JP2003511482A - Detergent composition comprising an enzyme that degrades aged starch - Google Patents

Abstract

  (57) [Summary] The present invention relates to a laundry detergent composition comprising an aged starch-degrading enzyme, wherein the aged starch index (ReSI) is less than 4%, preferably less than 3%. Such a composition is excellent in the effect of removing stains and stains containing starch, and therefore, is excellent in maintaining whiteness and cleaning light stains.

Description

Detailed Description of the Invention

FIELD OF THE INVENTION The present invention relates to detergent compositions comprising an enzyme that degrades aged starch.

[0002] Background detergent product of the present invention performance is determined by a number of factors including the ability to remove stains. To that end, detergent ingredients such as surfactants, bleaches and enzymes are incorporated into detergents. One such specific example is the use of proteases, lipases, amylases and / or cellulases.

Proteases are enzymes commonly used in cleaning applications. Proteases are known for their ability to hydrolyze other proteins. This ability has been exploited by incorporating naturally occurring or engineered proteases into laundry detergent compositions. It is known to incorporate a lipolytic enzyme into a detergent composition to improve the cleaning performance, for example, it is possible to more strongly remove stains and stains containing triglyceride from a fabric. Cellulase activity is the activity of cellulosic fibers or substrates attacked by cellulase, which depends on the cellulase, which may be an endo- or exocellulase, and the particular function of the respective hemicellulase. The cellulosic structure is depolymerized or cleaved into smaller fractions and therefore more soluble or dispersible. This activity, especially for fabrics, results in cleaning, recovery, softness,
And generally improved feel properties are imparted to the fabric structure. The amylase enzyme removes starchy food residues or starchy coatings from dishware or hard surfaces in detergent compositions, or against starchy soils and other soils typically found in laundry and dishwashing applications. It has long been recognized to provide cleaning performance.

In fact, starches, such as amylose and amylopectin, constitute one of the main constituents of stains / stains encountered in laundry, dishwashing or hard surface cleaning operations. Moreover, the textile industry uses starchy materials in textile finishing processes. As such, amylase enzymes have been previously incorporated into detergent products to remove starch-containing soils. However, it was surprisingly found here that such commonly used detergent amylases cannot hydrolyze retrograded starch.

JA Radley “Starch and its Derivatives” 4th Edition, Chapman and Hall Ltd
As studied in p194-201, aging is the term used for starch pastes or gels that change naturally over time. Aging of starch molecules
It is caused by the inherent tendency of molecules to bind to each other and increase in crystallinity. The low-concentration solution becomes increasingly cloudy due to the progressive association of starch molecules into large particles. Precipitation occurs spontaneously and the precipitated starch is believed to return to its original state of being insoluble in cold water. The thick paste solidifies on cooling to a gel and becomes increasingly stiff over time as the starch molecules gradually associate. This occurs because of the strong tendency to form hydrogen bonds between hydroxyl groups on adjacent starch molecules.

The changes that occur during aging are of great importance for the industrial use of starch. Aging is believed to be an important factor in the firmness of bread and the structural changes in other starch-containing foods, such as canned soups, beans, cooked meats, and the like. Starch and aged starch are also found in the textile, papermaking and adhesive industries. In fact, the fabric is woven and glued with starch. Depending on the gluing method,
Aged starch may form in the fabric and may not be removed in subsequent glue removal steps. Moreover, most of the stains / soils found on fabrics contain starch, which ages over time, eg in a laundry basket,
Such an associated starchy network structure results. As such, such aged starch-containing material will later form on the fabric to be washed. Moreover, surprisingly, when such aged starch traps other stains and is on the fabric surface, the appearance of the surface to be washed is smeared.

[0007] Such aged starches show great resistance to hydrolysis by amylolytic enzymes, hardly dissolve at normal temperature and very difficult to disperse, especially when the aged starch is first dried. Further increases the gel hardness. In fact, aged starch forms a very stable structure at very high temperatures, eg 150 ° C. for amylose, 60 ° C. for amylopectin, or 120 ° C. for amylose-lipid complex. Only melts. The level and timing of aging depends on the type of starch and can vary from 10% to 90% of starch content. Current detergent amylase has little or no effect on aged starch.

As can be seen from the above, there is a need to formulate detergent products for removing such aged starch-containing stains / stains. Here, the above object was achieved by formulating a detergent composition comprising an enzyme that is highly efficient against aged starch. Such an enzyme is known as the aged starch index (ReS
I) is characterized by less than 4%, preferably less than 3%. Preferably, the detergent composition of the present invention comprises a combination of several aged starch degrading enzymes.

Preferably, the detergent composition of the present invention comprises other detergent enzymes such as proteases,
It further comprises a detergent component selected from lipases and / or conventional amylases, starch debranching enzymes or pullulanase type II, nonionic surfactants, bleaches and / or anti-redeposition agents.

EP-A-368341 improves surfactants and at least one starch debranching enzyme selected from the group consisting of pullulanases, isopullanases and isoamylases, preferably starchy soil detergents. Detergent compositions comprising α-amylase for British Patent No. 222
No. 8945 describes an automatic dishwashing composition comprising an enzyme capable of breaking α-1,6 glucosidic bonds. International Patent No. WO98 / 2607
No. 8 relates to H mutant α-amylase with improved stability. EP-A-450627 describes a new detergent composition containing alkaline pullulanase which has excellent cleaning performance on starchy soils. International Patent W
O94 / 19468 relates to a DNA fragment containing a gene for alkaline pullulanase useful as a detergent component. U.S. Pat. No. 5,665,585 describes a unique glucoamylase P amino acid and DNA sequence with high debranching activity, a Trichoderma host cell transformed with such a sequence, and such a recombinant glucoamylase P. And the industrial use of recombinant enzymes and hosts transformed therewith, especially in alcoholic fermentation. US Pat. No. 3,640,877
Glucose and glucose oxidase or starch as precursors of hydrogen peroxide, amyloglucosidase and glucose oxidase,
And a detergent formulation comprising a system of hydroxylamines which stabilizes the hydrogen peroxide formed during use of the detergent. International Patent No. WO 95/29996 discloses a novel glucose oxidase, a process for its preparation and its use in bleaching and detergent compositions and its use as a dough enhancer. The enzyme has many uses in the cosmetics and confectionery industries, preferably in combination with other enzymes selected from amyloglucosidase, lactoperoxidase, α-amylase or the malt gene exo-amylase.

However, the use of enzymes which are highly efficient against aged starch for the removal of stain-stains containing aged starch in laundry detergent compositions has not been previously disclosed.

SUMMARY OF THE INVENTION The present invention has an aged starch index (ReSI) of less than 4%, preferably 3.
% Laundry detergent composition comprising an aged starch degrading enzyme. Such a composition has an excellent effect of removing starch-containing stains and stains, and therefore has excellent whiteness maintenance and thin stain cleaning properties. DETAILED DESCRIPTION OF THE INVENTION An essential component of the detergent composition of the present invention is an enzyme that has an activity on α-polysaccharide and has a high efficiency of degrading aged starch substances (hereinafter, referred to as “aged starch degrading enzyme”). Such enzymes are characterized by an aged starch index (ReSI) of less than 4%, preferably less than 3%.

In fact, enzymes meeting these criteria have been found to be highly efficient in degrading aged starch found on fabrics and, therefore, excellent in thin soil cleaning. It has been found that fabrics that are repeatedly washed, especially white fabrics, accumulate a low intensity of gray or yellow. While not wishing to be bound by theory, it is believed that such reminant aged starch attracts soil, causing a gray, lightly soiled appearance of the fabric.
It is believed that the selected enzymes of the present invention hydrolyze such aged starch layers and provide excellent cleaning performance for light soils. From the above, the object of the present invention is to
In particular, it is necessary to obtain this thin dirt cleaning performance. Therefore, according to the present invention, an enzyme having a high light-washing and washing efficiency is selected by the following test method using carbon black that simulates a lightly soiled appearance.

The enzymatic hydrolysis of the aging starch degrading enzyme of the present invention is measured by a color index. Aged starch index (ReSI) is determined as follows.

The fabric is provided with aged starch and carbon black. Aged starch is deposited on the fabric and traps carbon black in the starch structure and is used as a color indicator to indicate the presence of aged starch. Before and after enzyme treatment, the aged starch remaining on the test fabric is measured by spectroscopic color measurement. The measured% color strength of carbon black remaining on the fabric is proportional to the aged starch that was not hydrolyzed by the enzyme under test and was not removed from the fabric. The lower the% of the color strength of carbon black, the better the removal performance of carbon black,
This reflects the excellent performance of removing aged starch. Therefore, a low percentage of color intensity indicates high enzyme performance.

The Aged Starch Index (ReSI) is measured as follows. 1. Cut a piece of knit cotton (8 x 20 cm). 2. 50 g of corn starch (Amylum) is placed in 500 ml of deionized water. 3. The solution is stirred on a magnetic stir plate (Ikamag, position 4). 4. Gently add 10 g of carbon black (Fluka activated carbon 05100) to the beaker. 5. Heat the starch-carbon black solution (maximum heating, stirring position 4). 6. A gel is formed at a temperature of 60 to 70 ° C. Heat the gel for about 5 minutes. 7. Remove the beaker from the heating plate. 8. Knit cotton is coated with starch-carbon black gel by gentle tapping using a small wallpaper roller until the surface is covered with a black gel. 9. Wrap each knit cotton sample in aluminum foil and store in the refrigerator for 3 days. After 10.3 days, the fabric is removed, hung and dried. 11. Put the test fabric obtained as described above in 400 ml of sodium acetate buffer solution in Launder-o-meter (4 pieces of fabric per Launder-o-meter) at a temperature of 40 ° C and an optimum pH of the test enzyme for 1 hour. , Spin dry the fabric. Spectraflash for fabric color intensity
Measure at Datacolor International.

The optimum pH of the tested enzyme is described in the technical data accompanying the commercial sample of enzyme or can be derived from the% activity vs. pH curve. For example, No
The amyloglucosidase AMG300L data sheet from vo Nordisk has a pH of 4.
Instructing 3.

This experiment is carried out in the presence of excess test enzyme. This excess concentration is obtained when the test enzyme concentration is increased further and the corresponding ReSI index no longer decreases. For example, such a concentration corresponds to 4 ml of the amyloglucosidase AMG3000L commercially available from Novo Nordisk A / S (activity 300 GA / ml and protein content 145 mg / ml).

12. The color intensity of the fabric is measured before and after the enzyme treatment. Spectraflash 500 Datac
olor International standard setting: ^* SPECULAR: Excluded, ^* APERTURE: Ultra small, ^* UV
FILTER (cut-off filter 400 nm).

13. The calculation of% color intensity is performed by integrating the K / S curve over the visible spectrum, where K / S is the Kubelka-Munk constant K and S (Datacolor In
ternational Datamaster software program). The ratio of the surface under the K / S curve of the fabric before and after enzyme treatment indicates the color intensity.

A color strength of less than 4%, preferably less than 3%, shows very good whiteness and light stain cleaning performance. The amyloglucosidase marketed under the trade name AMG from Novo Nordisk A / S (Sample AMG300L with activity 300 GA / ml at 4 ml level in Launder-o-meter) has 3.8% color intensity (standard deviation) 0.15).

The aged starch degrading enzyme is generally contained in the detergent composition of the present invention in an amount of 0.0002 to 10% by weight, preferably 0.001 to 2% by weight, more preferably 0.001% by weight based on the entire detergent composition. ˜1% by weight pure enzyme. Preferred aged starch degrading enzymes for special applications are alkaline aged starch degrading enzymes, i.e. at least 10%, preferably at least 25%, more preferably at least 40% of maximal activity of the enzyme at pH 7-12, preferably 10.5. It is an enzyme that has. The more preferable aged starch degrading enzyme has a maximum activity of pH 7-1.
The enzyme having 2 and preferably 10.5.

Aged starch degrading enzymes having a ReSI of less than 4%, suitable for the purposes of the present invention, are:
The following enzyme category (IUPAC category), namely amyloglucosidase EC3.2
． 1.3, α-amylase EC 3.2.1.1, beta-amylase EC 3.2
． 1.2, isoamylase EC 3.2.1.68, pullulanase type IEC3
． 2.1.41, Isopullulanase EC 3.2.1.57, Neopullulanase E
C3.2.1.135, pullulanase type II, dextrin dextranase EC 2.4.1.24, cyclodextrin glycosyl transferase EC
2.4.1.19 and the malt gene alpha-amylase C3.2.1.33. Preferably, the detergent composition comprises a combination of several aged starch degrading enzymes.

[0024] Amyloglucosidase , EC 3.2.1.3 is a glucan 1,4-α-glucosidase, and is referred to as "glucoamylase, γ-amylase, lysosoma system".
1) α-glucosidase, acid maltase or exo-1,4-α-glucosidase ”, and its systematic name is 1,4-α-D-glucan glucohydrolase. Amyloglucosidases are α-1,4 in polysaccharides such as starch.
It hydrolyzes both the and α-1,6 bond, releasing glucose units from the non-reducing end of the polysaccharide. These two activities are remarkable. α-1,4 and α-1,6
By hydrolyzing the glucosidic bond, amyloglucosidase releases β-D-glucose units from the non-reducing end of glucose polymers such as starch. Amyloglucosidase differs significantly from starch debranching enzyme by its ability to hydrolyze α-1,6-glucosidic bonds.

Alpha-amylase , EC 3.2.1.1, is a 1,4-α-D-glucan glucano hydrolase, containing three or more α-1,45 linked D-glucose units. Endohydrolysis of 1,4-α-D-glucoside bonds in the polysaccharide is performed.

Beta-amylase , EC 3.2.1.2, is a 1,4-α-D-glucan maltohydrolase, which is capable of exohydrolyzing 1,4-α-D-glucoside bonds in polysaccharides. Doing so removes contiguous maltose units from the non-reducing end of the chain.

[0027] The starch debranching enzymes generally include pullulanase type I, isopullulanases and isoamylase enzymes.

The pullulanase type I enzymes are classified under the IUPAC category EC 3.2.1.41 and the systematic name α-dextrin 6-glucanohydrolase. The pullulanase enzyme is 1 in pullulan, amylopectin and glycogen, and in α- and β-amylase limiting dextrins of amylopectin and glycogen.
, 6-α-D-Glucoside bonds, as well as branched oligosaccharides formed by their partial decomposition. Because of this feature, pullulanase is called a "debranching enzyme." In fact, pullulanase is an enzyme that breaks only the α-1,6-glycosidic bond of pullulan and ultimately produces maltriose.

Isopullulanases are classified under the IUPAC category EC 3.2.1.57 and the systematic name pullulan 4-glucanohydrolase. The isopullulanase enzyme hydrolyzes pullulan to isopanose (6-α-maltosyl glucose).

The isoamylase enzyme is capable of debranching glycogen. These enzymes are classified under the IUPAC classification EC 3.2.1.68 and the systematic name glycogen 6-glucanohydrolase. The isoamylase enzyme hydrolyzes 1,6-α-D-glucoside branch bonds in glycogen, amylopectin and their β-limit dextrins. Isoamylase cannot attack pullulan, α
-Limited action on limiting dextrins and complete action on glycogen distinguish it from pullulanase enzymes.

The neopullulanase enzyme is defined as an enzyme that decomposes pullulan to form panose and is classified in the IUPAC category EC 3.2.1.135. Pull Run 4-
The D-glucanohydrolase, the neopullulanase enzyme, has the ability to cleave both the 1,4- and 1,6-glucosidic bonds found in common starch and carbohydrate type stains or soils. For example, this enzyme hydrolyzes pullulan to panose (6-alpha-D-glucosylmaltose). In particular, the neopullulanase enzyme is used for hydrolysis of alpha- (1 → 4) glucoside bond, hydrolysis of alpha- (1 → 6) glucoside bond, transglycosylation reaction to form alpha- (1 → 4) glucoside bond, and It can catalyze four types of reactions, including transglycosylation reactions that form alpha- (1 → 6) glucosidic bonds. In contrast, other known enzymes catalyze only one or two of these reactions, the second being weaker. Also, four types of reactions are catalyzed by the same mechanism.

The pullulanase type II enzyme is defined as amylopullulanase and irregularly hydrolyzes α, 1-4 bonds in addition to branch points (α-1,6-bonds) in polysaccharides and dextrins. This is in contrast to pullulanase type I enzymes, which hydrolyze only α, 1-6 bonds in branched-chain polysaccharides.

Another suitable enzyme of the amylase class is dextrin dextranase . Dextrin dextranase (EC 2.4.1.2) is an enzyme that produces dextran and low molecular weight oligosaccharides from starch.

Cyclomaltodextrin glucanotransferase , EC 2.4.1.1
9 is 1,4-α-D by forming a 1,4-α-D-glucoside bond.
An enzyme that cyclizes a part of the glucan chain, 1,4-α-D-glucan 4-α-
It has the systematic name for D- (1,4-α-D-glucano) -transferase (cyclization).

Malt Gene Alpha-Amylase Also suitable is the malt gene alpha-amylase of the IUPAC category EC 3.2.1.133, which hydrolyzes the 1,4-α-D-glucoside linkages in the polysaccharide, Remove consecutive alpha-maltose units from the non-reducing end. A preferred malt gene alpha-amylase has been cloned from Bacillus as described in EP120693 and is commercially available from Novo Nordisk A / S under the Novamyl trade name amylase, CGT-ase activity. Mutant of malt gene alpha-amylase having and CGT- having malt gene alpha-amylase activity
ase variants, and the constructed hybrid enzymes described in WO 99/43793, and the stereotype of the malt gene alpha-amylase Novamyl described in WO 99/47394. Based on the physical structure, the characteristics are improved (the physicochemical characteristics are changed, for example, the optimum pH is changed,
Malt gene alpha-amylase variant with improved thermostability, increased specific activity, altered cleavage pattern, or increased ability to block starch aging or bread hardening).

A specific enzyme that meets the ReSI criteria of the present invention is, for example, the enzyme commercially available from Novo Nordisk A / S under the trade name AMG.

In another embodiment of the present invention, the detergent composition of the present invention can further comprise one or more starch binding zones. Such starch binding zones can be added to the detergent compositions of the present invention as such or as part of a chimeric aged starch degrading enzyme hybrid. In fact, the aged starch degrading enzymes of the invention have or add a starch binding zone (SBD). In general, enzymes such as amylases, cellulases and xylanases have a modular structure consisting of a catalytic zone and at least one non-catalytic zone, the function of the non-catalytic zone generally being the zone that binds the polysaccharide. (PBD), starch binding zone (SBD), cellulose binding zone (CBD) and xylan binding zone functions. The function of these binding zones is to selectively bind to the substrate of the enzyme, in particular the main function of SBD is to bind starch. Surprisingly, the detergent compositions of the present invention comprising one or more SBDs and / or aging starch degrading enzymes comprising such SBDs are more effective against starch-containing stains / stains. Found to be removed. Moreover, it has been found that such enzymes can be formulated in a cost and more efficient manner. Without wishing to be bound by theory, such aged starch degrading enzymes are specifically and more effectively directed at their substrates from the wash solution and thus preferentially deposit on starch-containing stains / stains. , It is believed that the performance will be improved or new performance will be exhibited. Moreover, it is believed that the binding of SBD disturbs the surface of the starch, resulting in a higher rate of hydrolysis. A preferred SBD for use in the present invention is the SBD contained in glucoamylase (Sigma) from Aspergillus niger and β-galactosidase from A. awamori. Recovery and fusion of SBD is described by Ford, C. et
al., J. Cell. Biochem. (Suppl.) 14D: 30 (1990) and Chen, L. et al., Abst.
It can be accomplished as described in .Annu. Meet. Am. Soc. Microbiol. 90: 269 (1990).

Detergent Composition The detergent composition of the present invention should include at least one additional detergent ingredient. The exact nature of these additional ingredients and their loadings depend on the physical form of the composition,
And the nature of the washing operation using the composition.

The detergent compositions of the present invention are preferably other conventional amylases, conventional starch debranching enzymes, conventional pullulanase type II, proteases or lipases, nonionic surfactants, bleaches and / or redeposits. Comprising an inhibitor.

In a preferred embodiment, the invention relates to laundry and / or fabric protection compositions (Examples 1-16) comprising aged starch degrading enzymes. It has been found that selected enzymes of the present invention exhibit excellent starch / staining stain / soil removal performance when formulated for dishwashing or hard surface cleaning applications. Thus, in a second embodiment, the invention relates to a dishwashing or household cleaning composition (Examples 17-23).

The compositions of the present invention include, for example, hand and machine dishwashing compositions, laundry additive compositions and hand and machine including compositions suitable for dipping and / or pre-treating soiled fabrics. It can be formulated as a laundry detergent composition, a fabric softener composition added during rinsing, and a composition used in common household hard surface cleaning operations. When formulated as a composition for use in a manual dishwashing process, the composition of the present invention is preferably a surfactant and preferably an organic polymeric compound, a foam enhancer, a Group II metal ion, a solvent, a hydrotropic agent. And other detergent compounds selected from additional enzymes.

When formulated as a composition suitable for use in a machine wash method, the composition of the present invention preferably comprises both a surfactant and a builder compound, and preferably an organic polymeric compound, a bleaching agent, It comprises one or more detergent ingredients selected from additional enzymes, foam inhibitors, dispersants, lime soap dispersants, soil dispersants and anti-redeposition agents and corrosion inhibitors. The laundry composition can also include a softening agent as an additional detergent component. Such a composition comprising amyloglucosidase removes starch-containing stains, maintains whiteness and cleans light soils when formulated as a laundry detergent composition.

The composition of the present invention can also be used as a detergent additive product. Such additive products are intended to supplement or enhance the performance of conventional detergent compositions.

The detergent composition of the present invention may be a liquid, paste, gel, bar, tablet, spray, foam material, powder or granules. The granular composition may be in "compact" form and the liquid composition may be in "concentrated" form. If necessary, the laundry detergent composition of the present invention has a density of 400 to 1200 g / liter, preferably 500 to 9 measured at 20 ° C.
It is a 50 g / liter composition. The "compact" form of the composition of the present invention is best reflected by the density and, in terms of composition, by the amount of inorganic filler, the inorganic filler salt being a common ingredient of detergent compositions in powder form, In the detergent compositions of the present invention, the filler salt is present in significant amounts, typically in the amount of 17-35% by weight of the total composition. In compact compositions, the filler salt is present in an amount up to 15% by weight of the total composition, preferably up to 10% by weight and most preferably up to 5% by weight. The inorganic filler salt referred to in the present composition is selected from alkali and alkaline earth metal sulfates or hydrochlorides. The preferred filler salt is sodium sulfate. The liquid detergent composition of the present invention may be in "concentrated form", in which case the liquid detergent composition of the present invention will contain a small amount of water as compared to conventional liquid detergents. Typically, the water content of the concentrated liquid detergent is preferably less than 40% by weight of the detergent composition, more preferably less than 30% by weight and most preferably less than 20% by weight.

Suitable detergent compounds for use herein are selected from the group consisting of the compounds described below.

Surfactant System The detergent compositions of the present invention generally comprise a surfactant system, where the surfactant is nonionic and / or anionic and / or cationic and / or cationic. Or it can be selected from ampholytic and / or zwitterionic and / or semipolar surfactants.

Preferably, the detergent composition of the present invention comprises a nonionic surfactant, preferably a nonionic surfactant based on a polyoxyethylene condensate with an alcohol. In fact, the detergent composition of the present invention further comprising a nonionic surfactant,
Surprisingly, it has been found to more effectively remove starch from fabrics, dishes, and other hard surfaces. Without wishing to be bound by theory, nonionic surfactants are adsorbed on the granular surface of starch, thereby disturbing the starch structure,
It is thought to affect and interfere with the aging process of starch. Such structural perturbations make the enzyme more accessible to the substrate. Moreover, nonionic surfactants can also be used in the pretreatment step and thus delay the starch aging process. As a result, the starch-containing stains / soils are more easily hydrolyzed by the enzymes, resulting in synergistic degradation of the starch soils by the aged starch-degrading enzymes and nonionic surfactants.

The surfactant is typically present in an amount of 0.1-60% by weight. A more preferred compounding level is 1-35% by weight, most preferably 1-30% by weight of the detergent composition of the present invention.

The surfactant is preferably formulated so as to be compatible with the enzyme components present in the composition. In liquid or gel compositions, the surfactant is most preferably formulated so as to enhance, or at least not reduce, the stability of all enzymes present in these compositions.

Nonionic Surfactants: Polyethylene, polypropylene, and polybutylene oxide condensates of alkylphenols are suitable for use as the surfactant-based nonionic surfactants of the present invention, polyethylene oxide condensates. Is preferred. These compounds include condensation products of alkylphenols and alkylene oxides having an alkyl group with about 6 to about 14, preferably about 8 to about 14, carbon atoms in the straight or branched chain structure. In a preferred embodiment, ethylene oxide is about 2 to about 25 moles per mole of alkylphenol, more preferably about 3 to about 1 mole.
Present in an amount equal to 5 moles of ethylene oxide. Commercially available nonionic surfactants of this type include Igepal (trade name) commercially available from GAF Corporation.
CO-630, and Triton (trade name) X-45, X-114, X-100 and X-102, all commercially available from Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (eg alkylphenol ethoxylates).

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 in the nonionic surfactant system of the present invention. It is suitable. The alkyl chain of the aliphatic alcohol may be linear or branched, primary or secondary, and generally has about 8 to about 22 carbon atoms. A preferred material is the condensation product of an alcohol having an alkyl group with 8 to 20 carbon atoms and about 2 to about 10 moles of ethylene oxide per mole of alcohol.
About 2 to about 7 moles of ethylene oxide are present in the condensation product, and most preferably 2 to 5 moles of ethylene oxide are present per mole of alcohol. Examples of commercially available nonionic surfactants of this type are both Union Carbide Corporation.
Commercially available from Tergitol (trade name) 15-S-9 (condensation product of C _{11 to} C ₁₅ linear alcohol and 9 mol of ethylene oxide), Tergitol (trade name) 24-L-6 NMW
(Of C ₁₂ -C ₁₄ primary alcohol with 6 moles ethylene oxide, a narrow molecular weight distribution condensation product), Shell Chemical Company from commercially available Neodol (trade name) 45-9
(Condensation product of C _{14 to} C ₁₅ straight chain alcohol and 9 mol of ethylene oxide)
, Neodol (trade name) 23-3 (condensation product of C _{12 to} C ₁₃ straight chain alcohol and 3.0 mol of ethylene oxide), Neodol (trade name) 45-7 (C _{14 to} C ₁₅ straight chain alcohol) And 7 mol ethylene oxide condensation product), Neodol (trade name) 45-5 (
A condensation product of C ₁₄ -C ₁₅ straight chain alcohol and 5 mol of ethylene oxide),
And Procter & Gamble Company from commercially available Kyro (trade name) EOB _(C 13 ~C ₁
Condensation product of ₅ alcohols and 9 moles of ethylene oxide), G commercially available from Hoechst
enapol LA 030 or 050 (condensation product of C _{12 to} C ₁₄ alcohol and 3 or 5 mol of ethylene oxide). The preferred HLB range in these products is 8-11, most preferably 8-10.

Examples of the surfactant-based nonionic surfactant of the present invention include US Pat.
No. 5,647, Llenado, promulgated Jan. 21, 1986, hydrophobic groups having about 6 to about 30, preferably about 10 to about 16 carbon atoms, and about 1.3. To about 10, preferably about 1.3 to about 3, most preferably about 1.3 to about 2.
Alkyl polysaccharides having hydrophilic groups of polysaccharides containing 7 sugar units, eg polyglycosides, are also suitable. All reducing sugars having 5 or 6 carbon atoms can be used, for example glucose, galactose and galactosyl moieties can be replaced by glucosyl moieties (hydrophobic groups can optionally be 2-, 3-, 4-. , Etc. to give glucose or galactose to glucoside or galactoside). The inter-sugar linkage is, for example, at the position of the additional sugar unit and at the position of the preceding sugar unit.
It may be between the-, 3-, 4-, and / or 6-positions.

[0053]   Preferred alkyl polyglycosides have the formula:

R ² O (C _n H _2n O) t (glycosyl) _{x In the} formula, R ² has an alkyl group having about 10 to about 18, preferably about 12 to about 1.
4 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof, where n is 2 or 3,
It is preferably 2, t is 0 to about 10, preferably 0, and x is about 1.3 to about 10, preferably about 1.3 to about 3, and most preferably about 1.3 to about 2. 7
Glycosyl is preferably derived from glucose. To produce these compounds, an alcohol or alkyl polyethoxy alcohol is first formed and then reacted with glucose or a source of glucose to form a glucoside (1
-Add at position). Additional glycosyl units can then be added between their 1-position and the preceding glycosyl units 2-, 3-, 4-, and / or 6-position, preferably predominantly the 2-position.

Condensation products of ethylene oxide with a hydrophobic base formed by the condensation of propylene oxide and propylene glycol are also suitable for use as the additional nonionic surfactant system of the present invention. The hydrophobic portion of these compounds preferably has a molecular weight of about 1500 to about 1800 and is insoluble in water. Adding a polyoxyethylene moiety to this hydrophobic moiety tends to increase the water solubility of the entire molecule, and the liquid nature of the product is such that the polyoxyethylene content is about 50% of the total weight of the condensation product. It is held up to the point, which corresponds to condensation with up to about 40 mol of ethylene oxide. Examples of compounds of this type include Plurafac® LF404 and Pluronic® surfactants commercially available from BASF.

Other suitable nonionic surfactants are the condensation products of ethylene oxide with the product obtained 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. The hydrophobic portion is condensed with ethylene oxide to such an extent that the condensation product contains about 40 to about 80% by weight of polyoxyethylene and has a molecular weight of about 5,000 to about 11,000. Examples of this type of nonionic surfactant include the Tetronic® compounds commercially available from BASF.

Preferred materials for use as the surfactant-based nonionic surfactants of the present invention include polyethylene oxide condensates of alkylphenols, primary and secondary aliphatic alcohols and from about 1 to about 25 moles. Condensation products of ethylene oxide, alkyl polysaccharides, and mixtures thereof. The most preferred material is 3-15 _C 8 having ethoxy groups _{-C 14} alkyl phenol ethoxylates and 2-10 _C 8 having ethoxy groups _{-C 18} alcohol ethoxylates (preferably C1
0 average) and mixtures thereof.

Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants having the formula:

[0059]

[Chemical 1] Wherein R ¹ is H, or R ¹ is C _1-4 hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl, or a mixture thereof, R ₂ is C _{5 -31} hydrocarbyl, Z Is a polyhydroxyhydrocarbyl having a hydrocarbyl straight chain and at least three hydroxyl groups directly bonded to the chain, or an alkoxylated derivative thereof. Preferably R ¹ is methyl,
R ₂ is a linear C _11-15 alkyl or C _16-18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, Z is a reducing sugar such as glucose, fructose, in a reductive amination reaction. It is derived from maltose and lactose.

[0060] The linear ester anionic surfactants suitable anionic surfactants used are linear alkyl benzene sulfonates, C ₈ -C ₂₀ carboxylic acids (i.e. fatty acids), "The Journal of American Oil Chemists Society , 52 (1975), pp.32
3-329 is an alkyl ester sulfonate surfactant including materials sulfonated with gaseous SO ₃ . Suitable starting materials include natural fatty substances derived from tallow, palm oil, and the like. Particularly preferred alkyl ester sulfonate surfactants for laundry applications comprise an alkyl ester sulfonate surfactant having the formula:

[0061]

[Chemical 2] Wherein R ³ is C ₈ -C ₂₀ hydrocarbyl, preferably alkyl, or a combination thereof, R ⁴ is C ₁ -C ₆ hydrocarbyl, preferably alkyl, or a combination thereof, and M is an alkyl ester sulfonate. It is a cation that forms a water-soluble salt with. 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 3} is _C 10 _{-C 16} alkyl, ^{R 4} is methyl, ethyl or isopropyl. A particularly preferred material is a methyl ester sulfonate in which R ³ is C ₁₀ -C ₁₆ alkyl.

[0062] Other suitable anionic surfactants include alkyl sulfate surfactants which are water soluble salts or acids of the formula RSO ₃ M, wherein, R is preferably _C 10 _{-C 2 4} hydrocarbyl, preferably an alkyl or hydroxyalkyl having a _C 10 _{-C 20} alkyl component, more preferably a _C 12 _{-C 18} alkyl or hydroxyalkyl, M is H or a cation, such as alkali metal cations (
For example sodium, potassium, lithium), or ammonium or substituted ammonium (for example methyl-, dimethyl-, and trimethylammonium cations and quaternary ammonium cations, for example tetramethylammonium and dimethylpiperidinium cations and alkylamines. , Quaternary ammonium cations, such as from ethylamine, diethylamine, triethylamine, and mixtures thereof). Typically, C ₁₂ -C ₁₆ alkyl chains are preferred for low wash temperatures (eg, below about 50 ° C.) and C _16-18 alkyl chains are preferred for high wash temperatures (eg, above about 50 ° C.).

[0063]   Other anionic surfactants useful for cleaning purposes are also included in the detergent compositions of the present invention.
be able to. These surfactants include salts of soaps (e.g. sodium, potassium).
Lithium, ammonium, and substituted ammonium salts such as mono-, di-
And triethanolamine salts), C₈~ C₂₂First grade or first
Secondary alkane sulfonate, C₈~ C₂₄Olefin sulfonates, for example UK
Alkaline earth metal citric acid described in Japanese Patent No. 1,082,179
Sulfonated polycarboxylic acids prepared by sulfonation of salt pyrolysis products
Acid, C₈~ C₂₄Alkyl polyglycol ether sulfate (up to 10 mol)
(Including ethylene oxide), alkyl glycerol sulfonate, fatty acyl
Glycerol sulfonate, fatty oleyl glycerol sulphate, alkyl
Phenol ethylene oxide ether sulfate, paraffin sulfonate,
Alkyl phosphates, isethionates, such as acyl isethionates, N-acetates
Siltaurate, alkylsuccinamates and sulfosuccinates, sulfos
Cuccinate monoesters (especially saturated and unsaturated C₁₂~
C₁₈Monoesters) and sulfosuccinate diesters (especially saturated)
And desaturated C₆~ C₁₂Diester), acyl sarcosinate,
Sulfates of alkyl polysaccharides, eg sulfates of alkyl polyglucosides
(Nonionic non-sulfated compound described below), branched primary alkyl monkey
Fates, and alkyl polyethoxycarboxylates such as the formula RO (CH _Two CH_TwoO)_k-CH_TwoCOO-M⁺(In the formula, R is C₈~ C₂₂Is alkyl
, K is an integer of 1 to 10 and M is a cation forming a soluble salt)
Is mentioned. Resin acids and hydrogenated resin acids such as rosin, hydrogenated rosin, and
And hydrogenated resin acids present in or derived from tall oil
, Are also suitable.

Another example is “Surface Active Agents and Detergents” (Vol. I and II).
, Schwartz, Perry and Berch). A variety of such surfactants are described in US Pat. No. 3,929,678, Laughl, Dec. 30, 1975.
in et al. promulgated, paragraphs 23, 58 to paragraphs 29, 23 generally.

When included, the laundry detergent composition of the present invention typically comprises from about 1 to about 40% by weight.
%, Preferably about 3 to about 20% by weight of such anionic surfactants.

Highly preferred anionic surfactants include alkylalkoxylated sulphate surfactants, which are water-soluble salts of the formula RO (A) _m SO3M, in which R is substituted. no _C 10 _{-C 24} hydroxyalkyl group having an alkyl or _C 10 _{-C 24} alkyl component, preferably a _C 12 _{-C 20} alkyl or hydroxyalkyl, more preferably _C 12 _{-C 18} alkyl or hydroxyalkyl, a is Is an ethoxy or propoxy unit, m is greater than 0, typically about 0.5 to about 6, more preferably about 0.5 to about 3, and M is H
Or a cation, wherein the cation is, for example, a metal cation (eg, sodium,
Potassium, lithium, calcium, magnesium, etc.), ammonium or substituted ammonium cations. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl-, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyldipiperidinium cations, and alkylamines such as Cations derived from ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary surfactants _are, C 12 _{-C 18} alkyl polyethoxylate (1.0) sulfate _{(C 12 ~C 18 E (1} .
_{0) M), C 12 ~C} 18 alkyl polyethoxylate (2.25) sulfate _{(C 12 ~C 18 E (2.25} ) M), C 12 ~C 18 alkyl polyethoxylate (3.0) sulfate _{(C 12 ~C 18 E (3.0} ) M), and _{C 1} 2 _{-C 18} alkyl polyethoxylate (4.0) a sulfate _{C 12 ~C 18 E (4.0)} M), wherein Advantageously, M is selected from sodium and potassium.

The detergent compositions of the present invention include cationic, ampholytic, zwitterionic, and semipolar surfactants, as well as nonionic and / or anionic non-surfactants previously described herein. A systemic surfactant can also be included.

Cationic Surfactant The cationic detersive surfactant suitable for use in the detergent compositions of the present invention is a surfactant having one long chain hydrocarbyl group. Examples of such cationic surfactants include ammonium surfactants such as alkyl trimethyl ammonium halides, and surfactants having the formula:

[0069]

[Chemical 3] In the formula, R ² is an alkyl or alkylbenzyl group having about 8 to about 18 carbon atoms in the alkyl chain, and each R ³ is —CH ₂ CH ₂ — or —CH ₂ CH (CH ₃ ).
_{-, - CH 2 CH (CH} 2 OH) -, - CH 2 CH 2 CH 2 -, and is selected from the group consisting of mixtures thereof, each ^{R 4} _is, C 1 -C _{4 alkyl,} C 1 -C ₄ Hydroxyalkyl, a benzyl ring structure formed by combining two R ⁴ groups, —C
_{^{H 2 CHOH-CHOHCOR 6 CHOHCH 2}} OH ( wherein ^{R 6} is hexose polymer hexose or molecular weight of less than about 1000), and y is 0
Otherwise selected from the group consisting of hydrogen, R ⁵ is the same as R ⁴ or is an alkyl chain, where the total carbon number of R ² and R ⁵ is less than or equal to about 18 and each y is 0.
Is about 10 and the sum of y values is 0 to about 15 and X is all compatible anions.

[0070]   Suitable quaternary ammonium surfactants for the present invention have the formula (I):

[Chemical 4] Wherein R1 is short chain length alkyl (C6 to C10) or alkylamidoalkyl of formula (II),

[Chemical 5] Wherein y is 2 to 4, preferably 3, R2 is H or C1 to C3 alkyl, x is 0 to 4, preferably 0 to 2, most preferably 0, R3, R4 and R5 Are the same or different and are short-chain alkyl (C1 -C3) or alkoxylated alkyl of formula III, X ^- is a counterion, preferably a halide such as chloride or methylsulfate. is there.

[0071]

[Chemical 6] Wherein, R6 is _C 1 -C _4, z is 1 or 2.

Preferred quaternary ammonium surfactants are those of the formula I in which R ₁ is C ₈ , C ₁₀ or mixtures thereof, x = 0 and R ₃ , R ₄ = CH ₃ and R ₅ = A surfactant that is CH ₂ CH ₂ OH.

Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition, R ₁ R ₂ R ₃ R ₄ N ⁺ X ⁻ (i) having the formula ^: In the formula, R ₁ is C ₈ -C ₁₆ alkyl, and each of R ₂ , R ₃ and R ₄ is independently C ₁ -C ₄ alkyl, C ₁ -C ₄ hydroxyalkyl, benzyl, and-(C ₂ H _{40) x} H (a where x has a value of 2 to 5), X is an anion. No two or more of R ₂ , R ₃ or R ₄ should be benzyl.

Preferred alkyl chain lengths for R ₁ are in particular mixtures of chain lengths in which the alkyl groups are derived from coconut or palm kernel fat, or synthetically by olefin accumulation,
Alternatively, when it is produced by OXO alcohol synthesis, it is C _{12 to} C ₁₅ . Preferred groups for R ₂ , R ₃ and R 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 formula (i) suitable for use herein are coconut trimethylammonium chloride or bromide, coconut methyldihydroxyethylammonium chloride or bromide, decyltriethylammonium chloride, decyl Dimethylhydroxyethylammonium chloride or bromide, C _12-15 dimethylhydroxyethylammonium chloride or bromide, coconut dimethylhydroxyethylammonium chloride or bromide, myristyltrimethylammonium methylsulfate, lauryldimethylbenzylammonium chloride or bromide, lauryldimethyl ( _{ethenoxy) 4} ammonium chloride or bromide, choline esters (formula (i), _{R 1} is _{CH 2 -CH 2 -O-C-} C An _2-14 alkyl ‖ _O, compound _{R 2} R 3 R ₄ is methyl), di - alkyl imidazoline [compound of formula (i)].

Other cationic surfactants useful herein are US Pat. No. 4,228,044, Cambre, promulgated October 14, 1980, and European Patent Application No. E.
It is also described in the specification of P000,224.

Typical cationic fabric softening ingredients include water-soluble quaternary ammonium fabric softening actives, the most commonly used being di-long chain alkyl ammonium chlorides and methyl sulphates. is there. Among these, preferable cationic softening agents include 1) ditallow dimethyl ammonium chloride (DTDMAC), 2) dihydrogenated tallow dimethyl ammonium chloride, 3) dihydrogenated tallow dimethyl ammonium methyl sulfate, 4) dihydrogenated tallow dimethyl ammonium methyl sulfate. Stearyl dimethyl ammonium chloride, 5) Dioleyl dimethyl ammonium chloride, 6) Dipalmityl hydroxyethyl methyl ammonium chloride, 7) Stearyl benzyl dimethyl ammonium chloride, 8) Tallow trimethyl ammonium chloride, 9) Tallow trimethyl hydride ammonium chloride, _{10) C 12-14} alkyl hydroxyethyl dimethyl ammonium chloride, _{11) C 12-18} alkyl dihydroxyethyl methyl ammonium chloride, 12) di (stearoyl oxyethyl Dimethyl ammonium chloride (DSOE
DMAC), 13) di (tallowoyloxyethyl) dimethylammonium chloride, 14) ditallowimidazolinium methylsulfate, 15) 1- (2-tallowylamidoethyl) -2-tallowylimidazolinium methylsulfate Can be mentioned.

Biodegradable quaternary ammonium compounds have been developed as an alternative to the traditionally used two long chain alkyl ammonium chlorides and methyl sulphates. Such quaternary ammonium compounds contain long chain alkyl (alkenyl) groups interrupted by functional groups such as carboxy groups. Such materials and fabric softening compositions containing them are described in many publications, for example in European patent EP-A-0,040.
, 562 and EP-A-0,239,910.

Here, the quaternary ammonium compound and the amine precursor are represented by the following formula (I) or
Have (II).

[0080]

[Chemical 7] Wherein, Q is -O-C (O) -, - C (O) -O -, - O-C (O) -O-, NR 4 -C (O) -, - C (O) -NR is selected from ^{4, R 1} is ^{_{(CH 2) n -Q-T}} 2 or ^{T 3, R 2} is ^{_{(CH 2) m -Q-T}} 4 or ^{T 5} or ^{R 3, R 3} is C a ₁ -C ₄ alkyl or _C 1 -C ₄ hydroxyalkyl or H, ^{R 4} is H or _C 1 -C ₄ alkyl or _C 1 -C ₄ ^{hydroxyalkyl, T 1, T 2, T} 3, T ⁴ , T ⁵ are independently C ₁₁ -C ₂₂ alkyl or alkenyl, n and m are integers from 1 to 4, and X ⁻ is an anion compatible with the softening agent. Examples of anions compatible with emollients include, but are not limited to, chloride or methylsulfate.

The alkyl or alkenyl, chains T ¹ , T ² , T ³ , T ⁴ , T ⁵ must have at least 11, preferably at least 16 carbon atoms. The chain may be straight or branched. Tallow is a convenient, inexpensive source of long chain alkyl and alkenyl materials. Particularly preferred are compounds in which T ¹ , T ² , T ³ , T ⁴ , T ⁵ represent a mixture of long chain materials typical of tallow.

Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening composition of the present invention include: 1) N, N-di (tallowyl-oxy-ethyl) -N, N- Dimethylammonium chloride, 2) N, N-di (tallowyl-oxy-ethyl) -N-methyl, N- (2-hydroxyethyl) ammonium methylsulfate, 3) N, N-di (2-tallowyl-oxy- 2-oxo-ethyl) -N, N-dimethylammonium chloride, 4) N, N-di (2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl) -N, N-dimethylammonium chloride, 5) N -(2-Taroyl-oxy-2-ethyl) -N- (2-tallowyl-oxy-2-oxo-ethyl) -N, N-dimethylammonium chloride, 6) N, N, N -Tri (tallowyl-oxy-ethyl) -N-methylammonium chloride, 7) N- (2-tallowyl-oxy-2-oxo-ethyl) -N- (tallowyl-N, N-dimethylammonium chloride, and 8) 1,2-Ditarouyl-oxy-3-trimethylammoniopropane chloride, and mixtures of any of the above materials.

When included, the cleaning compositions of the present invention will typically be from 0.2 to about 25% by weight,
Preferably it comprises from about 1 to about 8% by weight of such a cationic surfactant.

Amphoteric Surfactants Amphoteric surfactants are also suitable for the cleaning compositions of the present invention. These surfactants are generally as aliphatic derivatives of secondary and tertiary amines, or of heterocyclic secondary and tertiary amines, where the aliphatic groups may be linear or branched. Can be explained. One of the aliphatic substituents has at least about 8 carbons, typically from about 8 to about 18, and at least one contains an anionic water-solubilizing group such as carboxy, sulfonate, sulfate. For examples of ampholytic surfactants, see US Pat.
929,678, published Dec. 30, 1975, Laughlin et al.,
See paragraphs 19, lines 18-35.

When included, the cleaning compositions of the present invention will typically be from 0.2 to about 15% by weight,
Preferably it comprises from about 1 to about 10% by weight of such an ampholytic surfactant.

Zwitterionic surfactants are also suitable for the zwitterionic surfactant cleaning composition. These surfactants include derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. Can be roughly described as. For examples of zwitterionic surfactants, see US Pat. No. 3,929,678.
Issue, December 30, 1975, promulgated in Laughlin et al., Paragraphs 19, 38.
See lines-paragraphs 22, 48, lines.

When included, the cleaning compositions of the present invention will typically be from 0.2 to about 15% by weight,
Preferably it comprises from about 1 to about 10% by weight of such zwitterionic surfactant.

Semipolar Nonionic Surfactants Semipolar nonionic surfactants are a special group of nonionic surfactants that contain one alkyl moiety having from about 10 to about 18 carbon atoms and A water-soluble amine oxide containing two moieties selected from the group consisting of alkyl and hydroxyalkyl groups having from about 1 to about 3 carbons, having about 10 carbons
A water-soluble phosphine oxide containing one alkyl moiety of about 18 to about 18 and two moieties selected from the group consisting of alkyl and hydroxyalkyl groups of about 1 to about 3 carbons; Mention may be made of water-soluble sulfoxides containing one alkyl moiety of 10 to about 18 and one moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of about 1 to about 3 carbon atoms.

Semi-polar nonionic detersive surfactants include amine oxide surfactants having the formula:

[0090]

[Chemical 8] In the formula, R ³ is alkyl, hydroxyalkyl, which has about 8 to about 22 carbon atoms,
Or an alkylphenyl group or a mixture thereof, and R ⁴ has a carbon number of about 2
An alkylene or hydroxyalkylene group of about 3 or a mixture thereof, wherein x is 0 to about 3 and each R ⁵ is an alkyl or hydroxyalkyl group of about 1 to about 3 carbon atoms, Alternatively, it is a polyethylene oxide group having 1 to 3 ethylene oxide groups. The R ⁵ groups can also be added to each other, for example through an oxygen or nitrogen atom, to form a ring structure.

These amine oxide surfactants include in particular C _{10 to} C ₁₈ alkyldimethylamine oxides, and C _{8 to} C ₁₂ alkoxyethyldihydroxyethylamine oxides. When included, the cleaning compositions of the present invention will typically be 0.
． 2 to about 15% by weight, preferably about 1 to about 10% by weight, of such a semipolar nonionic surfactant.

[0092] Co-surfactant cleaning composition of the present invention may further comprise a cosurfactant selected from the group of primary or tertiary amines.

[0093]   Suitable primary amines for use herein have the formula R₁NH_TwoWrapping amine with
In the formula, R₁Is C₆~ C₁₂, Preferably C₆~ C₁₀Alkyl chain or R _Four X (CH_Two)_nAnd X is -O-, -C (O) NH- or -NH-
, R_FourIs C₆~ C₁₂It is an alkyl chain and n is 1 to 5, preferably 3. R ₁ Alkyl chains may be linear or branched, up to 12, preferably less than 5
May be interrupted by the ethylene oxide portion of

A preferred amine according to the above formula is an n-alkylamine. Suitable amines for use herein can be selected from 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary amines include C8-C10 oxypropylamine, octyloxypropylamine, 2
-Ethylhexyl-oxypropylamine, laurylamidopropylamine and amidopropylamine.

Suitable tertiary amines for use herein include tertiary amines having the formula R ₁ R ₂ R ₃ N, where R _{1 and} R ₂ are C ₁ -C ₈ alkyl chains or

[Chemical 9] And a, _{R 3} is _C 6 _{-C 12,} preferably either a _C 6 _{-C 10} alkyl chain or _{R 3,} is _{R 4 X (CH 2) n} , wherein X is -O -, - C (O) NH- or a -NH-, _{R 4} is a _C 4 _{-C 12,} n is from 1 to 5, preferably 2 to
It is 3. R ₅ is H or C ₁ -C ₂ alkyl and x is 1-6.

R ₃ and R ₄ can be straight-chain or branched and the R ₃ alkyl chain can be interrupted by up to 12, preferably less than 5, ethylene oxide moieties.

Preferred tertiary amines have the formula R ₁ R ₂ R ₃ N, wherein R ₁ is a C 6 -C 12 alkyl chain and R _{2 and} R ₃ are C ₁ -C 3 alkyl or

[Chemical 10] And R ₅ is H or CH 3, and x = 1 to 2.

[0098]   Also preferred are amidoamines having the formula:

[0099]

[Chemical 11] Wherein R ₁ is C ₆ -C ₁₂ alkyl, n is 2-4, preferably n is 3 and R ₂ and R ₃ are C ₁ -C ₄ .

Most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, C8-10 oxypropylamine, Ncoco 1-3 diaminopropane, coconut alkyldimethylamine. , Lauryldimethylamine, laurylbis (hydroxyethyl) amine, cocobis (hydroxyethyl) amine, 2 mol propoxylated laurylamine, 2 mol propoxylated octylamine, laurylamidopropyldimethylamine, C8-10amidopropyldimethylamine And C10 amidopropyldimethylamine.

The most preferred amines for use in the composition are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Particularly desirable are n-dodecyldimethylamine and bishydroxyethylcoconut alkylamine and 7-fold ethoxylated oleylamine, laurylamidopropylamine and cocoamidopropylamine.

Conventional Detergent Enzymes The detergent compositions of the present invention may comprise, in addition to aged starch degrading enzymes, one or more enzymes that provide detergency, fabric protection and / or bactericidal effects. The enzyme includes cellulase, hemicellulase, peroxidase, protease, gluco-amylase, amylase, mannanase, xyloglucanase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase,
Keratanase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, malanase, β-glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase or a mixture thereof can be mentioned.

In fact, the detergent composition according to the invention preferably further comprises a conventional amylase, a conventional starch debranching enzyme or a conventional pullulanase type II, a protease and / or a lipase. Ordinary means that the amylase, starch debranching enzyme or pullulanase type II does not fall within the ReSI index defined in the present invention.

In fact, the inclusion of a combination of aged starch degrading enzymes and such conventional amylases, starch debranching enzymes or pullulanase type II in the detergent compositions of the present invention synergistically removes aged starch. I found out. Therefore, the detergent composition comprising such a combination of enzymes enhances the performance of removing stains and stains containing starch, and the ability of maintaining whiteness and cleaning thin stains. In addition, aged starches commonly found on textiles generally comprise large amounts of protein and triglyceride compounds. In particular, starch materials are typically associated with lipid compounds. Therefore, the detergent composition preferably comprises protease and / or lipase enzymes to enhance the removal of such complex substances.

As mentioned above, the detergent composition of the present invention preferably further comprises a conventional α-amylase. Α-Amylase suitable for the purpose of the present invention is described in the following documents. International Patent WO 94/02597, Novo Nordisk A / S, published February 3, 1994, discloses a cleaning composition incorporating a mutant amylase. International Patent No. WO 95/10603, Novo Nordisk A / S, 1995 4
See also on 20th of May. Other amylases known for cleaning compositions include both α- and β-amylases. Alpha-amylases are known in the art and are described in US Pat. No. 5,003,257, European Patent 252,666, International Patent WO 91/00353, French Patent 2,676,456, European Patent. Enzymes disclosed in 285,123, 525,610, 368,341, and British Patent 1,296,839 (Novo) are included. Other suitable amylases are described in International Patent No. WO 94/18314, 19
Published August 18, 1994, and WO 96/05295, Genencor, 1
Amylase with enhanced stability as described on February 22, 996, and commercially available from Novo Nordisk A / S as described in International Patent No. WO 95/10603, published April 1995, It is an amylase mutant further denatured by the immediate parent. In addition, European Patent No. 277216 and International Patent No. WO95 / 26
Also suitable are the amylases described in the respective specifications of 397 and WO 96/23873 (all from Novo Nordisk). Examples of commercially available α-amylase products are Purafect Ox Am (trade name) available from Genencor, and all Novo N
ordisk A / S, Termamyl (trade name), Ban (trade name), and Funga marketed in Denmark
These are myl (trade name) and Duramyl (trade name). International Patent No. WO95 / 2639
No. 7 shows that other specific amylase, namely Phadebas (trade name) α-amylase activity assay, has a specific activity of Termamyl (trade name) at a pH value of 8 to 10 in a temperature range of 25 ° C. to 55 ° C. Α-amylase, characterized in that it is at least 25% higher than the specific activity of). Variants of the above enzymes described in WO 96/23873 (Novo Nordisk) are preferred. Preferably, the variant is a variant demonstrating improved thermostability, more preferably F180.
, R181, G182, T183, G184, or K185, in which at least one amino acid residue is deleted from the parent α-amylase.
Particularly preferred is the amino acid deletion R181 ^* + G182 ^* or T183 ^* + G.
A mutant with improved thermal stability, comprising 184 ^* . Other amylolytic enzymes with improved properties with respect to activity levels and thermostability combined with high activity levels are described in WO 95/35382. Other suitable amylases are the H-stabilized α-amylase enzymes with improved stability described in International Patent No. WO 98/26078 by Genencor.

The starch degrading enzyme is present in the detergent composition of the present invention in an amount of 0.0001 to 2% by weight of the composition, preferably 0.00018 to 0.06% by weight, more preferably 0.0002.
Formulated in an amount of 4-0.048 wt% pure enzyme.

The starch debranching enzyme used in the compositions of the present invention can be obtained from a variety of sources. However, in general, starch debranching enzymes are of microbial origin. Preferred varieties of starch debranching enzymes are pullulanase type I, isopullulanases and isoamylases.

These enzymes are commercially available, examples of which are SP for pullulanase.
LENTASE (trade name) (manufactured by Amano Pharmaceutical Co., Ltd.) and PROMO
ZYME (trade name) 200L (manufactured by Novo Industri A / S), and isoamylase includes “isoamylase” (reagent, Seikagaku Kogyo Co., Ltd.). Such starch debranching enzymes are generally supplied in the form of granules and have an enzyme activity of about 1
It is from 0 ⁵ to 10 ⁸ units / liter.

Starch debranching enzymes are generally included in the detergent compositions according to the invention in an amount of 0.0001 to 10% by weight, preferably 0.001 to 0.5% by weight.

Pullulanase type I enzymes are classified under the IUPAC category EC 3.2.1.41 and the systematic name α-dextrin 6-glucano hydrolase. The pullulanase enzyme is 1 in pullulan, amylopectin and glycogen, and in α- and β-amylase limiting dextrins of amylopectin and glycogen.
, 6-α-D-Glucoside bonds, as well as branched oligosaccharides formed by their partial decomposition. Because of this feature, pullulanase is called a "debranching enzyme." In fact, pullulanase is an enzyme that breaks only the α-1,6-glycosidic bond of pullulan and ultimately produces maltriose. Microbial sources include Aerobacter Aerogenes, Pseudomonas stutzeri, Bacillus polymyxa
, B. maceranas, Klebsiella pneumonia and Streptomyces sp.
The activity of this enzyme is standardized at 200 PUN / g (pullulanase unit Novo). 1UPN reduces the reducing carbohydrates that release pullulan under standard conditions
It is defined as the amount of enzyme that hydrolyzes with a reducing power equal to μmol glucose / min. Also preferred is pullulanase isolated from a strain of Bacillus No. 202-1, as described in Biochimica et Biophysica Acta, 397 (1985) 188-193. This pullulanase has an optimum pH of about 8.55-9.0 and is therefore of particular importance in highly alkaline detergent compositions.

Pullulanase was described by Bender and Wallenfels in 1961 in Aerobacter aerog.
It was first discovered from a strain belonging to enes [Biochem. Z., 334, 79, (1961)]. In recent years, various microorganisms capable of producing pullulanase have been reported. These microorganisms are known, for example, in Bacillus sp. [J. Jpn. Soc. Starch Sci., 30, 200, (1983)], Bacil
lus acidopullulyticus [Agric. Biol. Chem., 52, 2293, (1984)], Bacillus st
earothermophilus [Eur. J. Appl. Microbiol. Biotechnol., 17, 24, (1983)],
Streptococcus mitis-[Biochem, J., 108, 33, (1968)], Lactobacillus [Den
pun Kagaku, 28, 72 (1981)], Clostridium sp. [Appl., Environ. Microb., 53
, 7 (1987)], Clostridium thermohydrosulfuricum [Appl., Environ. Microb.,
49, 5, (1985), J. Bacteriol., 164, 3, (1985), Biochem. J., 246, (1987)]
, Thermus aquaticus [Enzyme Microb. Technol., 8, (1986)], Thermus sp. [J.
Jpn. Soc. Starch Sci., 34, 1, (1987)] and Clostridium thermosulfurogene
s [Appl. Microb. Biotechnol., 33, 511, (1990)]. In addition, two publications report methods for making alkaline or alkaline resistant pullulanases. That is, Horikoshi et al. Cultivated an alkaline alkaline strain of the genus Bacillus (Bacillus sp. 202-1) to produce alkaline pullulanase (Japanese Patent No. 27).
7786/1978) and International Patent No. WO94 / 19468 (Published Japanese Patent Application No. 87176/1991).
It is an alkaline pullulanase obtained from cillus sp. KSM-AP 1876.

Related pullulanases include, for example, pullulanases obtained from Bacillus varieties (eg B.
acidopullulyticus, such as Promozyme ™ from Novo Nordisk A / S). Other pullulanases suitable for the detergent compositions of the present invention are alkaline pullulanases described by Kao Corporation in EP450627, which have a pH optimum in the alkaline region and are stable to surfactants. Is. Such alkaline pullulanases include alkaline pullulanase A and alkaline pullulanase B, both suitable for the purposes of the present invention. Other alkaline pullulanases suitable for detergents are described in International Patent No. WO94 / 1946 by Kao Corporation.
No. 8 specification. The pullulanase enzyme described in the following Japanese patents / applications is also suitable. All Japanese patent JP0 by Kao Corporation
No. 4073298 describes a nonionic surfactant, a calcium chelating agent,
Regarding an automatic dishwashing detergent composition for high detergency comprising lipase and alkaline pullulanase, Japanese Patent No. JP062644094 discloses a soap,
A highly detersive laundry detergent composition comprising a surfactant and an alkali resistant pullulanase is described. A particularly preferred enzyme is the Pullulanase Promozyme (trademark of Novo) isolated from Bacillus sp. Pullulanase.

Isopullulanases are classified under the IUPAC category EC 3.2.1.57 and the systematic name pullulan 4-glucanohydrolase. The isopullulanase enzyme hydrolyzes pullulan to isopanose (6-α-maltosyl glucose).

Isoamylase : Isoamylase is capable of debranching glycogen.
These enzymes have been detected in various microorganisms including B. amyloliquefacines, Cytophaga sp., P. amyloderamosa and Streptomyces sp. No. 28. The activity of this enzyme is given in MU (maltose units). 1 MU is defined as the amount of enzyme that, under standard conditions, hydrolyzes a reduced carbohydrate releasing isoamylose with a reducing power equal to 1 μmol maltose / min.

Isoamylases are classified under the IUPAC category EC 3.2.1.68 and the systematic name glycogen 6-glucanohydrolase. The isoamylase enzyme is 1,6-α in glycogen, amylopectin and their β-limit dextrins.
-Hydrolyze D-glucoside branch bonds. Isoamylases are distinguished from pullulanase enzymes by their inability to attack pullulan, their limited action on α-limit dextrins, and their full action on glycogen. Related isoamylases include Pseudomonas varieties (eg Pseudomonas sp. SMP1 or Pseudomonas amyloderomosa SB15), Bacillus varieties (eg B. amyloliquef
aciens), Flavobacterium varieties or Cytophaga (Lysobacter) varieties. Isoamylases are Sigma, ICN and Hayashibara
Is commercially available from.

The following Japanese patents / applications, that is, Japanese patents JP07179900, JP06172769, and JP0617279, all issued by Kao Corporation.
No. 2, JP04065494, JP02132193 and JP02.
Also suitable are the pullulanases, isopullulanases and iso-amylases described as starch debranching enzymes in the specifications of 132192.

The pullulanase type II enzyme is defined as amylopulllanase, which randomly hydrolyzes the α, 1-4 bonds in addition to the branch points (α-1,6-bonds) in polysaccharides and dextrins, This is in contrast to pullulanase type I enzymes, which hydrolyze only α, 1-6 bonds in branched-chain polysaccharides.

Pullulanase type II is used for extremophiles, especially hyperthermophilic and hyperthermophilic microorganisms such as Pyrococcus woesei, P. furiosus, as described in “A new Bacterial World” Extremophiles, 1997, 1: 2-13. Thermococcus litoralis, Th
ermococcus celer, Desulfurococcus mucosus, Bacteroides thetiaotaomicron
, Staphylothermmus marinus, Pyrodictium abysii, Bacillus stearothermophi
It can be obtained from microorganisms isolated from lus. Other pullulanases suitable for the purposes of the present invention are the alkaline pullulanases which exhibit alkaline α-amylase activity as described in WO 96/35794. Also suitable is alkaline pullulanase Y having α-amylase activity as described in EP 418835, which has an optimum pH in the higher alkaline region than normal alkaline pullulanase and a broad pH range. It exhibits excellent pH stability in the range and strong resistance to almost all detergent ingredients such as surfactants, chelating agents and proteases.

Combined pullulanase-amylase enzyme produced by Bacillus subtilis TU
(Agric. Biol. Chem., 51, 9. (1987), Published Japanese Patent No. 18717/1989.
Specification) is also suitable.

Pullulanase type II is generally 0.0001-1 in the detergent composition of the present invention.
It is contained in an amount of 0% by weight, preferably 0.001 to 0.5% by weight.

Suitable lipase enzymes are microorganisms of the Pseudomas family, for example British Patent No. 1,372.
, 034, Pseudomas stutzeri ATCC 19.154, described herein. The preferred lipase is the microorganism Pseudomonas fluorescent.
Includes lipases produced by IAM 1057 that exhibit a positive immunological cross-reactivity with lipase antibodies. This lipase is commercially available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan under the trade name of Lipase P "Amano" (hereinafter referred to as "Amano-P"). Other suitable commercially available lipases include Amano-CES, Toyo Jozo Co.,
Chromobacter viscosum, eg Chromob, commercially available from Tagata, Japan
lipase from acter viscosum var. lipolyticum NRRLB 3673, US Bioch
Chromobacter v available from emical Corp., USA and Disoyynth Co., The Netherlands
There are iscosum lipases and lipases derived from Pseudomonas gladioli. Particularly preferred lipases are M1 Lipase (trade name) and Lipomax (trade name) (Gist-Broc
Lipases such as ades) and Lipolase ™ and Lipolase Ultra ™ (Novo) have been found to be very effective when used in combination with the compositions of the present invention. Novo Nordisk, European Patent No. 258068, International Patent Nos. WO92 / 05249 and WO95 / 22615, and Unil.
Also suitable are the lipolytic enzymes described by ever in WO 94/03578, WO 95/35381 and WO 96/00292.

A cutinase [EC 3.1.1.50] is also suitable but is considered to be a special type of lipase, ie a lipase which does not require surface activation. Addition of cutinase to detergent compositions is described, for example, in International Patent No. WO-A-88 / 09.
367 (Genencor), WO90 / 09446 (Plant Genetic System) and WO94 / 14963 and WO94 / 14964 (Unilever).

The lipase and / or cutinase is generally included in the detergent composition in an amount of 0.0001 to 2% pure enzyme by weight of the detergent composition.

A preferred protease is subtilisin (subtilisin BPN and BPN ') obtained from specific strains of B. Subtilis and B. licheniformis. One suitable protease is obtained from Bacillus strains, has maximum activity in the pH range 8-12 and was developed by Novo Industries A / S of Denmark, hereafter "Novo", ESPERASE
It is sold as (product name). The production of this enzyme and similar enzymes is described in Novo UK Patent No. 1,243,784. Other suitable proteases include ALCALASE ™, DURAZYM ™ and SAVIN ™ commercially available from Novo.
ASE (trade name), MAXATASE (trade name), MAXACAL (trade name), PROPERASE (trade name), and MAXAPEM (trade name) commercially available from Gist-Brocades (protein-engineered MA
XACAL). The present invention includes proteases described in patent application EP 251446 and International Patent No. WO91 / 06637, protease BLAP (trade name) described in International Patent No. WO91 / 02792, and Also suitable are variants thereof, which are described in WO 95/23221. See also the high pH protease obtained from Bacillus sp. NCIMB 40338 as described in WO 93 / 18140A to Novo. Enzymatic detergents comprising a protease, one or more other enzymes, and a reversible protease inhibitor are described in International Patent No. WO 92/03529 to Novo.
If desired, there are also proteases with reduced adsorptivity and increased hydrolyzability, such as those described in WO 95/07791 to Procter & Gamble.
A preferred recombinant trypsin-like protease for detergents herein is the International Patent No. W
O94 / 25583. Other suitable proteases are Un
ilever European Patent 516200.

The proteolytic enzyme may be a modified bacterial serine protease such as European Patent Application No. 87303761.8 filed April 28, 1987 (particularly 17,
24 and 98), referred to herein as the enzyme referred to as "Protease B", and to modified bacterial serine proteolytic enzymes, European Patent Application No. 199,404, Venegas, October 29, 1986. Included herein is an enzyme referred to herein as "Protease A", which is described in Japanese Submission. A protease referred to herein as "Protease C" is preferred, which is a variant of the alkaline serine protease obtained from Bacillus , in which lysine produces 27 arginine.
Position, tyrosine replaces valine at position 104, serine replaces asparagine at position 123, and alanine replaces threonine at position 274. Protease C is described in International Patent No. WO 91/06637. Also included herein are genetically modified variants, especially variants of Protease C.

A preferred protease, referred to as “Protease D”, is a variant of a carbonyl hydrolase having an amino acid sequence not found in nature, which is derived from the precursor carbonyl hydrolase from International Patent No. WO 95/10591. Bacillus amyloli as described in WO 95/10592 and WO 95/10592.
According to the quefaciens subtilisin numbering, a plurality of amino acid residues at a position equal to position +76 in the carbonyl hydrolase is preferably +99, +101.
, +103, +104, +107, +123, +27, +105, +109, +
126, +128, +135, +156, +166, +195, +197, +2
04, +206, +210, +216, +217, +218, +222, +26
1 equal to a position selected from the group consisting of 0, +265 and / or +274
It is obtained by combining with amino acid residue positions of more than one species and substituting different amino acids. The "Protease D" variant is preferably the amino acid substitution set 76/103/104, more preferably the substitution set N76D / S103A / V.
Has 104I. Also suitable are the carbonyl hydrolase variants of the proteases described in WO95 / 10591, which contain a plurality of amino acid residues corresponding to the +210 position in the precursor enzyme as described below. Residues: +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, obtained by substituting in combination with one or more, and the numbered positions are the natural subtilisins or other carbonyl hydrolases or subtilisins obtained from Bacillus amyloliquefaciens,
For example, it corresponds to the equivalent amino acid residue in Bacillus lentus subtilisin (pending application WO 98/55634). More preferred proteases are protease variants with multiple substitutions. These protease variants have amino acid residues replaced by other natural amino acid residues, Bacillus
amyloliquefaciens subtilisin comprising substitution at the amino acid residue position corresponding to position 103 of Bacillus amyloliquefaciens subtilisin 1, 3
4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21, 22
, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61
, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97
, 98, 99, 101, 102, 104, 106, 107, 109, 111, 1
14, 116, 117, 119, 121, 123, 126, 128, 130, 1
31, 133, 134, 137, 140, 141, 142, 146, 147, 1
58, 159, 160, 166, 167, 170, 173, 174, 177, 1
81, 182, 183, 184, 185, 188, 192, 194, 198, 2
03, 204, 205, 206, 209, 210, 211, 212, 213, 2
14, 215, 216, 217, 218, 222, 224, 227, 228, 2
30, 232, 236, 237, 238, 240, 242, 243, 244, 2
45, 246, 247, 248, 249, 251, 252, 253, 254, 2
55, 256, 257, 258, 259, 260, 261, 262, 263, 2
65, 268, 269, 270, 271, 272, 274, and 275 in combination with the replacement of amino acid residues with other natural amino acid residues at one or more amino acid residue positions corresponding to positions. Contains a substitution of amino acid residues at positions corresponding to positions 103 and 76, Bacillus amyloliqu
efaciens subtilisin 27, 99, 101, 104, 107, 109, 123
, 128, 166, 204, 206, 210, 216, 217, 218, 222
There is also a substitution of amino acid residues at one or more amino acid residue positions other than the amino acid residue positions corresponding to positions 260, 265 or 274, and / or all 1's
Multiple substitutions, as described in PCT applications Nos. PCT / US98 / 22588, PCT / US98 / 22482 and PCT / US98 / 22486 filed October 23, 998 by The Procter & Gamble Company. Protease variants were Bacillus amyloliquefaciens subtilisin 62, 212, 2
Substituting amino acid residues with other natural amino acid residues at one or more amino acid residue positions corresponding to positions 30,232,252 and 257. A preferred multiple-substituted protease variant is the amino acid substitution set 101/103/104/159/23 by Bacillus amyloliquefaciens subtilisin numbering.
2/236/245/248/252, more preferably 101G / 103A / 1
It has 04I / 159D / 232V / 236H / 245R / 248D / 252K.

The composition of the invention may further comprise other enzymes. Cellulases that can be used in the present invention include both bacterial or fungal cellulases. Preferably, these cellulases have an optimum pH of 5-12 and a specific activity of 50 CEVU / mg.
(Cellulose viscosity unit) is exceeded. Suitable cellulases are Barbesgoard et al
Of U.S. Pat. Sporotrichu
Disclosed is a fungal cellulase produced from m. European Patent No. 73998
No. 2 discloses cellulases isolated from a novel Bacillus variety.
Suitable cellulases are described in British Patent GB-A-2,075,028, GB-A.
No. 2,095,275, German Patent DE-OS-2,247,832, and International Patent No. WO95 / 26398.

Examples of such cellulases include Humicola insolens (Humicola grisea var. Ther
moidea), in particular Humicola strain DSM 1800.

Another suitable cellulase is obtained from Humicola insolens, having a molecular weight of about 50 K.
Da, an isoelectric point of 5.5, a cellulase containing 415 amino acids, and Humicola i
nsolens, DSM 1800 and is a ~ 43kD endoglucanase showing cellulase activity, the preferred endoglucanase component being International Patent No. WO 91/17243.
Has the amino acid sequence disclosed in the specification. International Patent No. WO to Genencor
A suitable cellulase is also EGIII cellulase obtained from Trichoderma longibrachiatum described in Japanese Patent No. 94/21801. A particularly suitable cellulase is a cellulase with color-protecting properties. Examples of such cellulases are described in European Patent Application No. 91202879.2, filed Nov. 6, 1991 (Novo).
, A cellulase described in. Carezyme and Celluzyme (Novo Nordisk
A / S) is especially useful. International Patent Nos. WO 91/17244 and WO 91
See also / 21801. Other cellulases suitable for fabric protection and / or laundry properties are described in International Patents WO 96/34092, WO 96/17994,
And WO 95/24471. The cellulase is generally incorporated into the detergent composition in an amount of 0.0001 to 2% pure enzyme by weight of the detergent composition.

Peroxidase enzymes are used in combination with oxygen sources such as percarbonates, perborates, persulfates, hydrogen peroxide, etc., and phenolic substrates as bleach enhancing molecules. These enzymes are used to "solution bleach", ie to prevent dyes or pigments removed from the substrate during the washing operation from migrating to other substrates present in the laundry solution. Peroxidase enzymes are known in the art, such as horseradish peroxidase, ligninase, and haloperoxidase,
Examples include chloro- and bromoperoxidase. Detergent compositions containing peroxidase are described, for example, in PCT International Application No. WO 89/099813, W.
O89 / 09813, and European Patent Application No. 91202882.6,
No. 9687001.8, filed Nov. 6, 1991, filed Feb. 20, 1996, respectively. Laccase enzymes are also suitable.

Reinforcing agents are generally included in amounts of 0.1 to 5% by weight of the total composition. Preferred tougheners are substituted phenothiazine and phenoxazine, 10-phenothiazinepropionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (
EPC), 10-phenoxazine propionic acid (POP) and 10-methylphenoxazine (described in WO 94/12621), substituted syringates (C3 to C5 substituted alkyl syringates), phenol. And mixtures thereof. Sodium percarbonate or sodium perborate are the preferred sources of hydrogen peroxide.

The peroxidase is generally present in a detergent composition in an amount of 0.0001 to
Formulated in the amount of 2% by weight pure enzyme.

The above enzymes may be from any suitable source, for example plants, animals, bacteria, fungi and yeast. The origin may further be mesophilic or exstremophilic (cryotrophic, psychrotrophic, thermophilic, pressureophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or unpurified forms of these enzymes can be used. It is common today to denature wild-type enzymes by protein / genetic engineering techniques and optimize their performance efficiency with the laundry detergent and / or fabric protection compositions of the present invention. . For example, variants can be designed to increase the compatibility of the enzyme with the components commonly used in such compositions. Alternatively, the variants can be designed such that the optimum pH of the enzyme variant, stability to bleaching or chelating agents, catalytic activity, etc. are compatible with a particular cleaning application.

In particular, attention should be paid to amino acids that are sensitive to oxidation in the case of bleach stability and to surface charges for compatibility of surfactants. The isoelectric point of such an enzyme can be changed by substituting a part of charged amino acids, and for example, the increase of the isoelectric point may improve the compatibility with an anionic surfactant. Enzyme stability can be further enhanced by, for example, forming additional salt bridges, forcing calcium binding sites, and increasing chelator stability. Special attention should be paid to cellulases, as most cellulases have separate binding domains (CBD). The properties of such enzymes can be altered by denaturing these regions.

Enzymes can be added as individual single components (prills containing one enzyme, granules, stabilized liquids, etc.) or as a mixture of two or more enzymes (eg cogranulates).

Other suitable detergent ingredients that can be added are European patent application No. 9 under examination.
No. 287008.6, filed on Jan. 31, 1992, and is an enzyme antioxidant. An example of such an enzymatic antioxidant is ethoxylated tetraethylene polyamine.

A series of enzyme materials and means of incorporation into synthetic detergent compositions have been described by Genencor Internati.
International Patent Nos. WO93 / 07263A and WO93 / 07260A to onal
No. WO89 / 08694A to Novo, and US Pat. No. 3,553,139 to McCarty et al. Enzymes are described in US Pat.
101,457, Place et al, July 18, 1978, and 4,
No. 507,219, Hughes, March 26, 1985. Enzyme materials that are particularly useful in liquid detergent formulations, and the incorporation of those enzymes into such formulations, is described in US Pat. No. 4,261,868, Hora et al, April 14, 1981. Have been described. Enzyme stabilization techniques are described, for example, in US Pat.
0,319, August 17, 1971, Gedge et al., EP 199,405 and EP 200,586.
Venegas, 29 October 1986. Enzyme stabilization systems are also described in US Pat. No. 3,519,570. A useful Bacillus, sp. AC13 producing protease, xylanase and cellulase is WO94 / 0 to Novo.
1532A.

Bleach Other preferred components of the detergent compositions of the present invention include bleach. In fact, it has been found that oxidizing the starch material with bleach increases the solubility of the starch material and thus is more easily removed. In addition, the bleaching agent makes it easier to wash thin soils by reducing the overall color of the treated fabric. Therefore, by further containing a bleaching agent in the composition of the present invention, removal of stains and stains containing starch is improved, and maintenance of whiteness and cleaning of thin stains are mainly improved.

Bleaching agents suitable for the purposes of the present invention include hydrogen peroxide, PB1, PB4 and particle size 4
Examples include percarbonates of 00 to 800 microns. These bleach components can include one or more oxygen bleaches and, depending on the bleaching agent selected, one or more bleach activators. The oxygen bleaching compound, if present, is typically from about 1% to about 2%.
Present in an amount of 5%.

The bleach component used herein can be any of the bleaches useful in detergent compositions, including oxygen bleaches as well as other bleaches known in the art. The bleach suitable for the present invention may be an activated or non-activated bleach.

One group of oxygen bleaches that can be used includes percarboxylic acid bleaches and their salts. Suitable examples of this type of bleaching agent include magnesium monoperoxyphthalate hexahydrate, magnesium salt of metachloroperbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxidedecanedioic acid. Such bleaching agents are described in U.S. Pat. No. 4,483,781, U.S. Patent Application No. 740,4.
46, European Patent Application No. 0,133,354, and U.S. Pat. No. 4,412,934. U.S. Pat.
6-nonylamino-6-oxoperoxycaproic acid, described in 551, is also a highly preferred bleaching agent.

Another group of bleaches that can be used includes halogen bleaches. Examples of hypohalide bleaching agents include trichloroisocyanuric acid and sodium and potassium dichloroisocyanurates and N-chloro and N-bromoalkanesulfonamide. Such materials are usually added in amounts of 0.5 to 10% by weight of the final product, preferably 1 to 5%.

Hydrogen peroxide releasing agents include bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene sulfonate (NOBS, described in US Pat. No. 4,412,934), 3,5- Trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or pentaacetyl glucose (PAG) or phenolsulfonate ester of N-nonanoyl-6-aminocaproic acid (NACA-OBS).
, International Patent No. WO 94/28106), these substances, by perhydrolysis, form peracids as active bleaching substances and improve the bleaching effect. For example European patent application 918702 under examination
Acylated citrates and Procte as described in EP 07.7
US Patent Application No. 60 / 022,786 (submitted July 30, 1996) and No. 60 / 028,122 (October 1, 1996)
Asymmetric acyclic imide bleach activators having the formula:

[0144]

[Chemical 12] In the formula, R ₁ is a C _{7 to} C ₁₃ linear or branched saturated or unsaturated alkyl group, and R ₂ is a C _{1 to} C ₈ linear or branched saturated or unsaturated alkyl group. And R ₃ is a C ₁ -C ₄ linear or branched saturated or unsaturated alkyl group.

Bleaching agents, including peracids, and bleaching systems comprising bleach activators and peroxygen bleaching compounds useful in the detergent compositions of the present invention are described in our pending application, USSN 0.
8 / 136,626, PCT / US95 / 07823, International Patent No. WO95
/ 27772, WO95 / 27773, WO95 / 27774, and WO95 / 27775.

Hydrogen peroxide can also be present by adding an enzyme system capable of generating hydrogen peroxide (ie an enzyme and a substrate therefor) at the beginning or during the washing and / or rinsing process. Such an enzyme system is described in European Patent Application No. 9
1202655.6, filed October 9, 1991.

[0147]   Metal-containing catalysts used in bleach compositions include cobalt-containing catalysts such as penta
Amine acetate cobalt (III) salts and manganese-containing catalysts, such as Europe
Patent Application Nos. EPA549271, EPA549272, EPA4583
97, US Pat. No. 5,246,621, European Patent EPA 45839.
No. 8, US Pat. Nos. 5,194,416 and 5,114,611
And the catalysts described in the book. Bleach containing peroxy compounds and manganese
Bleaching compositions comprising an agent catalyst and a chelating agent are described in Patent Application No. 948702.
No. 06.3. Bleaching compounds are catalyzed by manganese compounds
Can be used. Such compounds are well known in the art, eg
U.S. Patents 5,246,621, 5,244,594, 5,194,4
16, 5,114,606, and published European patent application 549,2.
71A1, 549, 272A1, 544, 440A2, and 54
4,490A1, the manganese-based catalysts disclosed in the respective specifications are included. This
Preferred examples of these catalysts include Mn^IV _Two(u-O)_Three(1,4,7-trimethyl
-1,4,7-Triazacyclononane)_Two-(PF₆)_Two, Mn^III _Two(u-O)₁ (u-OAc)_Two(1,4,7-Trimethyl-1,4,7-triazacyclononane
)_Two-(ClO_Four)_Two, Mn^IV _Four(u-O)₆(1,4,7-triazacyclononane
)_Four-(ClO_Four)_Four, Mn^IIIMn^IV _Four(u-O)₁(u-OAc)_Two (1,4
, 7-trimethyl-1,4,7-triazacyclononane)_Two-(ClO_Four)_Three, Mn ^IV (1,4,7-trimethyl-1,4,7-triazacyclononane (OCH_Three )_Three-(PF₆) And mixtures thereof. Better to use here
The preferred material is a transition metal bleach catalyst, which is described, for example, in Procter & Gamble's patent.
Applications WO98 / 39405, WO98 / 39406 and WO98 /
Transition metals and cross-bridges such as those described in each of the '39098 patents.
It is a complex of a large polycyclic ligand. The most preferred substance is of the formula [Mn (Bcycl
am) Cl_Two] Mn complex bleach catalyst of the above, represented by the following formula.

[0148]

[Chemical 13] "B-cyclam" (5,12-dimethyl-1,5,8,12-tetraazabicyclo [6.6.2] hexadecane) Such transition metal bleach catalysts are described in Procter & Gamble patent application WO98 / Three
9335 or J. Amer. Chem. Soc., (1990), 112, 8604.

Bleaching agents other than oxygen bleaching agents are known in the art and can be used herein. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as sulfonated zinc and / or aluminum phthalocyanines. These materials can be deposited on the substrate in a cleaning process. Activation of the sulfonated zinc phthalocyanine by illuminating it in the presence of oxygen, for example hanging and drying the garment in outdoor sunlight, results in bleaching of the substrate. Preferred zinc phthalocyanines and photoactive bleaching methods are described in US Pat. No. 4,033,718. Typically, the detergent composition comprises from about 0.025 to about 1.25% by weight sulfonated zinc phthalocyanine.

Color and Fabric Protection Properties Techniques that provide certain color protection properties can also be included. An example of these techniques is a metallocatalyst for color retention. Such metallocatalysts are described in pending European patent application No. 92870181.2. Color protection /
Other examples of fabric protection techniques are dye fixatives, polyolefin dispersions for anti-wrinkle and water absorption improvements, perfumes and amino-functional polymers for color protection and perfume adhesion, pending patent application 96870140. No. 9 specification, November 7, 1996
Submitted on the day.

A fabric softening agent may also be incorporated into the detergent composition of the present invention. These agents may be inorganic or organic. Representative inorganic softening agents are the smectite clays described in British Patent GB-A-1400898 and US Pat. No. 5,019,292. Organic fabric softening agents include
British Patent GB-A-1514276 and European Patent EP-B.
Water-insoluble tertiary amines described in 0011340 and their European patents EP-B-0026527 and EP-B-.
0026528 in combination with mono C12 to C14 quaternary ammonium salts, and the double long chain amides described in EP-B-0242419. Other useful organic components of the fabric softening system include the high molecular weight polyethylene oxide materials described in EP-A-0299575 and EP 0313146.

The smectite clay is added to the rest of the formulation as a dry mix component, generally in an amount of 2 to 20% by weight, more preferably 5 to 15% by weight. Organic fabric softening agents, such as water insoluble tertiary amine or two long chain amide materials, are 0.5 to 5
%, Generally 1-3% by weight, with the high molecular weight polyethylene oxide material and water-soluble cation-based material being 0.1-2% by weight, typically 0.15-1.
Add in an amount of 5% by weight. These materials are generally added to the spray-dried portion of the composition, but in some cases it is more convenient to add them as dry mixed particles or to spray them as a molten liquid onto other solid components of the composition. is there.

Builder System The composition of the present invention may further comprise a builder system. All customary builder systems are suitable for use, materials such as aluminosilicate materials, silicates, polycarboxylates, alkyl- or alkenyl-succinic acids and fatty acids, ethylenediaminetetraacetic acid, diethylenetriaminepentamethyleneacetate, metals. Ion sequestering agents such as aminopolyphosphonates, especially ethylenediaminetetramethylenephosphonic acid and diethylenetriaminepentamethylenephosphonic acid. Phosphate builders can also be used here.

Suitable builders are inorganic ion exchange materials, generally inorganic hydrated aluminosilicate materials, more particularly hydrated synthetic zeolites such as hydrated zeolites A, X, B,
It can be HS or MAP.

Another suitable inorganic builder material is layered silicates such as SKS-6 (Hoechst).
Is. SKS-6 is a crystalline layered silicate composed of sodium silicate (Na ₂ Si ₂ O ₅ ).

Suitable carboxylates containing one carboxy group include Belgian Patent No. 831
Examples include lactic acid, glycolic acid and their ether derivatives as described in the respective specifications of 368, 821,369 and 821,370. Two
Polycarboxylic acid salts containing one carboxy group include succinic acid, malonic acid, (ethylenedioxy) diacetic acid, maleic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid, and water-soluble salts thereof. No. 2,446,686 and No. 2,
446, 687 and U.S. Pat. No. 3,935,257, ether carboxylates, and Belgian Patent 840,623, sulfinyl carboxylates. Polycarboxylates containing three carboxy groups include especially water-soluble citrate, aconitate and citraconic acid salts, and succinate derivatives such as British Patent 1,379,241.
Carboxymethyl oxysuccinate described in US Pat. No. 6,025,086, lactoxysuccinate described in Dutch application No. 7205873, and oxypolycarboxylate materials such as British Patent No. 1,387, 2-oxa-1,1,3-propanetricarboxylic acid salt described in Japanese Patent No. 447 is mentioned.

Polycarboxylic acid salts containing four carboxy groups are described in British Patent 1,261,8
Oxydisuccinates, 1,1,2,2-ethanetetracarboxylic acid salts, 1,1,3,3-propanetetracarboxylic acid salts and 1,1 described in No. 29.
, 2,3-propane tetracarboxylic acid salt. Polycarboxylic acid salts containing sulfo substituents include British Patents 1,398,421 and 1,398,42.
2, and US Pat. No. 3,936,448, sulfosuccinate derivatives, and GB 1,082,179, sulfonated pyrolytic citric acid. Salts, including polycarboxylic acid salts containing phosphon substituents, are described in British Patent 1,439,000.

Cycloaliphatic and heterocyclic polycarboxylic acid salts include cyclopentane-cis, cis,
Cis-tetracarboxylic acid salt, cyclopentadienide pentacarboxylic acid salt, 2,3
, 4,5-Tetrahydrofuran-cis, cis, cis-tetracarboxylic acid salt, 2,
5-Tetrahydrofuran-cis-dicarboxylate, 2,2,5,5-tetrahydrofuran-tetracarboxylate, 1,2,3,4,5,6-hexane-hexacarboxylate, and polyhydric alcohols such as Carboxymethyl derivatives of sorbitol, mannitol and xylitol are mentioned. Aromatic polycarboxylic acid salts include the mellitic acid, pyromellitic acid and phthalic acid derivatives described in British Patent 1,425,343. Of the above, the preferred polycarboxylates are hydroxycarboxylates containing up to 3 carboxy groups per molecule, especially citrates.

Preferred builder systems for use in the present composition are water insoluble aluminosilicate builders such as Zeolite A or layered silicate (SKS-6), and water soluble carboxylate chelating agents such as A mixture of citric acid. Other preferred builder systems are water insoluble aluminosilicate builders such as Zeolite A,
And a water-soluble carboxylate chelating agent, such as citric acid. Preferred builder systems for use in the liquid detergent composition of the present invention are soaps and polycarboxylates.

Other builder materials that may form part of the builder system used in the granular composition include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as organic materials. Phosphonates, aminopolyalkylenephosphonates and aminopolycarboxylates.

Other suitable water-soluble organic salts are homopolymeric or copolymeric acids in which the polycarboxylic acid comprises at least two carboxyl groups separated from each other by not more than two carbon atoms. Or their salts. Polymers of this type are described in British Patent GB
-A-1,596,756. Examples of such salts are polyacrylates having a molecular weight of 2000 to 5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of 20,000 to 70,000, in particular about 40. 1,000.

Detergent builder salts are generally 5-80% by weight of the composition, preferably 10-7.
It is included in an amount of 0% by weight, most commonly 30-60% by weight.

Chelating Agents The cleaning compositions of the present invention can also optionally include one or more iron and / or manganese chelating agents. Such chelating agents can all be selected from the group consisting of aminocarboxylates, aminophosphonates, polyfunctionally substituted aromatic chelating agents and mixtures thereof, as described below. Without wishing to be bound by theory, it is believed that the benefits of these materials are due, in part, to their exceptional ability to remove iron and manganese from laundry solutions by forming soluble chelates.

Aminocarboxylates that are optionally used as chelating agents include:
Ethylenediaminetetraacetate, N-hydroxyethylethylenediaminetriacetate, nitrilotriacetate, ethylenediaminetetrapropionate, triethylenetetraaminehexaacetate, diethylenetriaminepentaacetate, and ethanoldiglycine, their alkali metal, ammonium, and substituted ammonium salts, and them There is a mixture of.

Aminophosphonates are also useful as chelating agents in the compositions of the present invention when at least a small amount of total phosphorus content is acceptable in the detergent composition, and ethylenediaminetetrakis (methylenephosphonate) such as DEQUEST. ). These aminophosphonates are preferably free of alkyl and alkenyl groups having more than about 6 carbon atoms.

Polyfunctionally substituted aromatic chelating agents are also useful in the compositions of the present invention. See U.S. Pat. No. 3,812,044, issued May 21, 1974, Connor et al. A preferred compound of this type in the acid form is a dihydroxydisulfobenzene, such as 1,2-dihydroxy-3,5-disulfobenzene.

A preferred biodegradable chelating agent for use herein is ethylenediamine disuccinate (“EDDS”), particularly US Pat. No. 4,704,233, 1
Promulgated in Hartman and Perkins, November 3, 987 [S, S
] Is an isomer.

The compositions of the present invention are co-builders that can also be used with water-soluble methylglycine diacetic acid (MGDA) salts (or acid forms) as chelating agents or with insoluble builders such as zeolites, layered silicates, and the like. Can be included as

When used, these chelating agents will generally comprise about 0 of the detergent compositions of the present invention.
． 1 to about 15% by weight. More preferably, when used, these chelating agents comprise from about 0.1% to about 3.0% by weight of such compositions.

Foam Inhibitors Another optional ingredient is silicones, and foam inhibitors represented by silica-silicone mixtures. Silicones are generally represented by alkylated polysiloxane materials, while silica is usually used in finely divided form, represented by silica aerogels and xerogels and various hydrophobic silicas. These materials can be formulated as particles, with the suds suppressor being formulated such that it can be released into a water-soluble or water-dispersible, non-surface-active detergent substantially impermeable carrier. . Alternatively, the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on one or more of the other ingredients. Preferred silicone suds control agents are described in Bartollota et al. US Pat. No. 3,933,672. Other particularly useful suds suppressors are the self-emulsifying silicone suds suppressors described in German Patent Application No. DTOS 2646126, published April 28, 1977. An example of such a compound is DC-544, a siloxane-glycol copolymer commercially available from Dow Corning. A particularly preferred foam control agent is a foam control system comprising a mixture of silicone oil and 2-alkyl-alkanol. A suitable 2-alkyl-alkanol is 2-butyl-octanol, which is commercially available under the trade name Isofol 12 R.

[0171] Such foam control systems are described in pending European patent application N928870174.
． No. 7, specification, filed Nov. 10, 1992.

A particularly preferred silicone foam control agent is the European patent application N ° 9 under examination.
2201649.8. The composition may comprise a silicone / silica mixture in combination with a non-porous fume silica such as Aerosil®.

The foam inhibitors mentioned above are generally used in an amount of 0.001 to 2% by weight of the composition, preferably 0.1.
Used in an amount of 01 to 1% by weight.

Other Ingredients Other ingredients used in cleaning compositions such as soil dispersants, soil release agents, optical brighteners, abrasives, bactericides, antifog agents, colorants, and / or encapsulates. Or, perfume, which is not encapsulated, can be used.

A particularly suitable encapsulation material is a water-soluble capsule consisting of a matrix of polysaccharides and polyhydroxy compounds, as described in GB 1,464,616. Other suitable water-soluble encapsulating materials are disclosed in US Pat.
Dextrin derived from non-gelatinized starch acid-esters of substituted dicarboxylic acids, as described in 455,838. These acid-ester dextrins are preferably made from starches such as waxy corn, waxy sorghum, sago, tapioca and potato. Suitable examples of the encapsulating material include N-Lok from National Starch. N-Lo
The k capsule containing material consists of modified corn starch and glucose.
The starch has been modified by the addition of monofunctional substituents such as octenyl succinic anhydride.

Preferred optical brighteners are anionic systems, examples of which are 4,4′-bis (
2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2: 2 ′ disodium disulfonate, 4, -4′-bis (2-morpholino-4-anilino-s-triazine-6- Ilamino-Stilbene-2: 2 '
-Disodium disulfonate, 4,4'-bis (2,4-dianilino-s-triazin-6-ylamino) stilbene-2: 2'-disulfonic acid disodium,
4 ', 4 "-bis- (2,4-dianilino-s-triazin-6-ylamino)
Stilbene-2-sulfonic acid monosodium, 4,4'-bis- (2-anilino-
4- (N-methyl-N-2-hydroxyethylamino) -s-triazine-6-
Ilamino) stilbene-2,2'-disulfonic acid disodium, 4,4'-bis- (4-phenyl-2,1,3-triazol-2-yl) -stilbene-2
, 2'-Disulfonic acid disodium, 4,4'-bis- (2-anilino-4- (
1-Methyl-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene-2,2'-disulfonic acid disodium, 2 (stilbyl-4 "-
(Naphtho-1 ′, 2 ′: 4,5) -1,2,3-triazole-2 ″ -sodium sulfonate, and 4,4′-bis (2-sulfostyryl) biphenyl. Highly preferred bright The gnar is a special brightener from EP 753567.

Other useful polymeric materials are polyethylene glycols, especially those having a molecular weight of 1000.
~ 10,000, more preferably 2000-8000, most preferably about 4000
Of polyethylene glycol. These materials are used in an amount of 0.20-5% by weight, more preferably 0.25-2.5% by weight. These polymers and the previously described homopolymeric or copolymeric polycarboxylic acid salts are found to retain whiteness, fabric ash deposits, and clay, proteinaceous and oxidative soils in the presence of transition metal impurities. It is important to improve the cleaning performance.

Preferably, the detergent compositions of the present invention further comprise an anti-redeposition agent (also referred to as a soil dispersant) to improve thin soil detergency. Without wishing to be bound by theory, it is believed that such anti-redeposition agents capture the aged starch in the wash solution and prevent the aged starch from redepositing on the fabric surface. Therefore, by combining the anti-redeposition agent with the aged starch degrading enzyme of the present invention, synergistic thin soil cleaning properties are obtained.

Suitable anti-redeposition agents and soil dispersants here include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homopolymeric or copolymeric polycarboxylic acids or salts thereof. . Polymers of this type include the polyacrylates and maleic anhydride-acrylic acid copolymers previously described as builders, as well as maleic anhydride and ethylene, methyl vinyl ether or methacrylic acid at least 20 maleic anhydride copolymers. Copolymers that make up mol%. These materials are generally used in amounts of 0.5 to 10% by weight of the composition, more preferably 0.75 to 8% by weight and most preferably 1 to 6% by weight. The preferred anti-redeposition agent for the purposes of the present invention is carboxymethyl cellulose.

Soil release agents useful in the compositions of the present invention are typically copolymers or terpolymers of terephthalic acid and ethylene glycol and / or propylene glycol units in various configurations. Examples of such polymers are given in commonly assigned US Pat. No. 411.
6885 and 4711730 and published European patent application No. 0720233. European Patent No. EP-A-02
A particularly preferred polymer according to 72033 has the formula:

[0181]

[Chemical 14] Wherein, PEG is - _{(OC 2} H 4) a O-, PO is _{(OC 3 H} 6 O),
T is (pcOC ₆ H ₄ CO).

Of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propanediol, the terminal group consisting primarily of sulfobenzoate,
Secondly, modified polyesters such as random copolymers of monoesters of ethylene glycol and / or propanediol are also very useful. The goal is to obtain a polymer that is capped with sulfobenzoate groups on both ends, and in the present invention "first" most of the copolymer is endcapped with sulfobenzoate groups. However, some copolymers are not completely capped, so their end groups are "secondarily" ethylene glycol and / or propane 1
-2 May consist of monoester of diol.

The polyester selected here is about 46% by weight of dimethyl terephthalic acid, about 1%.
It contains 6% by weight propane-1.2 diol, about 10% by weight ethylene glycol, about 13% by weight dimethylsulfobenzoic acid, and about 15% by weight sulfoisophthalic acid and has a molecular weight of about 3,000. Polyesters and their methods of manufacture are described in detail in EPA311342.

It is well known in the art that free chlorine in tap water rapidly inactivates the enzymes contained in detergent compositions. Therefore, the use of chlorine scavengers, such as perborate, ammonium sulfate, sodium sulfite or polyethyleneimine, in the formulation in an amount of greater than about 0.1% by weight of the total composition allows the detergent enzyme to be washed during washing. Stability is improved. Compositions comprising chlorine scavengers are described in European Patent Application No. 928700188.6, filed January 31, 1992.

Alkoxylated polycarboxylates, such as materials made from polyacrylates, are useful here to add grease removal performance. Such materials are described in WO 91/08281 and PCT9, which are hereby incorporated by reference.
It is described on page 4 and subsequent pages of the specification of 0/01815. Chemically, these materials comprise polyacrylates with one ethoxy side chain for every 7-8 acrylate units. Side chain of the formula _{- (CH 2 CH 2 O)} m (CH 2) n C
Has a H _3, wherein, m is 2 to 3, n is 6-12. The side chains are ester linked to the polyacrylate "backbone" giving a "comb" polymer type structure. The molecular weight can vary, but is typically about 2000 to about 50,000. Such alkoxylated polycarboxylates can comprise from about 0.05 to about 10% by weight of the composition.

Dispersant The cleaning composition of the present invention can also include a dispersant. Suitable water-soluble organic salts are
The polycarboxylic acid is a homopolymeric or copolymeric acid or a salt thereof, which comprises at least two carboxyl groups separated from each other by not more than two carbon atoms. Polymers of this type are described in GB-A-1,596,756. Examples of such salts are polyacrylates of molecular weight 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of 1,000-100,000. In particular, a copolymer of acrylate and methacrylate, for example 480N with a molecular weight of 4000, is 0.5% of the composition.
It can be added to the cleaning compositions according to the invention in an amount of -20% by weight.

The composition of the present invention may comprise a lime soap peptizer compound having a lime soap dispersity (LSDP) as defined below of 8 or less, preferably 7 or less, most preferably 6 or less. The lime soap peptizer compound is preferably 0 to
It is present in an amount of 20% by weight.

The effect of lime soap peptizers was demonstrated by HC Borghetty and CA Bergman, J.
Am. Oil. Chem. Soc., Vol. 27, pp. 88-90, (1950), given numerically by the lime soap dispersancy (LSDP) measured by the lime soap dispersant test. The lime soap dispersion test method is widely used by experts in this field, for example, WN Linfield, Surfactant science Series, vol. 7, page 3, WN Linfield, Tenside surf. Det., Vol. 27, 159-163, (1
990), and MK Nagarajan, WF Masler, Cosmetics and Toiletries, 1
04, pp. 71-73, (1989). LSDP is 333 p
wt% ratio of dispersant to sodium oleate required to disperse a lime soap precipitate formed by 0.025 g of sodium oleate in 30 ml of water of pmCaCO ₃ (Ca: Mg = 3: 2) equivalent hardness. Is.

Surfactants that have good lime soap peptizer capacity include certain amine oxides, betaines, sulfobetaines, alkyl ethoxy sulphates and ethoxylated alcohols.

[0190]   Typical surfactants with an LSDP of 8 or less used according to the invention include C₁₆~
C₁₈Dimethylamine oxide, C having an average degree of ethoxylation of 1 to 5₁₂~ C ₁₈ Alkyl ethoxy sulphates, especially C having an ethoxylation degree of about 3.₁₂~
C₁₅Alkyl ethoxy sulphate (LSDP = 4), and average ethoxyl
C whose degree of conversion is 12 (LSDP = 6) or 30₁₄~ C₁₅Ethoxylated ar
Call (marketed as Lutensol A012 and Lutensol A030 from BASF GmbH respectively)
Sales).

Suitable polymeric lime soap peptizers for use herein are MK Nagaraj
Article by an and WF Masler, Cosmetics and Toiletries, 104, 71.
Pp. 73, (1989).

Hydrophobic bleaching agents, such as 4- [N-octanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-nonanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-decanoyl-6- Aminohexanoyl] benzenesulfonates and mixtures thereof, and nonanoyloxybenzenesulfonates can be used as lime soap peptizer compounds with hydrophilic / hydrophobic bleach formulations.

Dye Transfer Inhibition The cleaning compositions of the present invention also include compounds to prevent the transfer of dissolved and dispersed dye from one fabric to another during a fabric laundering operation involving colored fabrics. can do.

Polymeric Dye Transfer Inhibitor The cleaning composition of the present invention comprises 0.001 to 10% by weight, preferably 0.01 to 2% by weight, more preferably 0.05 to 1% by weight of a polymeric dye. It also comprises a dye transfer inhibitor. The polymeric dye transfer inhibitors are generally incorporated to prevent dye transfer from the dyed fabric to the fabric being laundered with the dyed fabric. These polymers have the ability to complex or adsorb the airborne dye washed out of the dyed fabric before it adheres to other laundry during laundering. Particularly suitable polymeric dye transfer inhibitors are polyamine N-oxide polymers,
It is a copolymer of N-vinylpyrrolidone and N-vinylimidazole, a polyvinylpyrrolidone polymer, polyvinyloxazolidone and polyvinylimidazole or a mixture thereof. The addition of such polymers also enhances the performance of the enzymes of the invention.

A) Polyamine N-Oxide Polymers Suitable polyamine N-oxide polymers for use herein include units having the structural formula:

[0196]

[Chemical 15] In the formula, P is a polymerizable unit to which an R—N—O group can be added, or an R—N—O group forms part of a polymerizable unit, or a combination of both. Is.

OO O ‖ ‖ ‖ A is NC, CO, C, —O—, —S—, —N—, x is 0 or 1, R is aliphatic, ethoxylated aliphatic, aromatic Group, heterocyclic or cycloaliphatic groups or combinations thereof, to which the nitrogen of the NO group can be added, or the nitrogen of the NO group is part of these groups.

[0198]   The N-O group is represented by the following general structure.

[0199]

[Chemical 16] Wherein R1, R2, and R3 are aliphatic, aromatic, heterocyclic or alicyclic groups or combinations thereof, and x and / or y and / or z is 0 or 1
And the nitrogen of the N—O group can be added, or the nitrogen of the N—O group forms part of these groups.

The N—O group can be part of the polymerisable unit (P) or can be added to the polymer backbone, or a combination of both. Suitable polyamine N-oxides in which the N—O group forms part of the polymerizable unit include polyamine N-oxides where R is selected from aliphatic, aromatic, cycloaliphatic or heterocyclic groups. Become. One section of the polyamine N-oxide comprises the polyamine N-oxide group in which the nitrogen of the N-O group forms part of the R group. Preferred polyamine N-oxides are those in which R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline,
The substances that are acridine and their derivatives. Another class of polyamine N-oxides comprises the group of polyamine N-oxides in which the nitrogen of the N-O group is attached to the R group.

Other suitable polyamine N-oxides are polyamine oxides in which N—O groups are attached to the polymerizable unit. A preferred class of these polyamine N-oxides has the general formula (I), in which R is an aromatic, heterocyclic or alicyclic group, N--O
The functional group nitrogen is a polyamine N-oxide that is part of the R group. Examples of these classes are polyamine oxides where R is a heterocyclic compound such as pyridine, pyrrole, imidazole and their derivatives.

Another preferred class of polyamine N-oxides has the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group and the nitrogen of the N—O functional group is the R group. Is a polyamine N-oxide added to the. Examples of these classes are polyamine oxides in which the R group can be aromatic, eg phenyl.

Any polymer skeleton can be used as long as the amine oxide polymer formed is water soluble and has dye transfer inhibiting properties. Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates and mixtures thereof.

The amine N-oxide polymers of the present invention typically have an amine to amine N-oxide ratio of 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 the appropriate degree of N-oxidation. Preferably, amine and amine N-
The oxide ratio is from 2: 3 to 1: 1,000,000. More preferably 1: 4-1
: 1,000,000, most preferably 1: 7 to 1: 1,000,000. The polymers of the present invention actually include random or block copolymers in which one of the monomers is an amine N-oxide and the other monomer type is an amine N-oxide, or not. The amine oxide unit of polyamine N-oxide has a pK
a <10, preferably pKa <7, more preferably pKa <6.

Polyamine oxides can be obtained with almost any degree of polymerization. The degree of polymerization is not critical provided that the material has the desired water solubility and dye dispersancy. Typically, the average molecular weight is 500 to 1,000,000, preferably 1,000 to 50.
1,000, more preferably 2,000 to 30,000, most preferably 3,000.
It is 0 to 20,000.

B) Copolymer of N-vinylpyrrolidone and N-vinylimidazole The N-vinylimidazole N-vinylpyrrolidone polymer used in the present invention has an average molecular weight of 5,000 to 1,000,000, preferably 5,000-200,
It is 000. Highly preferred polymers for use in the detergent compositions of the present invention have an average molecular weight of 5,000 to 50,000, more preferably 8,000 to 30,000,
Most preferably 10,000-20,000 N-vinyl imidazole N-
It comprises a polymer selected from vinylpyrrolidone copolymers. The average molecular weight range is Barth HG and Mays JW Chemical Analysis, Vol 113, `` Modern Method
s of Polymer Characterization ”.

Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an average molecular weight of 5,000 to 50,000, more preferably 8,000 to 30,000.
, And most preferably 10,000 to 20,000.

The N-vinylimidazole N-vinylpyrrolidone copolymer, which is characterized by having the average molecular weight range, exhibits excellent dye transfer-preventing properties and the cleaning performance of a detergent composition formulated with the copolymer. There is no adverse effect on. The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention comprises N-vinylimidazole and N-vinylimidazole.
The molar ratio of vinylpyrrolidone is 1 to 0.2, more preferably 0.8 to 0.3, and most preferably 0.6 to 0.4.

C) Polyvinylpyrrolidone The detergent composition of the present invention has an average molecular weight of about 2,500 to about 400,000, preferably about 5,000 to about 200,000, more preferably about 5,000 to about 50.
It is also possible to use polyvinylpyrrolidone (“PVP”), which is 5,000, most preferably from about 5,000 to about 15,000. A suitable polyvinylpyrrolidone is the product name PVP K-15 from ISP Corporation, New York, NY and Montreal, Canada.
(Viscosity molecular weight 10,000), PVP K-30 (average molecular weight 40,000), PVP K-60
(Average molecular weight 160,000), and PVP K-90 (Average molecular weight 360,000)
It is commercially available at. Other suitable polyvinylpyrrolidones commercially available from BASF Cooperation are Sokalan HP 165 and Sokalan HP 12, polyvinylpyrrolidone known to those skilled in the detergent art (for example EP-A-262,897 and EP-A). A-256,696).

D) Polyvinyl oxazolidone In the detergent composition of the present invention, polyvinyl oxazolidone can be used as a polymeric dye transfer inhibitor. The polyvinyl oxazolidone has an average molecular weight of about 2
, 500 to about 400,000, preferably about 5,000 to about 200,000, more preferably about 5,000 to about 50,000, and most preferably about 5,000 to about 15,000.

E) Polyvinylimidazole In the detergent composition of the present invention, polyvinylimidazole can also be used as a polymeric dye transfer inhibitor. The polyvinyl imidazole has an average of about 2,500 to about 400,000, preferably about 5,000 to about 200,000, more preferably about 5,000 to about 50,000, most preferably about 5,000 to about 15. 1,000
Have.

F) Crosslinked Polymer A crosslinked polymer is a polymer in which the skeletons are interconnected to some extent, and these bonds may be chemical or physical, and if desired, active groups are on the skeleton or on a branched chain. Crosslinked polymers are described in Journal of Polymer Science, volume 22, pages 1035-1039. In one embodiment, the crosslinked polymer is constructed to form a three-dimensional rigid structure, which allows the dye to be trapped within the pores formed by the three-dimensional structure. In another embodiment, the crosslinked polymer entraps the dye by swelling. Such crosslinked polymers are described in pending patent application No. 94870213.9.

Laundry Method The compositions of the present invention are suitable for use in substantially all laundering or cleaning methods, including dipping methods, pretreatment methods, and methods involving a rinsing step to which another rinsing composition can be added. Can be used.

The methods described herein comprise contacting a fabric, tableware or other hard surface with a cleaning solution in a conventional, exemplified manner. A typical laundry method comprises treating the soiled fabric with an effective amount of an aqueous liquid in which the laundry detergent and / or fabric protection composition is dissolved or dispersed. A preferred method of mechanical dishwashing comprises treating soiled dishes with an aqueous liquid in which an effective amount of a mechanical dishwashing or rinsing composition is dissolved or dispersed. A typical effective amount of a machine dishwashing composition means 8 to 60 g of product dissolved or dispersed in a wash volume of 3 to 10 liters. In the manual dishwashing method, soiled dishes are contacted with an effective amount of a dishwashing composition, typically 0.5-20 g (per 25 dishwashes to be treated). In a preferred manual dishwashing method, the concentrated solution is applied to the dish or immersed in a large volume of dilute solution of the detergent composition. The usual hard surface method is to use a sponge, brush, cloth, etc. to clean a dirty hard object with an aqueous liquid in which an effective amount of a hard surface cleaner is dissolved or dispersed, and / or diluted such. Comprising treating with no composition. Also included is synthesizing the concentrated or bulk dilute solution of the detergent composition. The method of the present invention is conveniently carried out during the washing process. This washing method is preferably carried out at 5 ° C to 95 ° C, particularly 10 ° C to 60 ° C. The pH of the treatment solution is preferably 7-12.

The following examples illustrate the compositions of the present invention, but do not limit or define the scope of the invention.

In the cleaning composition, the amount of enzyme is expressed as wt% of pure enzyme relative to the total composition, and unless otherwise indicated, the detergent components are expressed as wt% of the total composition. In the detergent composition, the abbreviated components have the following meanings.

LAS: sodium linear C _11-13 alkylbenzene sulfonate TAS: sodium tallow alkyl sulfate CxyAS: sodium C _1x -C _1y alkyl sulfate CxySAS: sodium C _1x -C _1y secondary (2,3) alkyl sulfate CxyEz : C _{1x to} C _1y mainly linear primary alcohol CxyEzS condensed with an average z mole of ethylene oxide: C _{1x to} C _1y sodium alkylsulfate condensed with an average Z mole of ethylene oxide CxEOy: Cy of an average ethoxylated y Alcohol nonionics: mixed ethoxylated / propoxylated fatty alcohols, such as alcohols having an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5.
Plurafac LF404 QAS: R ₂ . _{N + (CH 3) 2 (} C 2 H 4 OH), wherein _R 2 _{= C} 12 _{~C 1
4} QAS1: R ₂ . _{N + (CH 3) 2 (} C 2 H 4 OH), wherein _R 2 _{= C} 8 ~
C ₁₁ SADS: Formula 2- (R). C4H7-1,4 (SO4−) 2 sodium C14-22 alkyl disulfate, R = C10-18 MBAS: C12-18 medium chain branched alkyl sulphate surfactant, average branching 1.5
Methyl or ethyl branching group MES: x-Sulfomethyl ester of C18 fatty acid APA: _C8-10 amidopropyldimethylamine soap: sodium linear alkylcarboxylate STS derived from an 80/20 mixture of tallow and coconut fatty acids STS: sodium toluene Sulfonate TFAA: C _{16 to} C ₁₈ alkyl N-methylglucamide TPKFA: C _{12 to} C ₁₄ topped whole cut fatty acid DEQA: di- (tallow-oxy-ethyl) dimethylammonium chloride DEQA (2): di- (soft- Tallowyloxyethyl) hydroxyethylmethylammonium methylsulfate SDASA: 1: 2 ratio of stearyl dimethylamine: triple press stearic acid DTMAMS: ditallow dimethylammonium methylsulfate silicate Sodium amorphous silicate _{(SiO 2:} Na 2 O ratio = 1.6 to 3.
2: 1) Metasilicate: sodium metasilicate (SiO ₂ : Na ₂ O ratio = 1.0) Zeolite A: Formula Na ₁₂ (AlO ₂ SiO ₂ ) ₁₂ 27H ₂ O hydrated sodium aluminosilicate, primary particle size 0.1-10 micrometers (weight is expressed in anhydrous state) SKS-6: crystalline layered silicate of formula δ-Na ₂ Si ₂ O ₅ citrate: trisodium citrate dihydrate citric acid: Anhydrous citric acid carbonate: Anhydrous sodium bicarbonate Bicarbonate: Sodium hydrogen carbonate Sulfate: Anhydrous sodium sulfate Mg Sulfate: Anhydrous magnesium sulfate STPP: Sodium tripolyphosphate TSPP: Tetrasodium pyrophosphate MA / AA: Acrylate / Maleate 4: 1 Random copolymer, average molecular weight about 70,000 to 80,000 MA / AA1: acrylate / male G. 6: 4 random copolymer, average molecular weight about 10,000 AA: sodium polyacrylate polymer, average molecular weight 4,500 polycarboxylate: containing a mixture of carboxylated monomers such as acrylates, maleates and methyl acrylates. Copolymer, molecular weight 2,0
0-80,000, for example acrylic acid copolymer Sokolan, commercially available from BASF,
MW4,500 Clay: bentonite or smectite clay PB1: anhydrous sodium perborate monohydrate PB4: formula NaBO ₃ . 4H ₂ O of sodium perborate tetrahydrate Percarbonate salts: Anhydrous sodium percarbonate bleach, nominal formula _Na 2 _CO 3. 3H ₂ O ₂ NaDCC: sodium dichloroisocyanurate TAED: tetraacetylethylenediamine NOBS: nonanoyloxybenzenesulfonate in the form of sodium salt NACA-OBS: (6-nonamidocaproyl) oxybenzenesulfonate LOBS: in the form of sodium salt Dodecanoyloxybenzenesulfonate DOBA: Dodecanoylbenzoic acid DTPA: Diethylenetriaminepentaacetic acid HEDP: 1,1-Hydroxyethanediphosphonic acid DETPMP: Diethylenetriaminepenta (methylene) phosphonate, Monsan
sold by to under the trade name Dequest 2060 EDDS: ethylenediamine-N, N-disuccinic acid, (S, S) isomer, its sodium salt form MnTACN: manganese 1,4,7-trimethyl-1,4,7-triaza Cyclononane photo-activated bleach: sulfonated zinc or aluminophthalocyanine PAAC: pentaamine acetate cobalt (III) salt paraffin: paraffin oil, sold under the trade name Winog 70 by Wintershall NaBz: encapsulated in dextrin soluble polymer NaBz: Sodium Benzoate Protease: Proteolytic enzyme, Savinase, Alcala by Novo Nordisk A / S
marketed under the trade name se, the "Protease D" variant with the substitution set N76D / S103A / V104I, and PCT patent application No. PCT / US98 / 22588.
No., PCT / US98 / 22482 and PCT / US98 / 22486
Amino acid substitution set 101G / 103A / 10 described in each specification of No.
Protease with 4I / 159D / 232V / 236H / 245R / 248D / 252K Amylase: Starch-degrading enzyme, Termamyl and Duramy by Novo Nordisk A / S
commercially available under the trade name of l, and described in International Patent No. WO 95/35382,
Mutant enzyme lipase with improved thermostability containing amino acid deletion R181 ^* + G182 ^* or T183 ^* + G184 ^* : lipolytic enzyme, Lipolase, Lipolase Ultra by Novo Nordisk A / S,
And Reist-AMG under the trade name of Lipomax by Gist Brocades: amyloglucosidase, marketed under the trade name of AMG by Novo Nordisk A / S pullulanase type II: α-amylase activity as described in EP 418835. Alkaline pullulanase Y cellulase with: Cellulolytic enzyme, Novo Nordisk A / S by Carezyme, Celluzym
Commercially available under the trade name of e and / or Endolase CMC: Sodium carboxymethyl cellulose PVP: Polyvinyl polymer, average molecular weight 60,000 PVNO: Polyvinyl pyridine-N-oxide, average molecular weight 50,000 PVPVI: Copolymer weight of vinylimidazole and vinylpyrrolidone Coalescence, average molecular weight 2
50,000 brightener 1: disodium 4,4'-bis (2-sulfostyryl) biphenyl brightener 2: disodium 4,4'-bis (4-anilino-6-morpholino-1,3,5-triazine -2-yl) stilbene-2: 2'-disulfonate brightener 3: disodium 4,4'-bis (4,6-dianilino-1,3,3
5-triazin-2-yl) aminostilbene-2-2'-disulfonate silicone antifoaming agent: polydimethylsiloxane cell regulator containing siloxane-oxyalkylene copolymer as dispersant, said cell regulator and said dispersant Ratio of 10: 1
100: 1 Foam Inhibitor: 12% Silicone / Silica, 18% Stearyl Alcohol, 70%
Starch, granular form thickeners: high molecular weight crosslinked polyacrylates, eg BF Goodrich Chemical Compa
Carbopol and Polygel SRP 1: Nylon end-capped polyester SRP 2: 1) available from NY, US Pat. No. 5,415,807, Gosselink, Pan, Kell.
Stain free polymers selected from et and Hall, published May 16, 1995, and / or 2) non-stain free polymers according to US patent application 60/051517. QEA: Bis ((C ₂ H ₅ O) (C ₂ H ₄ O) _n ) (CH ₃ ) -N ⁺ -C ₆ H ₁₂ -N ⁺ -(
CH ₃ ) bis ((C ₂ H ₅ O)-(C ₂ H ₄ O)) _n , n = 20 to 30 PEI: polyethyleneimine, average molecular weight 600 to 1800, average ethoxylation degree 7 to 20 per nitrogen Ethyleneoxy residue SCS: sodium cumene sulfonate HMWPEO: high molecular weight polyethylene oxide PEGX: polyethylene glycol, molecular weight X PEO: polyethylene oxide, average molecular weight 5,000 TEPAE: tetraethylene pentaamine ethoxylate BTA: benzotriazole pH: 1% distillation Measured at 20 ℃ in aqueous solution

Example 1 The following granular laundry detergent composition was prepared according to the present invention. I II III IV V Spray-dried granules LAS 10.0 10.0 15.0 5.0 5.0 TAS-1.0---MBAS---5.0 5.0 C ₄₅ AS--1.0-2.0 C ₄₅ AE ₃ S---1.0-QAS--1.0 1.0-DTPA, HEDP and / or EDDS 0.3 0.3 0.5 0.3-Mg Sulfate 0.5 0.5 0.1--Citrate---3.0 5.0 Carbonate 10.0 7.0 15.0--Sulfate 5.0 5.0--5.0 Silicate--- -2.0 Zeolite A 16.0 18.0 20.0 20.0-SKS-6---3.0 5.0 MA / AA or AA 1.0 2.0 11.0--PEG4000-2.0-1.0-QEA 1.0---1.0 Brightener 1 or 2 or 3 0.05 0.05 0.05- 0.0 Silicone oil 0.01 0.01 0.01-- Agglomerate Carbonate----4.0 SKS-6 6.0---6.0 LAS 4.0 5.0--5.0 Dry addition particulate component Maleic acid / carbonate / bicarbonate 8.0 10.0 10.0 4.0- (40:20:40) QEA---0.2 0.5 NACA-OBS 3.0--4.5-NOBS 1.0 3.0 3.0--TA D 2.5 - - 1.5 2.5 MBAS - - - 8.0 - LAS ( flake) 10.0 10.0 - - - Spray Brightener 1 or 2 or 3 0.2 0.2 0.3 0.1 0.2 Perfume 1.0 0.5 1.1 0.8 0.3 Dry additives Citrate - - 20.0 4.0 - Percarbonate 15.0 3.0 6.0 10.0-Perborate----6.0 Photoactive bleach 0.02 0.02 0.02 0.1 0.05 Enzyme (cellulase, amylase, 0.04 0.01 0.02 0.02 0.05 Protease and / or lipase) ReSIAMG 1.0 0.05 0.002 0.001 0.05 Carbonate Salt 0.0 10.0---Fragrance (encapsulated)-0.5 0.5-0.3 Foam inhibitor 1.0 0.6 0.3-0.10 Soap 0.5 0.2 0.3 3.0 0.5 Citric acid---6.0 6.0 SKS-6---4.0-Up to 100% filler

Example 2 The following granular laundry detergent composition was prepared according to the present invention. I II III IV Brow powder MES 2.0 0.5 1.0-SADS---2.0 LAS 6.0 5.0 11.0 6.0 TAS 2.0--2.0 Zeolite A 24.0--20.0 STPP-27.0 24.0-Sulfate 4.0 6.0 13.0-MA / AA 1.0 4.0 6.0 2.0 Silicate 1.0 7.0 3.0 3.0 CMC 1.0 1.0 0.5 0.6 Brightener 1 0.2 0.2 0.2 0.2 Silicone antifoam 1.0 1.0 1.0 0.3 DTPMP 0.4 0.4 0.2 0.4 Spray brightener 1 or 2 or 3 0.02--0.02 C45E7---5.0 C45E2 2.5 2.5 2.0-C45E3 2.6 2.5 2.0-Fragrance 0.5 0.3 0.5 0.2 Silicone defoamer 0.3 0.3 0.3 -Drying additive QEA---1.0 EDDS 0.3---Sulfate 2.0 3.0 5.0 10.0 Carbonate 6.0 13.0 15.0 14.0 Citric acid 2.5 --2.0 QAS 0.5--0.5 SKS-6 10.0---Percarbonate 4.0 3.0-1.9 PB4---NOBS 0.5--0.3 TAED 0.75 4.5-0.5 Clay--10.0-Protease 0.03 0.03 0.03 0.03 Lipase 0.008 0. 008 0.008 0.004 ReSI-AMG 0.001 0.01 0.01 0.004 Pullulanase type II--0.01-Amylase 0.003-0.003 0.006 Brightener 1 0.05--0.05 Other / small amount components and speckles up to 100%

Example 3 The following granular laundry detergent composition was prepared according to the present invention. I II III IV V VI BROWN POWDER LAS 23.0 8.0 7.0 9.0 7.0 7.0 QAS----1.0-C45AS 6.0 6.0 5.0 8.0--C45AE11S-1.0 1.0 1.0--MES 2.0---2.0 4.0 Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0 MA / AA-0.5---2.0 MA / AA1 7.0-----AA-3.0 3.0 2.0 3.0 3.0 Sulfate 5.0 6.3 11.0 11.0 11.0 18.1 Silicate 10.0 1.0 1.0 1.0 1.0 1.0 Carbonate 15.0 20.0 10.0 20.7 8.0 6.0 PEG4000 0.4 1.5 1.5 1.0 1.0 1.0 DTPA-0.9 0.5--0.5 Brightener 2 0.3 0.2 0.3-0.1 0.3 Spray C45E7-2.0--2.0 2.0 C25E9 3.0-----C23E9--1.5 2.0-2.0 Fragrance 0.3 0.3 0.3 2.0 0.3 0.3 Aggregate C45AS-5.0 5.0 2.0-5.0 LAS-2.0 2.0--2.0 Zeolite A-7.5 7.5 8.0-7.5 Carbonate-4.0 4.0 5.0-4.0 PEG4000-0.5 0.5--0.5 Others (water, etc.)-2.0 2.0 2.0-2.0 Dry additive QASI----1.0- Acid----2.0-PB4----5-PB1--4 1.0--Percarbonate 2.0--1.0-2.0 Carbonate-5.3 1.8-4.0 4.0 NOBS 0.5-0.4 0.3--Clay--- --10.0 TAED 0.6 0.4 0.6 0.3 0.9-Methylcellulose 0.2----0.5 DTPA 0.7 0.5 1.0 0.5 0.5 1.2 Speckle---0.2 0.5-SKS-6 8.0-----STS--2.0-1.0-Cumene sulfone Acid-1.0---2.0 Lipase 0.004-0.004-0.004 0.008 Cellulase 0.0005 0.0005 0.0005 0.0007 0.0005 0.0005 Amylase 0.003-0.001-0.003-Pullulanase II-0.01--0.001-ReSI-AMG 0.01 5.0 0.05 0.002 0.001 0.05 Protease 0.01 0.015 0.015 0.009 0.01 0.01 PVPVI----0.5 0.1 PVP----0.5-PVNO--0.5 0.3--QEA----1.0-SRP1 0.2 0.5 0.3-0.2-Silicone defoamer 0.2 0.4 0.2 0.4 0.1-Mg sulfate --0.2-0.2-Other / Minor components 100% in total

Example 4 The following granular laundry detergent composition was prepared according to the present invention. I II III IV Base granule STPP -22.0 -15.0 Zeolite A 30.0 -24.0 5.0 Sulfate 5.5 5.0 7.0 7.0 MA / AA 3.0---AA-1.6 2.0 -MA / AA1 -12.0 -6.0 LAS 14.0 10.0 9.0 20.0 C45AS 8.0 7.0 9.0 7.0 C45AE11S-1.0-1.0 MES 0.5 4.0 6.0-SADS 2.5--1.0 Silicate-1.0 0.5 10.0 Soap-2.0--Brightener 1 0.2 0.2 0.2 0.2 Carbonate 6.0 9.0 8.0 10.0 PEG4000-1.0 1.5-DTPA-0.4 - - spray C25E9 - - - 5.0 C45E7 1.0 1.0 - - C23E9 - 1.0 2.5 - perfume 0.2 0.3 0.3 - dry additives carbonate 5.0 10.0 13.0 8.0 PVPVI / PVNO 0.5 - 0.3 - protease 0.03 0.03 0.03 0.015 lipase 0.008 - - 0.008 Resi -AMG 0.01 3.0 0.05 0.005 Pullulanase type II--0.02 0.001 Amylase 0.002--0.002 Cellulase 0.0002 0.0005 0.0005 0.0003 DTPA 0.5 0.3 0.5 1.0 LOBS-0.8-0. 3 PB1 5 3.0 10 4.0 DOBA 1.0-0.4-TAED 0.5 0.3 0.5 0.6 Sulfate 4.0 5.0-5.0 SRP1-0.4--Foam suppressor-0.5--Speckle 0.9-2.7 1.2 Other / minor components 100% in total

Example 5 The following granular laundry detergent composition was prepared according to the present invention.

[Table 1]

Example 6 The following granular laundry detergent composition was prepared according to the present invention. I II III IV C ₁₃ LAS 13.3 13.7 10.4 8.0 C ₄₅ AS 3.9 4.0 4.5-C ₄₅ AE (0.5) S 2.0 2.0--C ₄₅ AE (6.5) 0.5 0.5 0.5 5.0 C _{9 to} C ₁₄ alkyl 1.0 --0.5 Dimethyl hydroxyethyl quaternary ammonium salt Tallow fatty acid 0.5---Tallow alcohol--1.0 0.3 Ethoxylate (50) STPP-41.0-20.0 Zeolite A 26.3-21.3 1.0 Carbonate 23.9 12.4 25.2 17.0 AA 3.4 0.0 2.7- MA / AA--1.0 1.5 Silicate 2.4 6.4 2.1 6.0 Sulfate 10.5 10.9 8.2 15.0 Sodium perborate 1.0 1.0 1.0 2.0 PEG4000 1.7 0.4 1.0-CMC 1.0--0.3 Citric acid--3.0-NOBS / DOBS 0.2 0.5 0.5 0.1 TAED 0.6 0.5 0.4 0.3 SRP2 1.5 1.5 1.0 1.0 Moisture 7.5 3.1 6.1 7.3 Mg sulphate---1.0 DTPA, HEDP---0.5 and / or EDDS enzymes (amylase, cellulase,-0.025-0. 04 Protease and / or lipase ReSI-AMG 0.02 0.05 0.005 0.008 Other / minor components, perfume, brightener up to 100%, including photobleach

Example 7 A laundry detergent composition in the form of the following tablets or granular formulations was prepared according to the present invention. I II III IV V VI C ₁₃ LAS 20.0 16.0 8.5 5 20.0 6.0 C ₄₅ AS-4.0---C ₄₅ AE (3) S 1.0 1.0----C ₄₅ AE-5.0 5.5 4.0-C _{9 to} C ₁₄ alkyl 0.5 2.0----Dimethylhydroxyethyl quaternary ammonium salt Tallow fatty acid-1.0----STPP / zeolite 10.0 20.0 30.0 20.0 25.0 25.0 Carbonate 41.0 30.0 30.0 25.0 45.0 24.0 AA------MA / AA 2.0 0.5 0.5 1.0--Silicate 6.0 8.0 5.0 6.0 8.0 5.0 Sulfate 2.0 3.0---8.0 Perborate / Percarbonate 1.0-20.0 14.0--Sodium PEG4000-0.5---0.5 CMC 0.5 0.5 0.5 0.5-0.5 Quen Acid------NOBS / DOBS 0.7-----TAED / Preformed 0.7-4.5 5.0--Peracid DTPA, HEDP--0.5 0.5-and / or EDDS SRP 1.0-1.0 1.0--Clay 4.0 3.0 7.0 10.0 6.0 8.0 PEO 1.0 0.5 2.0 0.5 1.0 0.5 Wetting agent 0.5--0.5 --Wax 0.5--0.5--Cellulose 2.0--1.5-1.0 Sodium acetate--1.0 0.5 4.0 1.0 Moisture 3.0 5.0 5.0 5.0 8.0 10.0 Mg sulfate 0.5 1.5----Soap / foam suppressor 0.6 1.0 1.0 0.8 0.5 -Enzymes (amylase, 0.04 0.04 0.01 0.02 0.02 0.03 cellulase, protease and / or lipase ReSI-AMG 0.03 0.01 0.05 .003 0.1 .005 pullulanase type II--0.02--.002 minor components such as perfumes, up to 100% PVP, PVPVI / PVNO, brightener, photobleach, speckle, etc.

Example 8 The following laundry detergent composition was prepared according to the present invention. _{I II III IV V C 13 LAS} 12.0 16.0 23.0 19.0 18.0 C 45 AS - 4.5 - - - C 45 AE (3) S - - 2.0 - 1.0 C 45 AE 2.0 2.0 - 1.3 - C 9 ~C 14 alkyl - - - -1.0 Dimethyl hydroxyethyl quaternary ammonium salt STPP / zeolite 23.0 25.0 14.0 22.0 20.0 Carbonate 25.0 22.0 35.0 20.0 28.0 AA 0.5 0.5 0.5 0.5-MA / AA--1.0 1.0 1.0 Silicate 3.0 6.0 9.0 8.0 9.0 Na perfluoro Acid salt / percarbonate 5.0 5.0 10.0-3.0 PEG 4000 1.5 1.5 1.0 1.0-CMC 1.0 1.0 1.0-0.5 NOBS / DOBS-1.0--1.0 TAED / preformed 1.5 1.0 2.5-3.0 Peracid DTPA, HEDP 0.5 0.5 0.5 -1.0 and / or EDDS SRP 1.5 1.5 1.0 1.0-Clay 5.0 6.0 12.0 7.0 10.0 Flocculant PEO 0.2 0.2 3.0 2.0 0.1 Wetting agent----0.5 Wax 0.5----Cellulose 0.5 2.0--3.0 Sodium acetate 2.0 1.0 3.0 --Moisture 7.5 7 .5 6.0 7.0 5.0 Soap / foam inhibitor--0.5 0.5 0.8 ReSI-AMG 0.02 0.02 .005 .005 0.01 Enzymes (amylase,----0.045 Cellulase, protease and / or lipase Other / minor components such as perfume, 100 Up to% PVP, PVPVI / PVNO, speckle, brightener, photobleach, etc.

Example 9 The following liquid laundry detergent composition was prepared according to the present invention. I II III IV V VI LAS---1.0 2.0-C25AS 16.0 13.0 14.0 5.0-6.5 C25AE3S 5.0 1.0-10.0 19.0 3.0 C25E7 2.0 3.5-2.5 2.0 5.0 TFAA 5.0 4.5 4.5 6.5 4.0-APA 2.0 1.0-3.0-0.5 QAS- -2.0-1.5-TPKFA 4.5 8.0 15.0-5.0 5.0 Citric acid 2.2 3.0-0.5 1.0 2.0 Rapeseed fatty acid 2.0--3.0 6.0 1.5 Ethanol 3.2 2.0 2.5 2.2-0.5 1,2 Propanediol 5.7 8.5 6.5 7.0 7.0 5.5 Monoethanolamine 5.0 7.5-5.0 1.0 2.0 TEPAE-1.2-0.5 0.5-PE12-1.5-1.0 0.8-DTPMP 1.3 0.5 0.8 0.5-0.2 HEDP-0.5 0.2 1.0--Protease 0.02 0.03 0.02 0.02 0.02 0.01 ReSI-AMG 0.01 0.02 0.005 0.01 0.005 0.002 Pulllanase Type II--0.2 0.05--Lipase 0.002 0.001 0.001-0.001-Amylase .0008 .0006 .0006 0.002 0.001 0.001 Cellulase 0.002 0.002-0.002 0.001-SRP1 0.20 0.15 0.10-0.17 0.04 PVNO ---0.05 0.10-Brightener 3 0.20 0.15 0.10 0.05-0.05 Foam Inhibitor 0.25 0.20 0.15 0.15 0.30 0.10 Calcium Chloride 0.02 0.02-0.01 0.01-Boric Acid 2.5 2.0 1.5 2.2 1.5 1.2 Bentonite Clay--5.5---With NaOH Adjust pH 8.0 7.5 7.7 8.0 7.0 7.5 Water / Small components 100% in total

Example 10 The following non-aqueous liquid detergent composition was prepared according to the present invention. I II III LAS 16.0 16.0 16.0 C23E05S 21.5 21.5 19.0 Butoxypropoxypropanol 18.5-16.0 Hexylene glycol-18.5 5.0 Sodium citrate dihydrate 6.8 6.8 3.8 [NACA-OBS] Na salt 6.0 6.0 6.0 Methyl quaternary polyethoxylated 1.3 1.3 1.3 Methylsulfate salt of hexamethylenediamine EDDS 1.2 1.2 1.2 MA / AA--3.0 Sodium carbonate 10.0 10.0 10.0 Protease 0.05 0.02 0.02 Pullulanase type II--0.05 ReSI-AMG 1.0 0.01 0.02 Amylase 0.01 0.01 0.01 Cellulase 0.0001 0.0001 0.0001 PB1 12.0 12.0 12.0 Silicone antifoam 0.75 0.75 1.1 Perfume 1.7 1.7 1.7 Titanium dioxide 0.5 0.5 0.5 Dichloro-5,12-dimethyl--0.03 0.03 1,5,8,12-Tetraazabicyclo [6.6.2] hexadecane manganese (II) Brightener 2 0.2 0.2 0.2 Sodium hydrogenated C16-18 Fat 1 1 0.5 Soap coloring Speckle 0.4 0.4 0.4 Other 100% in total

Example 11 A laundry detergent composition having the following tablet form was produced according to the present invention. i) The detergent base powder of composition I was prepared as follows. All particulate materials of Base Composition I were mixed in a mixing drum to form a homogeneous particle mixture. Spraying was performed during this mixing.

Ii) Then, tablets were produced as follows. 50 g matrix with 5.5 diameter
Placed in a circular cm-shaped mold, the tablet has a tensile strength (or diametral breaking stress) of 1
It was compressed to 0 kPa.

Iii) The tablets are then tableted with 90 parts sebacic acid and Nymcel-ZSB16 (Metsa Serla).
It was immersed at 140 ° C. in a bath containing 10 parts by weight (trade name). The time of dipping the tablets in the heated bath was adjusted so that 4 g of the bath mixture was applied. Then, the tablets were left to cool at room temperature of 25 ° C. for 24 hours. Tensile strength of coated tablets is 30kP
increased to a.

[0231]                                                               I Anionic aggregate 1 (anionic substance 40%, 21.5 Zeolite 27% and carbonate 33%) Anionic aggregate 2 (anionic substance 40%, 13.0 28% zeolite and 32% carbonate) Cation-based aggregate (Cation-based substance 20%, 5.5 56% zeolite and 24% sulfate) Layered silicate (95% SKS6 and 5% silicate) 10.8 Sodium percarbonate 14.2 Bleach activator aggregates (TAED 81%, acrylic acid / 5.5 Maleic acid copolymer (acid form) 17% and water 2%) Carbonate 10.98 EDDS / sulfate particles (EDDS 58%, 0.5 Sulfate 23% and water 19%) HEDP 0.8 SRP 0.3 Fluorescent substance 0.2 Photoactive bleach (zinc phthalocyanine sulfonate 10% active) 0.02 Soap powder 1.4 Foam suppressor (silicone oil 11.5%, 1.9 Zeolite 59% and water 29.5%) Citric acid 7.1 ReSI-AMG 0.05 Protease 0.03 Lipase 0.006 Cellulase 0.0005 Amylase 0.02 Binder spray system (Lutensit K-HD 96 25%, 4.0 PEG 75% by weight)

Example 12 A laundry detergent composition having the following tablet form was prepared according to the present invention. I II III IV V VI Phase I percarbonate 45.0 45.0 45.0 45.0 45.0 45.0 TAED 9.7 9.7 9.7 9.7 9.7 9.7 9.7 Citric acid 10.0 15.0 20.0 15.0 15.0 15.0 STPP-----6.0 MA / AA 6.0 6.0 1.0 5.0--Kay Acid salt----6.0-Bicarbonate 15.0 15.0 10.0 15.0 15.0 15.0 Carbonate 5.0-----Brightener 1 or 2 0.1 0.1 0.1 0.1 0.1 0.1 0.1 Fragrance 0.2 0.2 0.2 0.2 0.2 0.2 C12-16 fatty acid--- 1.0--Protease 0.03 0.03 0.03 0.03 0.03 0.03 Amylase 0.02 0.02-0.02-- Phase 2 AMG 0.01 0.02 0.04 0.01 0.1 0.5 Protease 0.04 0.04 0.04 0.04 0.04 0.04 Amylase 0.02 0.02----Speckle 0.09 0.09 0.09 0.09 0.09 0.09 PEG4000 0.33 0.33 0.33 0.33 0.33 0.33 Citric acid 1.06 1.06 1.06 1.06 1.06 1.06 Bicarbonate 2.87 2.87 2.87 2.87 2.87 2.87

Example 13 The following laundry bar detergent composition was prepared according to the present invention (amounts are expressed in parts by weight,
Enzymes are expressed as pure enzymes).

[Table 2]

Example 14 In accordance with the present invention, a granular fabric detergent composition capable of "making laundry softer" was prepared. I II C45AS-10.0 LAS 7.6-C68AS 1.3-C45E7 4.0-C25E3-5.0 Coco-alkyl-dimethylhydroxy 1.4 1.0 ethylammonium chloride 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 Protease 0.02 0.01 Lipase 0.02 0.01 ReSI-AMG 0.05 0.02 Amylase 0.03 0.005 Cellulase 0.001 -Silicate 3.0 5.0 Carbonate 10.0 10.0 Foaming inhibitor 1.0 4.0 CMC 0.2 0.1 Other and minor components 100% in total

Example 15 In accordance with the present invention, a fabric softener composition for the following rinse was prepared. DEQA (2) 20.0 Cellulase 0.001 ReSI-AMG 0.005 HCL 0.03 Antifoaming agent 0.01 Blue dye 25 ppm CaCl ₂ 0.20 Fragrance 0.90 Other components and water 100% in total

Example 16 In accordance with the present invention, the following fabric softening agent and dryer-added fabric conditioning composition was prepared. I II III IV V DEQA 2.6 19.0---DEQA (2)----52.0 DTMAMS---26.0-SDASA--70.0 42.0 40.2 Stearic acid, IV = 0 0.3----C45EO1-3--13.0- -HCL 0.02 0.02---Ethanol--1.0--Perfume 0.3 1.0 0.75 1.0 1.5 Glycoperse S-20----15.4 Glycerol monostearate---26.0-Digeranyl succinate--0.38--Silicone antifoam Agent 0.01 0.01---Electrolyte-0.1---Amylase-0.2-0.2 0.2 ReSI-AMG 1.0 0.2 0.1 0.01 0.01 Clay---3.0-Dye 10ppm 25ppm 0.01--Water and minor components 100% 100%---

Example 17 The following compact high density (0.96 Kg / l) dishwashing detergent composition was prepared according to the present invention. I II III IV V VI STPP-51.0 51.0--44.3 Citrate 17.0--50.0 40.2-Carbonate 17.5 14.0 20.0-8.0 33.6 Bicarbonate---26.0--Silicate 15.0 15.0 8.0-25.0 3.6 Metasilicic acid Salt 2.5 4.5 4.5---PB1 10.0 8.0 8.0---PB4---10.0--Percarbonate----11.8 4.8 Nonionic substances 2.0 1.5 1.5 3.0 1.9 5.9 TAED 2.0--4.0-1.4 HEDP 1.0- ----DETPMP 0.6-----MnTACN----0.01-PAAC-0.01 0.01---Paraffin 0.5 0.4 0.4 0.6--Protease 0.07 0.05 0.05 0.03 0.06 0.01 Amylase 0.01 0.01 0.01 0.02 0.02 0.006 ReSI-AMG 0.02 0.2 2.0 1.0 0.002 0.02 Pullulanase type II-----0.02 Lipase-0.001-0.005--BTA 0.3 0.2 0.2 0.3 0.3 0.3 Polycarboxylate 6.0---4.0 0.9 Perfume 0.2 0.1 0.1 0.2 0.2 0.2 pH 11.0 11.0 11.3 9.6 10.8 10.9 Others, sulfate and water 100% in total

Example 18 In accordance with the present invention, the following granular dishwashing detergent composition having a bulk density of 1.02 Kg / L was prepared. I II III IV V VI STPP 30.0 33.5 27.9 29.6 33.8 22.0 Carbonate 30.5 30.5 30.5 23.0 34.5 45.0 Silicate 7.0 7.5 12.6 13.3 3.2 6.2 Metasilicate-4.5----Percarbonate----4.0-PB1 4.4 4.5 4.3---NADCC---2.0-0.9 Nonionic 1.0 0.7 1.0 1.9 0.7 0.5 TAED 1.0---0.9-PAAC-0.004----Paraffin 0.25 0.25----Protease 0.036 0.021 0.03-0.006- Amylase 0.03 0.005 0.004-0.005-ReSI-AMG 0.2 0.02 2.0 2.0 0.02 0.005 Pullulanase type II-----0.002 Lipase 0.005-0.001---BTA 0.15 0.15--0.2-Perfume 0.2 0.2 0.05 0.1 0.2-pH 10.8 11.3 11.0 10.7 11.5 10.9 Others, sulfate and water 100% in total

Example 19 A tablet detergent composition of the present invention was prepared by compressing a granular dishwashing detergent composition using a standard 12 head rotary press at a pressure of 13 KN / cm ² .

[Table 3]

Example 20 In accordance with the present invention, the following liquid dishwashing detergent composition having a density of 1.40 Kg / L was prepared. I II III IV STPP 17.5 17.2 23.2 23.1 Carbonate-2.4--Silicate 6.1 24.9 30.7 22.4 NaOCl 1.1 1.1 1.1 1.2 Thickener 1.0 1.1 1.1 1.0 Nonionic substance-0.1 0.06 0.1 NaBz 0.7---ReSI-AMG 0.005 1.0 0.005 0.02 NaOH 1.9---KOH 3.6 3.0--Perfume 0.05---pH 11.7 10.9 10.8 11.0 Water 100% in total

Example 21 In accordance with the present invention, a dishwashing composition having the following tablet form was prepared. I II III IV V VI Phase 1 STPP 9.6 9.6 10.4 9.6 9.6 11.5 Silicate 0.5 0.7 1.6 1.0 1.0 2.4 SKS-6 1.5 1.50 2.30 2.25 Carbonate 2.3 2.7 3.5 3.6 4.1 5.2 HEDP 0.2 0.2 0.2 0.3 0.3 0.3 PB1 2.4 2.4 2.4 3.7 3.7 3.7 PAAC 0.002 0.002 0.002 0.003 0.004 0.004 ReSI-AMG 0.01 0.02 0.05 0.002 0.001 1.0 Pullulanase type II--0.01--0.02 Amylase 0.002 0.001 0.001 0.004 0.003 0.003 Protease 0.002 0.002 0.002 0.003 0.003 0.003 Nonionic substance 0.4 0.8 0.8 1.2 1.2 1.2 PEG6000 0.4 0.3 0.3 0.4 0.4 0.4 BTA 0.04 0.04 0.04-0.06 0.06 Paraffin 0.1 0.1 0.1 0.15 0.15 0.15 Fragrance 0.02 0.02 0.02 0.01 0.01 0.01 Sulfate---0.5 0.05 2.3 Phase 2 ReSI-AMG 0.003 0.003 0.002 0.01 0.01 0.01 Amylase 0.0005 0.0005 0.0004 0.0005 0.006 0.0004 Protease 0.009 0.008 0.01 0.009 0.008 0.01 Citric acid 0.3 0.3 0.3 0.30 Sulfamic acid-0.3--0.3-Bicarbonate 1.1 0.4 0.4 1.1 0.4 0.4 Carbonate - 0.5 - - 0.5 - Silicate _{- - 0.6 - - 0.6 CaCl 2} - 0.07 - - 0.07 - PEG3000 0.06 0.06 0.06 0.06 0.06 0.06

A multiphase tablet composition was prepared as follows. The Phase 1 detergent active composition was mixed with the granular and liquid ingredients and then placed in a conventional rotary press die. The press includes a punch having a shape suitable for forming a mold. The die cross section is approximately 30 x 38 mm. The composition is then subjected to a compressive force of 940 kg / cm ² .
The punch is then pulled up to expose the first phase of the tablet containing the mold on the upper surface. The Phase 2 detergent active composition is prepared in a similar manner and placed in a die. The particulate active composition is then subjected to a compression force of 170 kg / cm ² , the punch is pulled up and the multiphase tablets are removed from the tablet press. The tablets formed dissolve or disintegrate in the above washing machine within 12 minutes and the phase 2 of the tablets dissolves within 5 minutes. These tablets have good solubility and cleaning properties and good tablet integrity and strength.

Example 22 The following hand dishwashing composition was prepared according to the present invention.

[Table 4]

Example 23 The following fabric and hard surface cleaner compositions were prepared according to the present invention. Sulfate 18.5 Bicarbonate 4.1 Polycarboxylate 18.6 C18 alpha-olefin 0.2 Enzyme (lipase, protease and / or cellulase) 0.004 Amylase 0.003 ReSI-AMG 0.05 Brightener 20 .1 Light activated bleach 0.04 Coated sodium percarbonate 45.0 TAED 8.8 Citric acid 2.5 Perfume 0.1 Others and water 100% in total

─────────────────────────────────────────────────── ─── Continued front page    (81) Designated countries EP (AT, BE, CH, CY, DE, DK, ES, FI, FR, GB, GR, IE, I T, LU, MC, NL, PT, SE), OA (BF, BJ , CF, CG, CI, CM, GA, GN, GW, ML, MR, NE, SN, TD, TG), AP (GH, GM, K E, LS, MW, MZ, SD, SL, SZ, TZ, UG , ZW), EA (AM, AZ, BY, KG, KZ, MD, RU, TJ, TM), AE, AL, AM, AT, AU, AZ, BA, BB, BG, BR, BY, CA, CH, C N, CR, CU, CZ, DE, DK, DM, EE, ES , FI, GB, GD, GE, GH, GM, HR, HU, ID, IL, IN, IS, JP, KE, KG, KP, K R, KZ, LC, LK, LR, LS, LT, LU, LV , MA, MD, MG, MK, MN, MW, MX, NO, NZ, PL, PT, RO, RU, SD, SE, SG, S I, SK, SL, TJ, TM, TR, TT, TZ, UA , UG, US, UZ, VN, YU, ZA, ZW (72) Inventor Johann, Sumetsu             Beer, Belgium 3210 Rubik, Bole             Nberg, 79 (72) Inventor Alfred, Bush             Belgium 1840 Ronda Tse             Le Handelsstraat, 210 F-term (reference) 4H003 AB03 AB19 AB27 AB31 AE06                       BA27 DA01 DA05 DA17 DA19                       EA12 EA15 EA16 EA24 EA28                       EB07 EB08 EB12 EB13 EB19                       EB22 EB25 EB26 EB32 EB36                       EC01 EC02 EC03 EE05 FA43                       FA47

Claims (12)

[Claims] 1. A detergent component and an aged starch degrading enzyme, wherein the aged starch degrading enzyme has an aged starch index (ReSI) of about 4.
% Of the detergent composition. 2. The aged starch degrading enzyme has an aged starch index (ReSI) of about 3%.
Detergent composition according to claim 1, characterized in that it is less than. 3. The detergent composition of claim 1, wherein the aged starch degrading enzyme is comprised in an amount of about 0.0002 to about 10% pure enzyme by weight of the total detergent composition. 4. The detergent composition of claim 3, wherein the aged starch degrading enzyme is comprised in an amount of about 0.002 to about 2% pure enzyme by weight of the total detergent composition. 5. The detergent composition of claim 4, wherein the aged starch degrading enzyme is comprised in an amount of about 0.002 to about 1% by weight pure enzyme of the total detergent composition. 6. The aged starch degrading enzyme is amyloglucosidase EC 3.2.1.3, α
-Amylase EC 3.2.1.1, beta-amylase EC 3.2.1.2, isoamylase EC 3.2.1.68, pullulanase type IEC 3.2.1.4
1, Isopullulanase EC 3.2.1.57, Neopullulanase EC 3.2.1
． 135, pullulanase type II, dextrin dextranase EC2.4.
1.24, cyclodextrin glycosyl transferase EC 2.4.1.
The detergent composition according to claim 1, which is selected from the group consisting of 19, malt gene alpha-amylase C 3.2.1.33 and / or mixtures thereof. 7. The detergent composition according to claim 1, wherein the aging starch degrading enzyme has a starch binding region, or a starch binding region is added to the aging starch degrading enzyme. 8. The method of claim 1, further comprising an enzyme selected from the group consisting of lipases, proteases, conventional amylases, conventional amylolytic enzymes, conventional pullulanase type II and / or mixtures thereof. Detergent composition. 9. The detergent composition according to claim 1, wherein the detergent component is selected from the group consisting of anti-redeposition agents, bleaching agents, nonionic surfactants, and / or mixtures thereof. 10. Aged starch index (ReS) for hydrolyzing aged starch.
Use of aged starch degrading enzymes, characterized in that I) is less than about 4%. 11. The aged starch degrading enzyme has an aged starch index (ReSI) of about 3%.
Use of the aged starch degrading enzyme according to claim 10, characterized in that it is less than. 12. Use of the aged starch-degrading enzyme according to claim 10 for maintaining whiteness and obtaining excellent performance for cleaning thin soils.