 where PEG is - (OC2H4) 0-PO is (OC3HgO) and T is (pcOCgH4CO). Also highly useful are polyesters polyesters such as random copolymers of dimethylterephthalate, dimethylsulfoisophthalate, ethylene glycol and 1,2-propanediol, the end groups consisting primarily of sulfonbenzoate and secondarily of monoesters of ethylene glycol and / or propanediol. The objective is to obtain a polymer blocked at both ends by sulfobenzoate groups; "Primordially", in the present context most of said copolymers herein will be blocked at the ends by the sulfobenzoate groups. However, some copolymers will be less than completely blocked and therefore the end groups may consist of monoesters of ethylene glycol and / or popane-1,2-diol, of which they consist "secondarily" in such species. The polyesters mentioned herein contain about 46% by weight of dimethylterephthalic acid, about 16% by weight of propane-1,2-diol, about 10% by weight of ethylene glycol, about 13% by weight of methylsulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and has a molecular weight of about 3,000. The polyesters and their method of preparation are described in detail in EPA 311 342. It is well known in the art that free chlorine from the tap water rapidly deactivates the enzymes comprised in the detergent compositions. Therefore, using chlorine scrubber such as perborate, ammonium sulfate, sodium sulfite or polyethyleneimine with a level greater than 0.1% by weight of the total composition, in the formulas, will provide improvement through the washing stability of the detergent enzymes. The compositions comprising chlorine scavenger are described in European patent application 92870018.6 filed on January 31, 1992. The polymerized alkoxylated polycarboxylates, such as those prepared from polyacrylate, are useful herein. poveer additional performance in the elimination of fat. Such materials are described in WO 91/08281 and PCT 90/07815 on page 4 and the following, incorporated herein by reference. Chemically, these materials comprise polyacrylates that have a side chain of ethoxy for every 7 and 8 acrylate units. The side chains are of the formula - (CH2CH2O) m (CH2) nCH3 where m is 2-3 and n is 6- 12. The side chains are linked with esters to the 5"base structure" of polyacrylate to provide a 1 structure of polymer type "comb". The molecular weight may vary, but is typically in the range of about 2,000 to about 50,000. Such benzylated polycarboxylates may comprise from about 0.05% to about 10%, by weight, of the compositions herein.

Fabric softening agents Fabric softening agents can be incorporated into laundry detergent compositions in accordance with the present invention. These agents may be of inorganic or organic type. Inorganic softening agents are exemplified with the smectite arecillas exposed in GB-A-1 400 898 and USP 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines which are disclosed in GBA-A1 514 276 and EP-BO 011 340 and their combination with quaternary ammonium momosales of c12_14 are disclosed in EP-BO 026 527 and EP- BO 026 528 and the dilarga chain amides are disclosed in EP-BO 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0 313 146. Smectite clay levels are usually in the range of 2% to 20%, more preferably 5% to 15% by weight, the material being added as a dry mixed component to the remainder of the formulation. Other organic fabric softening agents such as water insoluble tertiary amines or dilarga chain amide materials are incorporated at levels of 0.5% to 5% by weight, normally from 1% to 3% by weight while adding high molecular weight polyethylene oxide materials and water-soluble cationic materials at levels of 0.1% to 2%, usually from 0.15% to 1.15% by weight. These materials are usually added to the spray-dried portion of the composition, although in some cases it may be more convenient to add them as dry mixed material in the form of particles or sprinkle them as molten liquid over the other solid components of the composition.

Dispersants The detergent composition of the present invention may also contain dispersants: suitable water-soluble organic salts are homo- or copolymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from one another by no more than two carbon atoms. Polymers of this type are disclosed in GB-A-1,596, 756. Examples of such salts are polyacrylates with MW of 2000-5000 and copolymers with maleic anhydride, such copolymers having a molecular weight of 1,000 to 100,000. Especially, in the detergent compositions of the present invention, acrylate and methacrylate copolymers such as 480N having a molecular weight of 4000, at a level of 0.5 to 20% by weight of the composition can be added. The compositions of the invention may contain a lime soap peptising compound, having a lime soap dispersing power (LSDP), as hereinafter defined to be no more than 8 preferably no more than 7, more preferably no more of 6. The lime soap peptizer compound is preferably present at a level of 0% to 20% by weight. A numerical measure of the effectiveness of the lime soap peptizer is given by the lime soap dispersing power (LSDP) which is determined using the lime soap dispersant test, as described in an H.C. Borghetty and C.A. Bergman, J. Am. Oil. Chem. Soc., Volume 27, pages 88-90, (1950). This method of testing the dispersion of lime soap is used extensively by spatialists in this field of art who are referred to, * _ "5 for example, in the following articles of specialized journals: WN Linfield, Surfactant science Series, Volume 7, page 3: WN Linfield, Tenside surfing, volume 27, pages 159-163, (1990), and MK Nagarajan, WF Masler, Cosmetics and Toiletries, volume 104, pages 71-73, (1989) The 0 LSDP is the ratio of percent by weight of the dispersing agent to the sodium oleate required to disperse the lime soap deposits formed by 0.025. g of sodium oleate in 30 ml of water with an equivalent hardness of 333 ppm of CaC 3 (Ca.-Mg = 3: 2) Surfactants having a good capacity for lime soap peptising will include certain amine oxides, 1 betaines, sulfobetaines, alkyl ethoxysulfate and ethoxylated alcohols Exemplary surface active agents having an LSDP of not more than 8 for use in accordance with the present invention include dimethylamine oxide of C gC 8 C 2 -C 18 alkyl ethoxy sulfates with a medium degree of ethoxylation of 1 to 5, particularly C12-C15 ethoxy sulfate surfactant with an ethoxylation degree of about 3 (LSDP = 4) and C 4-5 C15 ethoxylated alcohols with an average degree of ethoxylation of either 12 (LSDP = 6) or 30, sold under the factory names of Lutensol A012 and Lutensol A030 respectively, by BASF GmbH. Polymeric lime soap peptizers suitable for use herein are described in the article by Nagarajan, W.F. Masier, which is in Cosmetics and Toiletries, volume 104, pages 71-73, (1989). They can also be used, as lime soap peptizer compounds, hydrophobic bleaches such as 4- [N-octanoyl-6-aminohexanoyl] benzenesulfate, 4- [N-nonanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-decanoyl- 6-aminohexa-noyl] benzenesulfonate, and mixtures thereof; and nonanoyloxybenzenesulfonate together with hydrophilic / hydrophobic bleach formulations.

Inhibition of dye transfer The detergent compositions of the present invention can include compounds for inhibiting the transfer of dyes from one fabric to another, of solubilized or suspended dyes that are encountered during fabric washing operations involving colored fabrics.

Polymeric Dye Transfer Inhibitory Agents The detergent compositions according to the present invention also comprise from 0.001% to 10%, preferably from 0.01% to 2%, more preferably from 0.05% to 1% by weight of agents. polymeric dye transfer inhibitors. Such polymeric dye transfer inhibiting agents are normally incorporated into the detergent compositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability to form complexes or absorb the fugitive centers released in the washing of the dyed fabrics before the dyes have the opportunity to be fixed to other articles in the wash. Especially suitable dye transfer inhibiting polymeric agents are polymers of polyamine N-oxide, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polymers of polyvinylpyrrolidone, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. The addition of such polymers also enhances the performance of the enzymes according to the invention.

Polyamine N-oxide polymers Polyamine N-oxide polymers suitable for use contain units having the following structure formula: (1) A X R wherein P is a polymerizable unit, to which the group R-N-O may be linked or wherein the group R-N-O forms part of the polymerizable unit or a combination of both. 0 0 0 A is NC, CO, C II, -0-, -SII-, -NII-; x is 0 or 1; R are aliphatic, aliphatic, ethoxylated, aromatic, heterocyclic or alicyclic groups or any combination thereof to which the nitrogen of the N-O group may be linked or in which the nitrogen of the N-O group is part of these groups. The N-O group can be represented by the following structures: O O I I (Rl) x-N- (R2) y = N- (Rl) X (R3) z wherein R 1, R 2, and R 3 are aliphatic, aromatic, heterocyclic or alicyclic groups or combination thereof, xo / y Y or / and z is 0 or 1 and wherein the nitrogen of the NO group can be linked or where the nitrogen The group is NOT part of these groups. The N-O group can be part of the polymerizable unit (P) or it can be linked to the polymeric base structure or a combination of both. The N-O suitable polyamine oxides wherein the N-O group forms part of the polymerizable unit comprises N-oxide polyamines in which R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups. A class of said polyamine N-oxides comprises the group of polyamine N-oxides in which the nitrogen of the NO forms part of the group R. The preferred polyamine N-oxides are those in which R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof. Another class of said polyamine N-oxides comprises the group of polyamine N-oxides in which the nitrogen of the NO group is linked to the R group. Other suitable polyamine N-oxides are the polyamine acids in which the NO group it is linked to the polymerizable unit. Preferred classes of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R are aromatic, heterocyclic or alicyclic groups in which the nitrogen of the functional group NO is part of said group R Examples of these classes are polyamine oxides in which R is a heterocyclic compound such as pyridine, pyrrole, imidazole and derivatives thereof. Another preferred class of N-polyamine oxides are the polyamine oxides having the general formula (I) wherein R are aromatic, heterocyclic or alicyclic groups in which the nitrogen of the functional group is NOT linked to said R groups. of these classes are the polyamine oxides in which the R groups can be aromatic such as phenyl. Any polymer base structure can be used as long as the formed amine oxide polymer is water soluble and has dye transfer inhibiting properties. Examples of polymeric base structures are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates and mixtures thereof. The amine N-oxide polymers of the present invention typically have a ratio of amine to amine N-oxide from 10: 1 to 1: 1,000,000. However, the amount of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymerization or by an appropriate degree of N-oxidation. Preferably, in the ratio of the amine to the amine N-oxide is from 2: 3 to 1: 1,000,000, more preferably from 1: 4 to 1, 1,000,000, more preferably from 1: 7 to 1: 1,000,000. The polymers of the present invention actually encompass random or block copolymers in which one type of monomer is an amine N-oxide of another type of monomer or is an amine N-oxide or not. The amine oxide unit of the polyamine N-oxides has a PKa <; 10, preferably PKa < 7, more preferably PKa < 6. Polyamine oxides can be obtained in almost any degree of polymerization. The degree of polymerization is not critical as long as the material has the water solubility and the suspension potency in desired dyes. Typically, the average molecular weight is within the range of from 500 to 1,000,000, preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000, more preferably even from 3,000 to 20,000. b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole The polymers of N-vinylimidazole and N-vinylpyrrolidone used in the present invention have a range of average molecular weights of 5000-1,000,000, preferably 5000-200,000. Highly preferred polymers for use in the detergent compositions according to the present invention comprise a polymer selected from copolymers of N-vinylimidazole and N-vinylpyrrolidone in which said polymer has a range of average molecular weights of from 5,000 to 50,000, more preferably from 8,000 to 30,000, more preferably even from 10,000 to 20,000. The range of average molecular weights per light diffusion was determined as described by Barth H.G. and Mays J.W., Chemical Analysis Vol 113, "Modern Methods of Polymer Characterization". The highly preferred N-vinylimidazole and N-vinylpyrrolidone copolymers have a range of average molecular weights of from 5,000 to 50,000; more preferably from 8,000 to 30,000; more preferably from 10,000 to 20,000. The copolymers of N-vinylimidazole and N-vinylpyrrolidone characterized in that they have said range of average molecular weights provide excellent dye transfer inhibition properties while not adversely affecting the cleaning performance of the detergent compositions formulated therewith. The copolymer of N-vinylimidazole and N-vinylpyrrolidone of the present invention have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, more preferably from 0.8 to 0.3, more preferably from 0.6 to 0.4. c) Polyvinylpyrrolidone The detergent compositions of the present invention can also use polyvinylpyrrolidone ("PVP") having an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000 and more preferably still from about 5,000 to about 15,000. Suitable polyvinyl pyrrolidones are commercially available from ISP Corporation, New York, NY and Montreal, Canada under the product names PVP K-15 (molecular weight with viscosity of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K -60 (average molecular weight of 160,000) and PVP K-90 (average molecular weight of 360,000). Other suitable polyvinyl pyrrolidones which are commercially obtainable from BASF Cooperation include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones known to those skilled in the detergent field (see for example EP-A-262,897 and EP-A-256,696). d) Polyvinyloxazolidone The detergent compositions of the present invention can also use polyvinyloxazolidone as the polymeric agent of the dye transfer division. Said polyvinyloxazolidones have an average molecular weight of from about 2,500 to about 40,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000 and more preferably even from about 5,000 to about 15,000. e) Polyvinylimidazole The detergent compositions of the present invention can also use polyvinylimidazole as a polymeric agent for inhibiting dye transfer. Said polyvinylimidazoles have an average of about 2,500 to about 400,000, preferably about 5,000 to 200,000, more preferably about 5,000 to about 50,000 and more preferably still about 5,000 to about 15,000. f) Interlaced polymers Interlaced polymers are polymers whose base structure is interconnected to a certain degree; these links may be of a chemical or physical nature, possibly with an active group n in the base structure or on the branches; the entangled polymers have been described in Journal of Polymer Science, volume 22, pages 1035-1039. In one embodiment, the entangled polymers are made in such a way that they form a rigid three-dimensional structure, which can trap dyes in the pores formed by the three-dimensional structure. In another embodiment, the entangled polymers trap the dyes by swelling. Such entangled polymers are described in patent application 94870213.9.

Washing Method The compositions of the invention can be used essentially in any washing or cleaning method, including soaking methods, pre-treatment methods and methods with rinsing steps for which a separate auxiliary rinsing composition can be added. The process described herein comprises contacting the fabrics with a washing solution in the usual manner and exemplified herein. The method of the invention is conveniently carried out during the course of the cleaning process. The cleaning method is preferably carried out at 5 ° C and up to 95 ° C, especially between 10 ° C and 60 ° C. The pH of the treatment solution is preferably from 7 to 11. The following examples are intended to exemplify compositions of the present invention, but are not necessarily intended to limit or otherwise define the scope of the invention. In the detergent compositions, the level of enzymes is expressed in pure enzyme by weight of the total composition and the identifications of the abbreviated components have the following meanings: LAS: Sodium linear C 2 alkylbenzene sulphonate TAS: sodium tallow alkyl sulphate CXYAS: Alkylsulfate of C? of C ?? of sodium 25EY: A predominantly linear primary alcohol of C ^ -C ^ s condensed with an average of Y moles of ethylene oxide CXYEZ A predominantly linear primary alcohol of C] _? - C? _? condensed with an average of Z moles of ethylene oxide XYEZS Alkyl Sulfate of Ct _? - C] _? of sodium condensed with an average of Z moles of ethylene oxide per mole QAS R2. + (CH3) 2 (C2H4OH) with R2 = C12-C1 Sodium linear alkylcarboxylate soap derived from an 80/20 mixture of tallow and coconut oils TFAA Alkyl-N-methylglucamide from Ci-Cis- TPKFA C12-C14 full-cut, crowned fatty acids.

DEQA Di- (tallowoxyethyl) dimethylammonium chloride.

SDASA 1: 2 ratio of steryl dimethyl amine: triple-compressed stearic acid.

Neodol 45-13 Ethoxylated C 4 -C 15 linear primary alcohol, sold by Shell Chemical CO.

Silicato amorphous sodium silicate (Si? 2: Na2 < - > = 2.0 ratio) NaSKS-6 Crystallized statified silicate of the formula delta-Na2SÍ2? 5.

Carbonate Anhydrous sodium carbonate with a particle size between 200μm and 900μm.

Bicarbonate Anhydrous sodium bicarbonate with a particle size between 400μm and 1200μm.

STPP Anhydrous sodium tripolyphosphate.

MA / AA Copolymer of maleic / acrylic acid at 1: 4, an average molecular weight of approximately 80,000.

Polyacrylate Polyacrylate homopolymer with an average molecular weight of 8,000, sold under the factory name PA30 by BASF GmbH.

Zeolite A Hydrated sodium aluminosilicate of the formula Na12 (A10 SiO2) 12 • 27H20 having a primary particle size in the range of 0.1 to 10 microns.

Citrate trisodium citrate dihydrate with activity of 86.4%, with a particle size distribution between 425. μm and 850 μm.

Citrus anhydrous citric acid.

PB1 Anhydrous sodium perborate bleach monohydrate, empirical formula NaB? 2-H2? 2.

PB4 Sodium perborate anhydrous tetrahydrate Percarbonate Anhydrous sodium percarbonate bleach of the empirical formula 2Na2C? 3.3H2? 2.

TAED Tetraacetylethylenediamine.

NOBS: Nonanoiloxybenzenesulfonate in the form of sodium salt.

Photoactivated bleach: Sulfonated zinc phthalocyanine encapsulated in dextrin-soluble polymer.

Antibody Antibody directed against an enzyme in accordance with the present invention.

Protease Proteolytic enzyme sold under the trade names Savinasa, Alcalasse, Durazim by Novo Nordisk A / S, Maxacal, Maxapem, Properase sold by Gist-Brocades and the proteases described in patents WO91 / 06637 and / or WO95 / 10591 and / or EP 251 446.

Amylase Aminolytic enzyme sold under the trade name Ox Am described in WO 94/18314, WO96 / 05295 sold by Genencor; Termamil, Fungamil • p and Duramil, all obtainable from Novo Nordisk A / S and those described in W095 / 26397.

Lipase Lipolytic enzyme sold under the factory name Lipolasa, Lipolasa Ultra by Novo Nordisk A / S.

Cellulase Cellulite enzyme sold under the factory name Carezime, Celluzime and / or Endolasa by Novo Nordisk A / S.

CMC Sodium-carboxymethylcelluloses.

HEDP 1, 1-hydroxyethanediphosphonic acid DETPMP Diethylenetriaminpenta (methylene phosphoric acid), sold by Monsanto under the factory name Dequest 2060.

PVNO Poly (4-vinylpyridine) -N-oxide.

PVPVI Poly (4-vinylpyridine) -N-oxide / copolymer of vinylimidazole and vinylpyrrolidone.

Rinse aid 1 Disodium-4, 4 '-bis (2-sulfostyril) biphenyl. 2-Disodium-4,4-bis (4-anilino-6-morpholino-1,3,5-triazin-2-yl) stilbene-2: 2'-disulfonate brightener.

Silicone antifoams Polydimethylsiloxane foam controller with siloxane-oxyalkylene copolymer as a dispersing agent with a ratio of said foam controller to said dispersing agent from 10: 1 to 100: 1. 12% silicone / silica granulated spupresor, 18% stearyl alcohol foam, 70% granular starch.

SRP 1 esters blocked at the ends of sulfobenzoyl with base structure of oxyethyleneoxytephthaloyl.

SRP 2 Short block polymer of poly (1, 2 -propikenteraphthalate) diethoxylate.

Sulfate Anhydrous sodium sulfate.

HMWPEO: High molecular weight polyethylene oxide.

PEG Polyethylene glycol.

Encapsulated particle Fragrance-insoluble fragrance dispensing technology Zeolite 13x perfume and a binder agglomerator detrusor / glycerin is used.

EXAMPLE 1 Production of antibodies: 1 ml of a 1 mg / ml emulsion of Savinase or Alcalase was injected into the muscle of the chicken breast. The proteolytic emulsion was prepared with a completed Freunds adjuvant (Freund and McDermott, 1942; Freund 1956), by intensively mixing an equal amount of Savmase or Alcalase® solution (2 mg / ml) and complete Freunds adjuvant. The immunization schedule ended with injections using an incomplete Freunds adjuvant, and after a period of 4 weeks, the eggs were collected for a week. The extraction of the antibodies from the egg yolk was done in accordance with the Polson extraction method, as described in Immunological Investigation 19, 1990, pp 253-258.

Enzymatic Protease Inactivation: A supply solution of p p Savmase or Alcalase was prepared in a Tris pH regulator (Tris at 5x10 2M, NaCl at 25 mM, pH = 8) at a concentration of 0.05% of active enzyme. A pH phosphate buffer (KH2P04 at 0.05 M, pH 6.8) contained the antibody (0.18 mg / ml). The interaction of the proteolytic enzyme (final concentration of 0.004%) / antibody in commercially available detergent solutions comprising liquid Ariel (0.8% in city water, pH 8.5) and Ariel Color Futur (0.8% in city water) was achieved. , pH 9.5) for 15 minutes at 40 ° C. Residual proteolytic activity was measured according to the method described in Delmar et al. (1979) Anal. Biochem. 99, pp 316-320. During 5 minutes, the enzymatic activity of the protease was successfully blocked, as shown in the following table.

RESIDUAL PROTEOLIC ACTIVITY (in% after 5 minutes) EXAMPLE 2 The following laundry detergent compositions according to the invention were prepared: I II III IV V VI LAS 8.0 8.0 8.0 8.0 8.0 8.0 C25E3 3.4 3.4 3.4 3.4 3.4 3.4 QAS - 0.8 0.8 - 0.8 0.8 Zeolith A 18.1 18.1 18.1 18.1 18.1 18.1 Carbonate 13.0 13.0 13.0 27.0 27.0 27.0 Silicate 1.4 1.4 1.4 3.0 3.0 3.0 Sulfate 26.1 26.1 26.1 26.1 26.1 26.1 PB4 9.0 9.0 9.0 9.0 9.0 9.0 TAED 1.5 1.5 1.5 1.5 1.5 1.5 DETPMP 0.25 0.25 0.25 0.25 0.25 0.25 HEDP 0.3 0.3 0.3 0.3 0.3 0.3 EXAMPLE 2 (CONTINUED) Amylase 0.0009 0.0009 0.0009 0.0009 0.0009 0.0009 Protease 0.15 0.005 0.004 0.002 0.001 0.1 Antibody 0.5 0.01 0.1 0.01 0.001 1.0 MA / AA 0.3 0.3 0.3 0.3 0.3 0.3 CMC 0.2 0.2 0.2 0.2 0.2 0.2 Bleach 15 15 15 15 15 15 photoactivated (ppm) Brightener 0.09 0.09 0.09 0.09 0.09 0.09 Perfume 0.3 0.3 0.3 0.3 0.3 0.3 Antifoams 0.5 0.5 0.5 0.5 0.5 0.5 silicone Various / minor ingredients for 100% Density in 850 850 850 850 850 850 g / liter EXAMPLE 3 The following granular laundry detergent compositions having a bulk density of 750 g / liter were prepared according to the invention: I II III LAS 5.25 5.61 4.76 TAS 1.25 1.86 1.57 C45AS - 2.24 3.89 EXAMPLE 3 (CONTINUED) C25AE3S 0.76 1.18 C45E7 3.25 - 5.0 C25E3 - 5.5 - QAS 0.8 2.0 2.0 STPP 19.7 - - Zeolite A - 19.5 19.5 NaSKS-6 / acid (citric acid (79: 21) - 10.6 10.6 Carbonate 6.1 21.4 21.4 Bicarbonate - 2.0 2.0 Silicate 6.8 - - Sulfate of 3? Dio 39.8 - 14.3 PB4 5.0 12.7 - TAED 0.5 3.1 - DETPMP 0.25 0.2 0.2 HEDP - 0.3 0.3 Antibody 0.01 0.1 1.0 Protease 0 .0026 0.0085 0.08 Lipasa 1 3.003 0.003 0.003 Cellulase 0 .00064 0.00064 0.00064 Amylase 0.0009 0.0009 0.0009 MA / AA 0.8 1.6 1.6 CMC 0.2 0.4 0.4 Bleach photoact: ivado (ppm) 15 27 27 Rinse aid 1 0.08 0.19 0.19 EXAMPLE 3 (CONTINUED) Rinse aid 2 - 0.04 0.04 Perfume particles 0.3 0.3 0.3 Silicone antifoams 0.5 2.4 2.4 Minor / various components up to 100% EXAMPLE 4 The following detergent formulations were prepared, in accordance with the present invention, wherein I is a detergent composition containing phosphorus, II is a detergent composition containing zeolite and III is a compact detergent composition: II III Blown powder STPP 24.0 - 24.0 Zeolite A - 24.0 - C45AS 9.0 6.0 13.0 MA / AA 2.0 4.0 2.0 LAS 6.0 8.0 11.0 TAS 2.0 - - Silicate 7.0 3.0 3.0 CMC 1.0 1.0 0.5 Brightener 2 0.2 0.2 0.2 EXAMPLE 4 (CONTINUED) Soap 1.0 1.0 1.0 DETPMP 0.4 0.4 0.2 Application by sprinkling C45E7 2.5 2.5 2.0 C25E3 2.5 2.5 2.0 Silicone antifoams 0.3 0.3 0.3 Perfume 0.3 0.3 0.3 Dry additives Carbonate 6.0 13.0 15.0 PB4 18.0 18.0 10.0 PB1 4.0 4.0 0 TAED 3.0 3.0 1.0 Photoactivated bleach 0.02 0.02 0.02 Protease 0.01 0.002 0.05 Lipase 0.009 0.009 0.009 Amylase 0.002 0.003 0.001 Antibody 0.03 0.03 0.5 Sodium sulphate mixed 3.0 3.0 5.0 Dry rest (humidity e 100.0 100.0 100.0 various ingredients) Density (g / liter) 630 670 670 EXAMPLE 5 The following detergent formulations that do not contain bleach of particular use were prepared in the laundry of color laundry, in accordance with the present invention: I II III blown Zeolite A 15.0 15.0 Sodium sulphate 0.0 5.0 LAS 3.0 3.0 DETPMP 0.4 0.5 CMC 0.4 0.4 MA / AA 4.0 4.0 Agglomerates C45AS - - 11.0 LAS 6.0 5.0 - TAS 3.0 2.0 - Silicate 4.0 4.0 - Zeolite A 10.0 15.0 13.0 CMC - - 0.5 MA / AA - - 2.0 Carbonate 9.0 7.0 7.0 Spray application Perfume 0.3 0.3 0.5 EXAMPLE 5 (CONTINUED) C45E7 4.0 4.0 4.0 C25E3 2.0 2.0 2.0 Dry additives MA / AA - - 3.0 NaSKS-6 - - 12.0 Citrate 10.0 - 8.0 Bicarbonate 7.0 3.0 5.0 Carbonate 8.0 5.0 7.0 PVPVI / PVNO 0.5 0.5 0.5 Protease 0.05 0.03 0.007 Lipase 0.009 0.009 0.009 Amylase 0.005 0.005 0.005 Cellulase 0.0014 0.0014 0.0014 Antibody 0.8 0.1 0.2 Silicone antifoams 5.0 5.0 5.0 dry itivos Sodium sulfate 0.0 9.0 0.0 Rest (moisture e 100.0 100.0 100.0 various ingredients) Density (g / liter) 700 700 700 EXAMPLE 6 The following detergent formulations were prepared, in accordance with the present invention: I II III IV LAS 20.0 14.0 24.0 22.0 QAS 0.7 1.0 - 0.7 TFAA - 1.0 - - C25E5 / C45E7 - 2.0 - 0.5 C45E3S - 2.5 - - STPP 30.0 18.0 30.0 22.0 Silicate 9.0 5.0 10.0 8.0 Carbonate 13.0 7.5 - 5.0 Bicarbonate - 7.5 - - DETPMP 0.7 1.0 - - SRP 1 0.3 0.2 - 0.1 MA / AA 2.0 1.5 2.0 1.0 CMC 0.8 0.4 0.4 0.2 Protease 0 .08 0.002 0.02 0 .005 Amylase 0 .007 0.004 - .002 Lipasa 0 .004 0.002 0.004 0 .002 Cellulase 0. 0004 0.0001 - - Antibody 0.3 0.16 0.2 0 .01 Bleach 70 ppm 45 ppm - 10 ppm photoactivated (ppm) EXAMPLE 6 (CONTINUED)Rinse aid 1 0.2 0.2 0.08 0.2 PB1 6.0 2.0 NOBS 2.0 1.0 Rest (humidity e 100 100 100 100 diverse ingredients) EXAMPLE 7 The following detergent formulations were prepared in accordance with the present invention: II III IV Blown powder Zeolite A 30.0 22.0 6.0 6.7 Na SKS-6 - - - 3.3 Polycarboxylate - - - 7.1 Sodium Sulfate 19.0 5.0 7.0 - MA / AA 3.0 3.0 6.0 - LAS 14.0 12.0 22.0 21.5 C45AS 8.0 7.0 7.0 5.5 Surfactant _ _ _ 1.0 Cationic Silicate - 1.0 5.0 11.4 Soap - - 2.0 - Brightener 1 0.2 0.2 0.2 _ EXAMPLE 7 (CONTINUED) Carbonate 8.0 16.0 20.0 10.0 DETPMP - 0.4 0.4 Application by sprinkling C45E7 1.0 1.0 1.0 3.2 Dry Additives PVPVI / PVNO 0.5 0.5 - Antibody 0.2 0.09 0.15 0.05 Protease 0.053 0.01 0.005 0.01 Lipase 0.009 0.009 0.009 0.009 Amylase 0.0008 0.0008 0.0008 0.0008 Cellulase 0.0002 0.0002 0.0002 0.0002 NOBS - 6.1 4.5 3.2 PB1 1.0 5.0 6.0 3.9 Sodium Sulfate - 6.0 - for the rest Rest (humidity 100 100 100 100 different ingredients) EXAMPLE 8 The following high density and bleach-containing detergent formulations were prepared in accordance with the present invention: II III Blown powder Zeolite A 15.0 15.0 15.0 Sodium sulphate 0.0 5.0 0.0 LAS 3.0 3.0 3.0 QAS - 1.5 1.5 DETPMP 0.4 0.4 0.4 CMC 0.4 0.4 0.4 MA / AA 4.0 2.0 2.0 Agglomerates LAS 5.0 5.0 5.0 TAS 2.0 2.0 1.0 Silicate 3.0 3.0 4.0 Zeolite A 8.0 8.0 8.0 Carbonate 8.0 8.0 4.0 Application by sprinkling Perfume 0.3 0.3 0.3 C45E7 2.0 2.0 2.0 C25E3 2.0 - - Dry additives EXAMPLE 8 (CONTINUED) Citrate 5.0 2.0 Bicarbonate - 3.0 - Carbonate 8.0 15.0 10.0 TAED 6.0 2.0 5.0 PB1 4.0 7.0 10.0 Polyethylene oxide with _ _ 0.2 PM of 5, 000, 000 Bentonite clay - - 10.0 Antibody 1.0 0.05 0.01 Protease 0.1 0.01 0.007 Lipase 0.009 0.009 0.009 Amylase 0.005 0.005 0.005 Cellulase 0.0014 0.0014 0.0014 Silicone antifoams 5.0 5.0 5.0 Dry additives Sodium sulphate 0.0 3.0 0.0 Other (moisture and miscellaneous ingredients) 100.0 100.0 100.0 Density (g / liter) 850 850 850 EXAMPLE 9 The following high density detergent formulations were prepared in accordance with the present invention: II Agglomerate C45AS 11.0 14.0 Zeolite A 15.0 6.0 Carbonate 4.0 8.0 MA / AA 4.0 2.0 CMC 0.5 0.5 DETPMP 0.4 0.4 Spray application C25E5 5.0 5.0 Perfume 0.5 0.5 Dry additives HEDP 0.5 0.3 SKS 6 13.0 10.0 Citrate 3.0 1.0 TAED 5.0 7.0 Percarbonate 20.0 20.0 SRP 1 0.3 0.3 Antibody 0.05 0.015 Protease 0.014 0.005 EXAMPLE 9 (CONTINUED) Lipase 0.009 0.009 Cellulase 0.0014 0.0014 0.005 0.005 0.005 0.005 Silicone antifoams 5.0 5.0 Brightener 1 0.2 0.2 Brightener 2 0.2 - Rest (moisture and ingredients 100 100 different) Density (g / liter) 850 850 EXAMPLE 10 The following formulations i were prepared? granular detergents, in accordance with the present invention: I II III IV V LAS 21.0 25.0 18.0 18.0 - Coco- (AS de C12-14) - - - - 21.9 AE3S - - 1.5 1.5 2.3 Decildimethylhydroxyethyl - 0.4 0.7 0.7 0.8 NH4 + C1 Surfactant 1.2 - 0.9 0.5 - nonionic EXAMPLE 10 (CONTINUED) Coco- (fatty alcohol of 1.0 C12-14) STPP 44.0 25.0 22.5 22.5 22.5 Zeolite A 7.0 10.0 - - 8.0 MA / AA - - 0.9 0.9 - SRP1 0.3 0.15 0.2 0.1 0.2 CMC 0.3 2.0 0.75 0.4 1.0 Carbonate 17.5 29.3 5.0 13.0 15.0 Silicate 2.0 - 7.6 7.9 - Antibody 0.16 0.5 0.1 0.9 10.0 Protease 0.005 0.04 0.007 0.009 0.15 Amylase - 0.004 0.004 - 0.004 Lipasa 0.003 0.003 0.003 - - Celulasa - 0.001 0.001 .001 .001 NOBS - - - 1.2 1.0 PB1 - - - 2.4 1.2 Diethylenetriamine- - - - 0.7 1.0 pentaacetic acid Diethylenetriamine- - - 0.6 - - pentamethylphosphonic acid Mg - - 0.8 - - Photoactivated bleach 45 50 ppm 15 45 ppm 42 ppm ppm ppm Rinse aid 1 0.05 0.04 0.04 0.04 EXAMPLE 10 (CONTINUED) Rinse aid 2 0.1 0.3 0.05 0.13 0.13 Water and minor ingredients up to 100% EXAMPLE 11 The following liquid detergent formulations were prepared in accordance with the present invention: I II III IV V VI VII VIII LAS 10.0 13.0 9.0 - 25.0 - - - C25AS 4.0 1.0 2.0 10.0 - 13.0 18.0 15.0 C25E3S 1.0 - - 3.0 - 2.0 2.0 4.0 C25E7 6.0 8.0 13.0 2.5 - - 4.0 4.0 TFAA - - • - 4.5 - 6.0 8.0 8.0 QAS - - - - 3.0 1.0 - - TPKFA 2.0 - 13.0 2.0 - 15.0 7.0 7.0 Fatty acids - - - 5.0 - - 4.0 4.0 Rapeseed seed Citric acid 2.0 3.0 1.0 1.5 1.0 1.0 1.0 1.0 Dodecetyltetra-decenylsuccinic acid 12. 0 10. 0 - 15.0 - - - Oleic acid 4.0 2.0 1.0 - 1.0 - - - Ethanol 4.0 4.0 7.0 2.0 7.0 2.0 3.0 2.0 1,2-Propanediol 4.0 4.0 2.0 7.0 6.0 8.0 10.0 13.0 EXAMPLE 11 (CONTINUED) Monoethanolamine - - - 5.0 - - 9.0 9.0 Triethanolamine _ _ 8 - - - - -NaOH (pH) 8.0 8.0 7.6 7.7 8.0 7.5 8.0 8.2 Tetraethylene- 0.5 - 0.5 0.2 - - 0.4 0.3 Ethoxylated pentamine DETPMP 1.0 1.0 0.5 1.0 2.0 1.2 1.0 - SRP-2 0.3 - 0.3 0.1 - - 0.2 0.1 PVNO - - - - - - - 0.10 Antibody 0.1 0.01 10E-5 0.1 0.001 10.0 0.01 .001 Protease 0.16 .002 .005 0.08 .008 o.i 0.01 .006 Lipasa - .002 - .0002 - - .003 .003 Amylase .002 .002 - .004 .002 - .005 .005 Celulasa - - - .001 - - .002 .001 Boric acid 0.1 0.2 - 2.0 1.0 1.5 2.5 2.5 Na Formate - - 1.0 - - - - - Chloride of Ca - 0.015 - 0.01 - - - - Clay of - - - - 4.0 4.0 - -bentonite Clay of suspension - - - - 0.6 0.3 SD3 Rest (humidity and diverse ingredients) : up to 100% EXAMPLE 12 Granular compositions were prepared for cleaning fabrics that provide "softening by washing" capability, in accordance with the present invention: I II 45AS - 10.0 LAS 7.6 68AS 1.3 45E7 4.0 25E3 - 5.0 Coconut-alkyl- 1.4 1.0 dimethylhydroxyethylammonium citrate 5.0 3.0 Na-SKS-6 - 11.0 Zeolite A 15.0 15.0 MA / AA 4.0 4.0 DETPMP 0.4 0.4 PB1 15.0 Percarbonate - 15.0 TAED 5.0 5.0 Smectite clay 10.0 10.0 HMWPEO - 0.1 Antibody 0.075 .0.1 Protease 0.02 0.006 EXAMPLE 12 (CONTINUED) Lipase 0.02 0.01 Amylase 0.03 0.005 Cellulase 0.001 - Silicate 3.0 5.0 Carbonate 10.0 10.0 Granulated foam suppressor 1.0 4.0 CMC 0.2 0.1 Water / minor ingredients up to 100% EXAMPLE 13 The following fabric softener composition added during the rinse was prepared in accordance with the present invention: Active agent softener 20.0 Antibody 0.01 Protease 0.005 Cellulase 0.001 HCl 0.03 Antifoaming agent 0.01 Blue coloring 25 ppm CaCl2 0.20 EXAMPLE 13 (CONTINUED) Perfume 0.90 Water / minor ingredients up to 100% EXAMPLE 14 The following fabric softening composition was prepared, in accordance with the present invention: DEQA 2.60 19.00 - SDASA - - 70.00 Stearic acid with VI = 0 0.30 - - Neodol 45-13 - - 13.00 Hydrochloric acid 0.02 0.02 - Ethanol - - 1.00 PEG - 0.60 - Antibody 0.1 0.1 1.0 Protease 0.01 0.008 0.05 Perfume 1.00 1.00 0.75 Succinate of digeranil - - 0.38 Silicone antifoams 0.01 0.01 - Electrolyte - 600ppm - Colorant lOOppm 50ppm 0.01 Water and minor ingredients 100% 100% - EXAMPLE 15 The Syndet bar fabric cleaning compositions were prepared in accordance with the present invention: I II III IV C26 AS 20.00 20.00 20.00 20.00 CFAA 5.0 5.0 5.0 5.0 LAS (Cll-13) 10.0 10.0 10.0 10.0 Sodium carbonate 25.0 25.0 25.0 25.0 Sodium pyrophosphate 7.0 7.0 7.0 7.0 STPP 7.0 7.0 7.0 7.0 Zeolite A 5.0 5.0 5.0 5.0 CMC 0.2 0.2 0.2 0.2 Polyacrylate (MW 1400) 0.2 0.2 0.2 0.2 Coconut Monetanolamide 5.0 5.0 5.0 5.0 Antibody 0.1 0.1 0.01 0.001 Amylase 0.01 - 0.01 - Protease 0.08 0.01 0.005 0.001 Rinse aid, perfume 0.2 0.2 0.2 0.2 CaS04 1.0 1.0 1.0 1.0 MgS04 1.0 1.0 1.0 1.0 Water 4.0 4.0 4.0 4.0 Filler *: subtract > for 100% * Suitable materials can be selected, such as CaCO3, talc, clay (kaolinite, smectite), silicates and the like. - EXAMPLE 16 Detergent additives were prepared, in accordance with the present invention: I II III 10 LAS 5 STPP 30 30 Zeolite A - - 35 PB1 20 20 15 TAED 10 10 8 15 * Protease 0.3 - 0.3 w Amylase 0.1 - - Antibody 10 10 1.0

Claims (10)

NOVELTY OF THE INVENTION CLAIMS

1. - A detergent composition, characterized in that it comprises a protease and an antibody directed against protease.

2. - The detergent composition according to claim 1, further characterized in that said anti-protease antibody is included at a level of 10E-6% at 10E + 1% by weight of the total composition.

3. The detergent composition according to claim 1, further characterized in that the protease is selected from serine proteases.

4. The detergent composition according to claim 1, further characterized in that the protease is included at a level of from 0.0001% to 2%, preferably from 0.001% to 0.2%, more preferably from 0.005% to 0.1% by weight of pure enzyme of the total composition.

5. - The detergent composition according to claim 1, further characterized in that said antibody directed against protease is incorporated in a release agent.

6. The detergent composition according to claim 1, further characterized in that it comprises one or more components selected from anionic, nonionic, cationic, amphoteric and zwitterionic surfactants, detergency builder, bleaching system, suds suppressors, polymer dirt release, * R dispersant of lime soap, suspending agents and anti-f 5 redeposition of dirt, smectite clays, and the like.

7. The detergent composition according to claim 1, further characterized in that it is in the form of a liquid, granulate, powder, gel, paste or stick.

8. A detergent additive, characterized in that it comprises an antibody directed against protease.

9. The detergent additive according to claim 8, further characterized in that it comprises a protease. r- 10.- The use of an antibody directed against protease in a laundry detergent composition to provide i? fabric care benefits.