JPH051319B2 - - Google Patents

Description

[Detailed description of the invention]

[Industrial Field of Application] The present invention relates to a cleaning composition. More specifically, the present invention relates to a detergent composition containing cellulase and cholesterol oxidase and having extremely excellent detergency. [Prior Art] In recent years, there has been significant progress in washing clothes. That is, washing clothes has become significantly easier due to the development of raw materials suitable for detergents, improvements in water quality, improvements and spread of washing machines, improvements in fibers, etc. In particular, improvements in raw materials for detergents have been remarkable, and it appears that the composition of laundry detergents has almost reached the point of perfection through modifications of surfactants, builders, dispersants, fluorescent dyes, bleaching agents, etc. be. However, the idea behind the development of laundry detergents is that (1) surfactants and builders adsorb to the dirt and/or fiber surface, thereby reducing the bond between the dirt and/or fiber and water; (2) Disperse and solubilize dirt with surfactants and inorganic builders; (3) Chemically decompose dirt with enzymes such as protease; (4) Bleaching colored stains with bleach, etc., (5) Adsorbing fluorescent dyes etc. to the fiber surface to brighten it, (6) Preventing precipitation due to divalent metal ions, which are effective ingredients for cleaning, with a chelating agent. It can be summarized as follows. That is, the basis of conventional clothing cleaning has been how to effectively incorporate components that directly attack dirt or components that assist in the attacking power of such components as one component of the detergent composition. [Problems to be Solved by the Invention] However, at present, the cleaning performance of cleaning compositions based on this basic principle has almost reached a saturation point in a sense, and there is a need for cleaning compositions with even higher cleaning power. The development of a composition has been desired. [Means for Solving the Problems] The present inventors have been actively investigating whether it is possible to grasp the various phenomena related to washing clothes from a completely new perspective without being bound by conventional preconceptions.
Quite unexpectedly, it was discovered by chance that by incorporating an enzyme, cellulase, into a cleaning composition, it showed an extremely excellent cleaning effect on unexpected stains that were completely unrelated to the enzymatic activity of cellulase. I found it. However, it has been found that it is difficult to obtain a general-purpose cleaning power by simply using cellulase as a component of a cleaning composition, and that an excellent general-purpose cleaning effect can be obtained by using it in combination with cholesterol oxidase. completed. That is, the present invention provides a cleaning composition characterized by containing cellulase and cholesterol oxidase. The essential cellulase of the present invention is not particularly limited, and may be those widely distributed in animals, plants, bacteria, and fungi, as well as purified fractions thereof. Examples of the origins of cellulases include those shown below. (a) Those originating from protozoa (ciliates, flagellates, amoebae, etc.) include (1) Endoplodinum neglectum, (2) Trichomonas thermocidus.
termopsidus) (b) Those originating from molluscs (snails, skull snails, giant snails, sea bream beetles, etc.) include (1) Helix ponatia;
(2) Stromonas gigas,
(3) Dolabella auricula solander, (4) Mytilus Ostera, (5) Xylophaga dorsalis, (6)
Oryptochiton stetzleri
(7) Pterocera crocata, (8) Caelatura
hautecoeuri ruellani), (9)Melanoides tuberculata, (10)
Mya arenaria, (11) Mactra soliditsima
solidissima), (12) Bankia setacea, (13) Bankia indica, (14) Teredo,
(15) Modiola modeiolus (Modiola
modiolus), (16) Cryptoplax japonica, (17) Haliotis japonica, (18) Turbo cornutus, (19) Tegula preifferi, ( 20)
Lemintina imbricata (Lemintina)
imbricata), (21) Fasciolaria trapezium, (22) Dolabella auricura, (23)
Homoiodoris japonica (Homoiodoris
japonica), (24)Dendrodoris ruba var.
nigromaculata), (25) Onchidium verruculatum, (26) Euhadra
peliomphala), (27) Mytilus edulis, (28) Meretrix meretrix
lusoria), (29) Venerupis philippinarum, (30) Octopus sp. (c) Originating from nematodes, (1) Ditylenchus destructor, (2) Deitelenchus・Ditylenchus dipasaci (d) Originating from annelids (1) Eunice
aphroditois), (2) Tylorrhynchus heterochaetus, (3) Glycara chirori, (4) Loimia medusa, (5) Sabellastarte indica,
(6) Rhizodrilus sp., (7) Pheretina sp. (e) Those originating from echinoderms (sea urchins, etc.) include (1) Anthocidaris crassispina, (2) Soids Pseudocentrotus (Pseudocentrotus)
depressus), (2) Hemicentrotus pulcherrimus, (4) Psammechinus
(f) Those originating from crustaceans include (1) Mitella mitella, (2) Megaligia exotica,
(3) Calappa lophus, (4)
Gaetice depretusas (Gaetice)
depressus), (5) Pachygrapsus crassipes, (6) Pragsia crassipes
Plagusia dentipes, (7) Charybdis miles, (8) Carcinoplax longimanus, (9) Tiarinia cornigera, (10) Leptomithrachus edwardosi (Leptomithrax edwardsi), (11) Naxioides hystrix, (12)
Hapadogaster dentata
dentata), (13) Aniculus aniculus, (14) Dardanus crassimanus, (15) Upogebia major, (16)
Panulirus japonicus
japonicus), (17) Penaeus japonicus, (18) Scyllarides sieboldi, (19) Procambarus
(g) Originating from insects (ants, beetles, etc.) (1) Termes obesus, (2)
Ctenolepisma lineata
lineata), (3) Cerambyx cerdo, (4) Xestobium rufovillosum, (5) Nasutitermes exitiosus, (6) Coptotermes lacteus, ( 7)
Stromatium fulvum (Stromatius)
fulvum), (8) Dixippus morosus, (9) Limnoria lignorum, (h) Bacterial origin: (1) Bacillus hydrolyteix.
(2) Cellulobacillus mucosus, (3) Cellulobacillus myxogenes
myxogenes), (4) Cellulomonas sp., (5) Cellvibrio fulvus, (6) Cellvibrio fulvus.
Cellvibrio vulgaris, (7) Clostridium thermocellulaseum, (8) Clostridium thermocellulaseum
thermocellum), (9) Corynebacterium sp., (10) Cytophaga globulosa, (11) Pseudomonas fluorescens var.cellulosa,
(12) Pseudomonas solanacearum, (13) Bacterioides succinogenes
succinogenes), (14) Ruminococcus albus, (15) Ruminococcus flabefuaciens (Ruminococcus
flavefaciens), (16) Sorangium compositum, (17) Butyrivibrio, (18) Clostridium sp., (19) Xanthomonas sp.
Xanthomonas
cyamopsidis), (20) Sclerotium bataticola, (21) Bacillus sp., (22) Thermoactinomyces sp., (23)
Actinobifida sp. (i-) Fungi; those originating from Actinobacteria include (1) Actinomyces sp.;
(2) Streptomyces sp. (i-) Fungi; Those originating from filamentous fungi (deuteromycetes, algae, ascomycetes, etc.) include (1) Arthrobotrys superba; (2) Aspergillus aureus, (3) Aspergillus flavipes
(4) Aspergillus flavus, (5) Aspergillus fumigatus, (6) Aspergillus
luchuenis), (7) Aspergillus nidulans, (8) Aspergillus nidulans
Aspergillus niger, (9) Aspergillus oryzae, (10) Aspergillus rugulosus
rugulosus), (11) Aspergillus sydwi, (12) Aspergillus sydwi
Tamari (Aspergillus tamarii), (13) Aspergillus tellurois (Aspergillus
terreus), (14) Aspergillus unguis, (15) Aspergillus
Aspergillus ustus, (16) Takamine Cellulase, (17)
Aspergillus saitoi
saitoi), (18) Botrytis cinerea, (19) Botryodiplodia
theobromae), (20) Cladosporium cucumerium, (21) Cladosporium herbalum
herbarum), (22) Coccospora agricola, (23) Curvularia
Curvularia Lunata, (24) Chaetomium thermophile var.coprophile,
(25) Chaetomium thermophile var.
dissitum), (26) Sporotrichum thermophile, (27) Taromyces emersonii
emersonii), (28) Thermoascus aurantiacus, (29) Humicola grisea var.thermoidea, (30)
Humicola insolence
insolens), (31) Malbranchea pultierella bal sulfrea
pulchella var. sulfurea), (32) Myriococcum albomyces
(33) Stilbella thermophila, (34) Torula thermophila, (35) Chaetomium
globosum), (36) Dictyostelium discoideum,
(37) Fusarium sp., (38) Fusarium burbigenum
bulbigenum), (39) Fusarium equiseti, (40) Fusarium lateritium, (41) Fusarium lini, (42) Fusarium oxysporum
oxysporum), (43) Fusarium vasinfectum, (44) Fusarium dimerum, (45)
Fusarium japonicum
japonicum), (46) Fusarium scirpi, (47) Fusarium solani, (48) Fusarium moniliforme, (49) Fusarium roseum, (50)
Helminthosporium sp.
sp.), (51) Memnoniella echinata, (52) Humicola fucoatra, (53) Humicola grisea, (54) Monilia sitophila, (55) )
Monotospora brevis
(brevis), (56) Mucor pusils (Mucor
pusillus), (57) Mycosphaerella citrullina, (58) Myrothecium verrcaria,
(59) Papulaspora sp., (60)
Penicillium sp., (61) Penicillium capsulatum
capsulatum), (62) Penicillium chrysogenum, (63) Penicillium
frequentans), (64) Penicillium janthinellum, (65) Penicillium luteum, (6
6) Penicillium
piscarium), (67) Penicillium soppi, (68) Penicillium spinulosum, (69) Penicillium
turbatum), (70) Penicillium digitatum, (71) Penicillium digitatum
Penicillium expansum, (7
2) Penicillium pusillum
pusillum), (73) Penicillium rubrum, (74) Penicillium wortmanii, (75)
Penicillium variabile
variabile), (76) Pestalotia palmarum, (77) Pestalotiopsis
westerdikii), (78) Phoma sp. (79)
Schizophyllum comune
commune), (80) Scopulariopsis brevicaulis, (81)
Rhizopus sp. (82) Sporotrichum carnis, (83) Sporotrichum pruinosum
pruinosum), (84) Stachybotrys atra, (85) Torula spp.
sp.), (86) Trichoderma viride, (87) Trichurus cylindricus, (88) Verticillium alboatrum, (89) Aspergillus cellulosae ), (9
0) Penicillium glaucum
glaucum), (91) Cunninghamella sp., (92) Mucor mucedo, (93) Rhyzopus chinensis, (94) Coremiella sp., (95) Carlingia.・Rosea (Karlingia rorea), (96) Phytophthora cactorum, (97) Phytophthora citricola
citricola), (98) Phytophthora parasitica, (99) Pythium sp., (100) Saprolegniaceae, (101) Ceratocysteis.
Ceratocystis ulmi, (102) Chaetomium globosum,
(103) Chaetomium indicum, (104) Neurospora crassa, (105) Sclerotium
rolfsii), (106) Aspergillus sp.
sp.), (107) Chrysosporium lignorum, (108) Penicillium notatum, (109)
Pyricularia oryzae
oryzae) (i-) Fungi; those originating from the basidiomycetes include (1) Collybia verteipes;
veltipes), (2) Coprinus scleroteigenus, (3) Hydnum.
Hydnum henningsii, (4) Irpex lacteus, (5)
Polyporus sulfurois
sulphreus), (6) Polyporus betreus, (7) Polyporus betreus
Polystictus hirfutus, (8) Trametes vitata, (9) Irpex consolus, (10) Lentinus lepidois
(11)Poria vaporaria (Poria
vaporaria), (12) Fomes pinicola (Fomes
pinicola), (13) Lenzites styracina, (14) Merulius lacrymans, (15) Polyporus palstris, (1
6) Polyporus annosus
annosus), (17) Polyporus versicolor, (18) Polystictus sanguinois
sanguineus), (19) Poria vailantii, (20) Puccinia graminis, (21) Tricholoma fumosum, (22) Tricholoma nudum, (23) Trametes Sanguinea (Trametes)
sanguinea), (24) Polyporus schweinitzii FR, (25) Conidiophora cerevera
cerebella) (j) Originating from algae (1) Cladophora rupestris (Cladophora rupestris)
rupestris), (2) Ulva lactauca (Ulva
lactuca), (3) Laminaria digitata, (4) Rhodymenia palmata (k) Those originating from lichens include (1) Usneaceae, (2) Cladoniaceae, (3) Parmeliaceae, (4) Umbilicariaceae (l) Those originating from terrestrial green plants include (1) Tobacco, (2) Pineapple stem,
(3) Stem of Acer soido plane tree (Acer
pseudoplatanus stem), (4) kidney bean leaves, (5)
Swiss chard, (6) spinach, (7) Solanum dulcamara root,
(8) Western squash, (9) the end of asparagus, (10) barley, (11) malt, and alkaline cellulase can also be used. (m) The microorganism deposit number is FEIKEN Bacteria No. 1138, No.
Cellulases cultured and collected from bacteria belonging to the genus Bacillus in Nos. 1139, 1140, and 1141 (see Japanese Patent Publication No. 1982-28515) (n) Dolabella auricula solander Cellulase originated from midgut gland extract (Biochem. J., (1966) 99 , 214-221) The present invention can use the following commercially available cellulases using these various sources. (1) Cellulase AP (Cellulase AP) Amano Pharmaceutical Co., Ltd. (2) Cellulosin AP (Cellulosin AP) Ueda Chemical Co., Ltd. (3) Cellulosin AC (Cellulosin
AC) Ueda Chemical Co., Ltd., (4) Cellulase-Onozuka, Yakult Manufacturing Co., Ltd., (5) Pancellase, Yakult Manufacturing Co., Ltd., (6) Macerozyme, Yakult Manufacturing Co., Ltd. Co., Ltd. (7)
Meicelase Meiji Seika Co., Ltd.
(8) Celluzyme Nagase Co., Ltd., (9) Solublu sclase Sankyo Co., Ltd., (10) Sanzyme Sankyo Co., Ltd.
(11) Cellulase A-12-C
C) Takeda Pharmaceutical Co., Ltd., (12) Toyo-Cellulase Toyo Jozo Co., Ltd.
(13) Driserase, Kyowa Hakko Kogyo Co., Ltd., (14) Luizyme, Luipold Werk, (15) Takamine
Cellulase (Takamine-Cellulase) Chemische Fabrik, (16)
Wallerstein Cellulase
-Cellulase) Sigma Chemicals
(17) Cellulase Type Sigma Chemicals, (18) Cellulase Serva Serva Laboratory, (19) Cellulase 36
(Cellulase 36) Rohm and Haas, (20) Miles Cellulase
4000 (Miles Cellulase 4000) Miles, (21) R&H Cellulase 35, 36, 38 CONC (R&H Cellulase 35, 36, 38 CONC) Philip Morris, (22) Combizym (Nisco)・Laboratory
Nysco Laboratory, (23) Cellulase, Makor Chemicals
Chemicals), (24) Cellucrust NOVO Industry, (25)
Cellulase Gist-Brocades The content of cellulase in the cleaning composition of the present invention is such that the enzymatic activity of cellulase is 0.001 unit/mg.
The composition contains 0.01 to 70% by weight of solids (1 unit/mg solids = 1.0 micro-mole (μ Mole) of glucose is produced from cellulose in 1 hour at 37°C and pH 5) or more. The amount is preferably 0.1 to 1.0% by weight, and more preferably 0.1 to 1.0% by weight. Alternatively, the content of cellulase is preferably such that the enzyme activity of cellulase in the bath is 0.1 to 1000 units/, more preferably 1 to 100 units/. The cleaning composition of the present invention has no restrictions on the pH range and can be used in a wide range of pH ranges from acidic to alkaline. As the essential component cholesterol oxidase other than cellulase of the present invention, cholesterol oxidase that is widely distributed in animals, plants, bacteria, and fungi, and purified fractions thereof can be used, and is not particularly limited. Examples of commercially available enzyme products and their manufacturers include ``Cholesterol Oxidase'' (Amano Pharmaceutical) ``Cholesterol Oxidase Takara'' (Takara Shuzo) ``Cholesterol Oxidase CO'' (Oriental Yeast Industry) ``Cholesterol Oxidase'' (Toyobo), etc. All of them can be used in the present invention. Cholesterol oxidase is blended into the detergent composition in a required amount depending on the purpose, but it is 0.001 to 1% by weight (preferably 0.02 to 1% by weight) in terms of purified enzyme.
3% by weight) is desirable. From the viewpoint of producing a detergent composition, it is preferable to use the enzyme as a crude enzyme or an enzyme granulate obtained by mixing the crude enzyme with other components in the detergent composition and granulating the mixture in advance. In this case, crude enzyme or granules are used so that the amount of purified enzyme is 0.001 to 5% by weight, for example, the amount used is preferably 0.002 to 10% by weight.
The purified enzyme is diluted to 0.1-5% by weight. The major advantage of the present invention is that it is particularly effective for removing stains on collars and cuffs that conventional detergents could not sufficiently remove, as well as inorganic solid stains such as fine mud stains and oil stains. It is also effective against complex stains, and is also very useful for improving phosphorus-free or low-phosphorus detergency. In other words, the present invention can be applied to (1) an alkaline phosphorus-free or low-phosphorus detergent when cleaning stains on cellulose fibers and blended fabrics with other types of fibers; (2) By applying the present invention to a weakly alkaline liquid phosphorus-free detergent, it is possible to obtain excellent cleaning power equivalent to or better than that of a weakly alkaline powder detergent containing a sufficient amount of phosphate. Also, neutral to weakly acidic detergents do not prevent the combined use of cellulase and cholesterol oxidase. Another great advantage of the present invention is that it can be applied to any form of cleaning agent. spray dried powder,
The product of the present invention can be obtained by adding cellulase and cholesterol oxidase to various forms such as powder blend powder, tablet, and liquid. Components other than cellulase and cholesterol oxidase in the detergent composition of the present invention are not particularly limited, and may be optionally blended according to the need for the inherent effects of the following components, for example. [1] Surfactant Anionic surfactants include linear or branched alkylbenzene sulfonates, alkyl or alkenyl ether sulfates, alkyl or alkenyl sulfates, olefin sulfonates,
Alkanesulfonates, saturated or unsaturated fatty acid salts, alkyl or alkenyl ether carboxylates, α-sulfo fatty acid salts or esters, amino acid type surfactants, N-acyl amino acid type surfactants, alkyl or alkenyl acidic phosphate esters, alkyl Amphoteric surfactants include carboxy or sulfobetaine type surfactants; Nonionic surfactants include polyoxyalkylene alkyl or alkenyl ethers, polyoxyethylene alkyl phenyl ethers, and higher Fatty acid alkanolamide or its alkylene oxide adduct, sucrose fatty acid ester,
Examples of the cationic surfactant include fatty acid glycerin monoester, alkylamine oxide, and quaternary ammonium salts. Preferably 10% by weight of one or more of the above surfactants in the composition
or more. Preferred surfactants include linear or branched alkylbenzene sulfonates, alkyl or alkenyl ether sulfates, alkyl or alkenyl sulfates, olefin sulfonates, alkanesulfonates, saturated or unsaturated fatty acid salts, carboxy or sulfonate Examples include betaine type surfactants, polyoxyalkylene alkyl or alkenyl ethers, polyoxyethylene alkyl phenyl ethers, higher fatty acid alkanolamides or salts thereof. [2] Divalent metal ion scavenger One or more builder components of the various alkali metal salts and alkanolamine salts listed below.
It can also contain up to 50% by weight. Phosphates such as tripolyphosphate and pyrophosphate, salts of phosphonic acids such as ethane-1,1-diphosphonate, salts of phosphonocarboxylic acids such as 2-phosphonobutane-1,2-dicarboxylic acid, and aspartic acid. , salts of amino acids such as glutamic acid,
Aminopolyacetates such as nitrilotriacetate and ethylenediaminetetraacetate, polymer electrolytes such as polyacrylic acid and polyaconitic acid, non-dissociated polymers such as polyethylene glycol and polyvinylpyrrolidone, salts of organic acids such as oxalic acid and citric acid. ,
Aluminosilicate [3] Alkaline agent or inorganic electrolyte Further, as an alkaline agent or inorganic electrolyte, one or more of the following various alkali metal salts are added in an amount of 1 to 50% by weight, preferably 5 to 30% by weight in the composition. % by weight. Silicates, carbonates, sulfates. In addition, as organic alkali agents, triethanolamine, diethanolamine, monoethanolamine, triisopropanolamine, etc. [4] Anti-restaining agent Further, one or more of the following compounds can be contained in the composition in an amount of 0.1 to 5% as an anti-restaining agent. polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone,
carboxymethylcellulose etc. Among these, the combination of carboxymethyl cellulose or polyethylene glycol with the cellulase and cholesterol oxidase of the present invention has a synergistic effect in removing mud stains. In order to avoid decomposition of carboxymethylcellulose by cellulase in detergents, it is desirable to blend carboxymethylcellulose in the form of granulation or coating. [5] Bleaching agents Bleaching agents such as sodium percarbonate, sodium perborate, sodium sulfate hydrogen peroxide adduct, sodium chloride hydrogen peroxide adduct, and/or photosensitive agents such as sulfonated phthalocyanine zinc salt, or aluminum salt. The combined use of a bleaching dye or the like with the cellulase and cholesterol oxidase of the present invention further improves the cleaning effect. [6] Enzymes (enzymes that perform their original enzymatic action during the washing process, excluding cellulase and cholesterol oxidase) Classified based on enzyme reactivity: hydrolases, lyases, oxidoreductases, and ligases , transferases, and isomerases, any of which can be applied to the present invention. Particularly preferred are hydrolases, including proteases, esterases, carbohydrases and nucleases. Specific examples of proteases include pepsin, trypsin, chymotrypsin, collagenase, keratinase, elastase, sptilisin,
BPN, papain, promeline, carboxypeptase A and B, aminopeptidase, aspergylopeptidase A and B. Specific examples of esterases include gastric lipase, pancreatic lipase, plant lipases, phospholipases, cholinesterases, and phosphotases. Carbohydrases other than cellulases that are characteristic of the present invention include maltase, satucarase, amylase, pectinase, lysozyme,
α-glycosidase is mentioned. [7] Inhibitors of factors that inhibit cellulase activity Cellulase activity may be inactivated by the presence of ions and compounds such as copper, zinc, chromium, mercury, lead, manganese, and silver. Various metal chelators and metal precipitators are effective against these inhibitory factors. Examples thereof include the divalent metal ion scavenger mentioned in optional component [2], magnesium silicate, magnesium sulfate, and the like. Cellbiose, glycols and gluconolactone are also sometimes inhibitors. Avoid the coexistence of these types of sugars and cellulases as much as possible, or if coexistence cannot be avoided, take measures to avoid direct contact between these sugars and cellulases.
For example, a method of coating each is needed. Strong chelating agents such as ethylenediaminetetraacetate, anionic surfactants, and cationic surfactants can also be inhibitors in some cases. The coexistence of these substances and cellulase is also possible by devising manufacturing techniques such as tableting and coating methods. The above-mentioned anti-inflammatory agents or methods can be combined or applied depending on the case. [8] Cellulase activator Depending on the type of cellulase, protein,
cobalt and its salts, calcium and its salts,
Potassium and its salts, sodium and its salts,
When monosaccharides such as mannose and xylose are present, cellulase is activated and the cleaning effect is dramatically improved. In addition, a bluing agent, a fluorescent dye, an anti-caking agent, an antioxidant, a solubilizer, and the like may be added as necessary. [Function] As mentioned above, the present invention is characterized by using cellulase and cholesterol oxidase as components of the cleaning composition. It exhibits remarkable cleaning properties for collar stains that change over time due to the mixture of oils. As mentioned above, the use of enzymes in the technical field of detergents is known, but only enzymes that are particularly effective against dirt are known. That is, brotease is known to be effective against protein stains, amylase is known to be effective against starch stains, and lipase is known to be effective against oil stains, all of which are enzymes that directly attack stains. Although the cleaning action of the enzyme on collar stains in the present invention is not yet fully elucidated, by using cellulase in combination with cholesterol oxidase, collar stains can be removed, which is considered to be the essence of the cleaning action of cellulase. It is thought that this reduces one factor that inhibits the hydrolytic action of cellulase on fibers, and it is also thought that hydrogen peroxide produced when oxidizing cholesterol in collar stains has bleaching ability. That is, the cleaning action in the present invention is not based on a mere swelling action of fibers whose essence can be seen in the surfactant. [Effects of the Invention] Thus, according to the present invention, by using the cleaning composition of the present invention containing cellulase and cholesterol oxidase, an excellent cleaning effect can be obtained in a wide range of PH of the cleaning bath. As is well known, enzymes exhibit their maximum enzymatic activity at an optimum pH; however, cellulase, which exhibits an optimum pH in an acidic region, can provide sufficient cleaning performance even in alkaline conditions when used in combination with cholesterol oxidase. Furthermore, if an alkali-resistant cellulase is used, the effect will be even more pronounced. In addition, no difference was observed in the strength of the fibers to be cleaned compared to conventional cleaning agents. Furthermore, this effect more than compensates for the decrease in detergency caused by the decrease in alkaline ability among the builder effects accompanying the decrease in the pH of the cleaning bath during cleaning. Next, the present invention will be specifically explained with reference to Examples. Note that the percentages in the examples are based on weight unless otherwise specified. The following examples were examined under the following conditions. 1. Contaminated natural collar cloth; Cotton gold cloth #2023 was sewn onto the collar of a dress shirt and an adult male was allowed to wear it for 3 days. 25 days after wearing
After leaving it at ℃ and 65% PH for one month, the degree of staining was divided into three levels, and among the most heavily soiled fabrics, the cloth with stains symmetrical about the center point was selected.
The cloth was cut in half at the symmetrical point of the stain and used for experiments. 2. Cleaning conditions and methods When cleaning naturally contaminated fabrics, cut a 9cm x 30cm naturally contaminated fabric in half at symmetrical positions, and wash one of the 9cm x 15cm pairs of contaminated fabrics with a standard detergent that does not contain enzymes. , and one side was washed with the detergent of the present invention, which is a comparison detergent. First, naturally contaminated cloth pieces.
Sewn 15 sheets onto a 50cm x 50cm cotton cloth, add 1kg of the contaminated cloth and cotton underwear to a 0.665% detergent solution (6) in the case of powdered detergent, soak it at 30℃ for 2 hours, and then use Toshiba's Transfer to washing machine "Ginga"
After adjusting the total volume to 30%, wash with strong inversion for 10 minutes,
After drying, it was subjected to evaluation. In the case of liquid detergent,
Apply cc of detergent solution evenly to the contaminated cloth, and after 10 minutes, combine it with cotton underwear to make a total weight of 1 kg, transfer it to a Toshiba washing machine "Ginga", make a total volume of 30 kg, and use strong inversion.
It was washed for 10 minutes, dried, and then subjected to evaluation. A half-cut fabric washed with the standard detergent and a half-cut fabric washed with the detergent of the present invention were evaluated by pairwise comparison by visual judgment. Cleaning cloths were ranked based on standard soiling, which is ranked in 10 levels to indicate the degree of soiling. The detergency was expressed as a score for the detergency of the detergent of the present invention, with the detergency of the reference detergent set at 100. A difference in detergency index of 0.5 or more can be considered a significant difference. 3 Enzyme used Alkaline cellulase Kao soap, origin Bacillus sp.
Aspergillus niger) Cholesterol oxidase Oriental Yeast Co., Ltd., Origin Nocardia sp. Lipase Gist Procades NV, Origin R.Oryzae Amylase Novo Industries, Termamil 60G Brotease Novo Industries, Alcalase 2.0M Example 1 The following detergent formulation A highly alkaline powder laundry detergent was prepared. Furthermore, the pH of a 0.665% aqueous solution of detergent is
It was 11.3. Linear sodium dodecylbenzenesulfonate 20% Soap (sodium tallow fatty acid) 2% Sodium orthophosphate 20% Sodium metasilicate 10% Sodium carbonate 15% Carboxymethyl cellulose 1% Polyethylene glycol 1% Fluorescent dye 0.4% Glauber's salt Balance Enzyme 0 or 2 % Moisture 5% Table 1 shows the results of cleaning tests using various detergents obtained.
Shown below. The detergent numbers in the table are expressed as Example number minus Enzyme number used. (However, those that do not use enzymes are indicated as Example number -.)

[Table] Example 2 A weakly alkaline powder laundry detergent was prepared using the following formulation. The pH of a 0.665% aqueous solution of detergent is
It was 10.5. Sodium alpha olefin sulfonate 10% Sodium linear dodecylbenzenesulfonate 10% Soap 1% Sodium tripolyphosphate 20% Sodium silicate (JIS No. 2 Keiso) 10% Sodium carbonate 5% Carboxymethyl cellulose 1% Polyethylene glycol 1% Fluorescent dye 0.4 % Glauber's Salt Balance Enzyme 0 or 2% Moisture 10% A cleaning test was conducted in the same manner as in Example 1, and the results are shown in Table 2.

[Table] Example 3 A neutral powder laundry detergent was prepared using the following formulation. The pH of the 0.665% aqueous detergent solution was 7.2. Straight chain alcohol (=14) sulfate soda
30% Polyethylene glycol 1% Sodium phosphate 1% Fluorescent dye 0.2% Glauber's salt Balance Enzyme 0 or 2% Water 5% The results of the cleaning test for each detergent are shown in Table 3.

[Table] Example 4 A phosphorus-free, weakly alkaline detergent was prepared using the following formulation. Linear sodium dodecylbenzenesulfonate 15% Sodium alkyl ethoxy sulfate ( _C14 - _C15 ,
= 3 moles) 5% Builders and enzymes (see Table 4) 20% Sodium silicate 15% Sodium carbonate 15% Sodium polyacrylate 1.5% Polyethylene glycol 1.5% Fluorescent dye 0.5% Glauber's salt Balance Moisture 5% Washing test results It is shown in Table 4.

【table】

[Table] Example 5 A weakly alkaline powder laundry detergent was prepared using the following formulation. Sodium alkyl sulfate (=14.5) 15% Sodium alkyl ethoxy sulfate (=14.5,
EO=3) 5% Soap (tallow-based) 2% Sodium pyrophosphate 18% Sodium silicate 13% Sodium carbonate 5% Polyethylene glycol 2% Fluorescent dye 0.2% Glauber's salt Balance Magnesium silicate 1% Water 5% Enzyme 2% Soda carbonate 15% Table 5 shows the results of the cleaning test for each detergent obtained.

[Table] Example 6 A weakly alkaline liquid laundry detergent was prepared using the following formulation. The pH of the stock solution was 9.5. Secondary alcohol ethoxylate (=13.5,
EO=7.0) 10% Linear sodium dodecylbenzenesulfonate 20% Coconut fatty acid diethanolamide 3% Carboxymethyl cellulose 1% Polyethylene glycol (6000) 2% Potassium pyrophosphate 14% Sodium formate 1% Calcium chloride 0.01% Sodium metaxylene sulfonate 5% Enzyme 2% Water Balance Total 100% Table 6 shows the results of the cleaning test for each detergent obtained.

[Table] Example 7 A neutral liquid laundry detergent was prepared using the following formulation. The pH of the detergent stock solution was 7.0. Sodium alkyl ethoxy sulfate ( _C14-15 , =
3 mol) 20% Secondary alcohol (=13.5) Ethoxylate (=7) 25% Triethanolamine 1% Polyethylene glycol (6000) 2% Carboxymethyl cellulose 1% Citric acid 1% Fluorescent dye 0.3% Blue tinting agent 0.05 % EtoH 8% Water Balance Enzyme 2% Total 100% Table 7 shows the results of the cleaning test for each detergent obtained.

【table】

Claims (1)

[Claims] 1. A cleaning composition containing cellulase and cholesterol oxidase.