JPH0336078B2 - - 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, glucose oxidase, or β-glucosidase 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 stage of completion through modifications to surfactants, builders, dispersants, fluorescent dyes, bleaching agents, etc. . However, the idea behind the development of laundry detergents is that (1) the adsorption of surfactants and builders on the dirt and/or fiber surface reduces 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. on the fiber surface,
(6) Using a chelating agent to prevent the precipitation of divalent metal ions in ingredients that are effective for cleaning. 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 a detergent composition. [Problems to be Solved by the Invention] However, at present, the cleaning performance of cleaning compositions based on the above basics has almost reached a saturation point in a sense, and there is a need for cleaning compositions with even higher cleaning power. development was desired. [Means for Solving the Problems] The present inventors have been actively investigating whether it is possible to grasp 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 had nothing to do with the enzymatic activity of cellulase. I also found out. However, it is difficult to obtain general-purpose cleaning power by simply using cellulase as a component of a cleaning composition, and if one or two specific enzymes are used in combination, an excellent general-purpose cleaning effect can be obtained. They discovered this and completed the present invention. That is, the present invention provides a cleaning composition characterized by containing cellulase, glucose oxidase, or both cellulase and β-glucosidase. The essential component cellulase of the present invention includes animals and plants,
Those widely distributed among bacteria and fungi and their purified fractions can be used, and there are no particular limitations. Examples of the origins of cellulases include those shown below. (a) Originating from protozoa (ciliates, flagellates, amoebae, etc.) (1) Endoplo-dinum neglectum, (2) Trichomonas thermocidus
termopsidus) (b) Originating from molluscs (snails, skull snails, giant snails, sea bream beetles, etc.) (1) Helix ponateia
(2) Stromonas gigas, (3) Dolabella auricula
solander), (4) Mytilus Ostera, (5) Xylophaga dorsalis, (6) Cryptochiton stelleri, (7)
Pterocera crocate,
(8) Caelatura hautecoeuri ruellani, (9) Melanoides
tuberculata), (10) Mia arenaria (Mya
(11) Mactra solidissima, (12) Bankia setacea, (13) Bankia indica, (14) Teredo, (15) Modeiola modeiolus (Modiola modiolus), (16) Cryptoplax japonica,
(17) Haliotis japonica (Haliotis
japonica), (18) Turbo
cornutus), (19) Tegula pfeifferi, (20) Lemintina imbricata, (21) Fasciolaria
trapezium), (22) Dolabella auricura, (23) Homoiodoris japonica,
(24)Dendrodoris ruba var
nigromaculata), (25) Onchidium verruculatum, (26)
Euhadra perionhuara
(27) Mytilus edulis, (28) Meratrix meretrix
lusoria), (29) Venerupis philipinarum, (30) Octopus sp. (c) Originated from nematodes: (1) Ditylenchus destructor, (2) Deitelenchus・Ditylenchus dipasaci, (d) as 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) Originating from echinoderms (sea urchins, etc.) (1) Anthocidaris crassispina, (2) Soids Pseudocentrotus (Pseudocentrotus)
depressus), (3) Hemicentrotus pulcherrimus, (4) Psammechinus
(f) Originating from crustaceans (1) Mitella mitella, (2) Megaligia exoteica
exotica), (3) Calappa lohus (Calappa
lophus), (4) Gaetice depressus, (5) Pachygrapsus crassipes, (6) Plagusia dentipes, (7)
Charybdis miles,
(8) Carcinoplax longimanus, (9) Tiarinia cornigera, (10) Leptomithrax edwardsi, (11) Naxioides hystrix,
(12) Hapalogaster dentata, (13) Aniclus
Aniculus aniculus, (14) Dardanus cratusimanus
crassimanus), (15) Upogebia major, (16) Panulirus japonicus, (17) Penaeus japonicus,
(18) Scyllarides sieboldi, (19) Procambarus clarkii (g) Originating from insects (ants, beetles, etc.) (1) Termes obesus;
(2) Ctenolepisma lineata (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
cyamopsidis), (20) Sclerotium bataticola, (21) Bacillus sp., (22) Thermoactinomyces sp.,
(23) Actinobifida sp.
sp.) (i-) Fungi; those originating from actinomycetes include (1) Actinomyces sp.
sp.), (2) Streptomyces sp., (i-) Fungi; those originating from filamentous fungi (Mycobacterium deuteromycetes, Mycobacterium chinensis, Ascomycetes, etc.) (1) Arthrobotrys superba (Arthrobotys superba), (2) Aspergillus aureus, (3)
Aspergillus flavibes (Aspergillus
flavipes), (4) Aspergillus flavus, (5) Aspergillus
Aspergillus fumigatus, (6) Aspergillus lucuenis
(7) Aspergillus nidulans, (8) Aspergillus niger, (9) Aspergillus oryzae
oryzae), (10) Aspergillus rugulosus, (11) Aspergillus sydwi, (12)
Aspergillus tamari
tamarii), (13) Aspergillus terreus, (14) Aspergillus unguis,
(15) Aspergillus ustus, (16) Takamine (-) Cellulase, (17)
Aspergillus saitoi
saitoi), (18) Botrytis cinerea, (19) Botryodiplodia
theobromae), (20) Cladosporium cucumerium,
(21) Cladosporium herbarum, (22) Coccospora agricola,
(23) Curvularia lunata (Curvularia
Lunata), (24) Chaetomium sermophyle bal coprophyle (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 insolens
insolens), (31) Malbranchea pultierella bal sulfrea (Malbranchea
pulchella var. sulfurea), (32) Myriococcum albomyces
(33) Stilbella thermophila, (34) Torula thermophila,
(35) Chaetomium globosum, (36) Dictyostelium discoideum, (37) Fusarium sp., (38) Fusarium
bulbigenum), (39) Fusarium equiseti, (40) Fusarium lateritium
lateritium), (41) Fusarium lini, (42) Fusarium oxysporum, (43)
Fusarium basinfuectum (Fusarium
vasinfectum), (44) Fusarium dimerum, (45) Fusarium japonicum,
(46) Fusarium silpi (Fusarium
scirpi), (47) Fusarium solani, (48) Fusarium moniliforme,
(49) Fusarium lozoime (Fusarium
roseum), (50) Helminthosporium sp., (51) Memnoniella echinata,
(52) Humicola fucoatla
fucoatra), (53) Humicola grisea, (54) Monilia sitophila, (55) Monotospora brevis,
(56) Mucor pusillus,
(57) Mycosphaeralla citrullina, (58) Myrothecium
verrcaria), (59) Papulaspora sp., (60) Penicillum sp., (61) Penicillum capsulatum,
(62) Penicillum chrysogenum, (63) Penicillium
(64) Penicillium janthinellum,
(65) Penicillium lutoim
luteum), (66) Penicillium piscarium, (67) Penicillium soppi, (68) Penicillium spinulosum
spinulosum), (69) Penicillium turbatum, (70) Penicillium daisitatum
digitatum), (71) Penicillium expansum, (72) Penicillium
pusillium), (73) Penicillium rubrum, (74) Penicillium waltmannii (Penicillium
wortmanii), (75) Penicillium variahbile, (76) Pestalotia palmarum
palmarum), (77) Pestaloteiopsis
Westerdaikie (Pestalotiopsis)
westerdikii), (78) Phoma species (Phoma
sp.), (79) Schizophyllum commune, (80) Scopulariopsis brevicaulis, (81) Rhizopus sp., (82) Sporotrichum carnis , (83)
Sporotrichum pruinosum, (84) Stachybotrys atra,
(85) Torula sp., (86) Trichoderma viride,
(87) Trichurus cylindricus, (88) Verticillium
alboatrum), (89) Aspergillus cellulosae, (90) Penicillium glaucum
(91) Cunninghamella sp., (92) Mucor mucedo, (93) Rhyzopus chinensis, (94) Coremiella sp. (95) Carlingia・Rosea (Karlingia rorea), (96)
Phytophthora cactrum
cactorum), (97) Phytophthora citricola, (98) Phytophthora parasitica
(99) Pythium spp.
sp.), (100) Saprolegniaceae, (101) Ceratocystis ulmi, (102) Chaetomium
globosum), (103) Chaetomium indicum, (104) Neurospora crassa,
(105) Sclerotium rolfsii, (106) Aspergillus sp., (107) Chrysosporium
lignorum), (108) Penicillium notatum, (109) Pyricularia oryzae (i-) Fungi; as those originating from the Basidiomycetes (1) Collybia
veltipes), (2) Coprinus scleroteigenus, (3) Hydnum henningsii
henningsii), (4) Irpex lacteus, (5) Polyporus sulphreus, (6) Polyporus betreus, (7)
Polystictus hirfutus, (8) Trametes vitata, (9) Irpex consolus, (10) Lentinus
lepideus), (11) Poria vaporaria, (12) Fomes pinicola, (13) Lenzites styracina,
(14) Merulius lacrimance (Merulius)
lacrymans), (15) Polyporus palstris, (16) Polyporus annosus,
(17) Polyporus versicolor, (18) Polystictus sanguinois
sanguineus), (19) Poria vailantii, (20) Puccinia graminis, (21) Tricholoma fumosum,
(22) Tricholoma nudoum
(23) Trametes sanguinea, (24) Polyporus scubainichii FR.
schweinitzii FR.), (25) Conidiophora cerebella (j) of algal origin (1) Cladophora rupestris, (2) Ulva lactuca, (3) Laminaria・Digitata (Laminaria digitata), (4) Rodeimenia ・
Rhodymenia palmata (k) Originated from lichens: (1) Usneaceae, (2) Cladoniaceae, (3) Parmeliaceae, (4) Umbilicariaceae. (l) Originating from terrestrial green plants: (1) Tobacco, (2) Pineapple stems.
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) end of asparagus, (10) barley, (11) malt.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 of No. 1139, No. 1140, and No. 1141 (see Japanese Patent Publication No. 50-28515) (n) Dolabella auricula solander Cellulase originating from midgut gland extract (Bio-
chem.J., (1966) 99 , 214-221) The present invention can use these various sources, for example, the following commercially available cellulases. (1) Cellulase AP Amano Pharmaceutical Co., Ltd. (2) Cellulosin AP
Ueda Chemical Co., Ltd. (3) Cellulosin AC
(Cellulosin AC) Ueda Chemical Co., Ltd. (4) Cellulase-Onozuka (Cellulase-Onozuka) Yakult Manufacturing Co., Ltd. (5) Pancellase (Pancellase) Yakult Manufacturing Co., Ltd. (6)
Macerozyme Kinki Yakult Manufacturing 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 (Cellulase A-12-C) Takeda Pharmaceutical Co., Ltd. Company, (12) Toyo-Cellulase Toyo Jozo Co., Ltd., (13)
Driserase, Kyowa Hakko Kogyo Co., Ltd., (14) Luizyme, Luipold Werk, (15) Takamine-Cellulase, Chemische Fabrik.
brik), (16) Wallerstein-Cellulase Sigma Chemicals, (17) Cellulase-Cellulase
Cellulase Type Sigma Chemicals, (18) Cellulase Serva Serva Laboratory, (19) Cellulase 36 Rohm and Haas Haas), (20) Miles
Cellulase 4000 (Miles), (21) R&H Cellulase 35,
36, 38 Conch (R&H Cellulase35, 36,
38CONC) Philip Morris Co.
Morris), (22) Combizym
Nysco Laboratory Co., Ltd.
(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 solid content (1 unit/mg solid content = 1.0 micromol (μMole) of glucose is produced from cellulose in 1 hour at 37°C and pH 5) or more is 0.01 to 70% by weight in the composition. The amount contained is preferably 0.1 to 10% by weight, and more preferably 0.1 to 10% 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/.
It is. As the essential components other than cellulase of the present invention, glucose oxidase or β-glucosidase, those widely distributed in animals, plants, bacteria, and fungi, as well as purified fractions thereof, can be used, and the optimal pH ranges from acidic to alkaline. It can also be used, and is not particularly limited. These glucose oxidases or β-
Glucosidase is included in cleaning compositions in the required amount depending on the purpose, but in terms of purified enzyme
0.001-5% by weight (preferably 0.02-3% by weight)
It is desirable to mix them. 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 in an amount of 0.001 to 5% by weight as the purified enzyme, for example, the amount used is 0.002 to 10% by weight, preferably 0.1 to 5% by weight.
The purified enzyme is diluted so that The major advantage of the present invention is that it is particularly effective in cleaning inorganic solid stains that conventional cleaning agents cannot sufficiently remove, such as fine mud stains, as well as stains on collars, cuffs, oil stains, etc. Furthermore, it is very useful for improving phosphorus-free or low-phosphorus detergency. Phosphate was effective in removing fine scale dirt that got between the fibers. However, due to the problem of eutrophication, the amount of phosphate added has been decreasing, and some products have had to be made phosphorus-free, making it extremely difficult to remove muddy dirt. Furthermore, it is well known that it is difficult to remove muddy dirt that has penetrated into cotton cloth, especially from areas where oil stains coexist. Housewives are also troubled by the muddy dirt that clings to the cotton-blend cloth trousers. The cleaning agent of the present invention brings light to the solution of such problems. That is, when cleaning muddy stains on cellulose fibers and blended fabrics with other types of fibers, for example, by applying the present invention to (1) an alkaline phosphorus-free or low-phosphorus detergent,
(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 sufficient phosphate. Furthermore, even in neutral to weakly acidic detergents, the combination use of cellulase and glucose oxidase, or combination thereof with β-glucosidase, is not prohibited. 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 glucose oxidase or both and β-glucosidase to various forms such as powder blend powder, tablet, and liquid. Components other than cellulase and glucose oxidase or these and β-glucosidase in the cleaning composition of the present invention are not particularly limited, and may be optionally blended depending on the essential effects of the following components, for example. [1] Surfactant Examples of 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-acylamino acid type surfactants, alkyl or alkenyl acidic phosphate esters, Examples of amphoteric surfactants include carboxy or sulfobetaine type surfactants, such as alkyl or alkenyl phosphate esters or salts thereof; Nonionic surfactants include polyoxyalkylene alkyl or alkenyl ethers, polyoxyethylene alkyl phenyl ethers, Examples of the cationic surfactant include higher fatty acid alkanolamide or its alkylene oxide adduct, sucrose fatty acid ester, 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 straight-chain 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 salts. 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 Furthermore, the composition contains 1 to 50% by weight, preferably 5 to 30% by weight of one or more of the various alkali metal salts shown below as an alkaline agent or inorganic electrolyte. can do. Silicates, carbonates, sulfates. Also, organic alkaline agents such as triethanolamine, diethanolamine, monoethanolamine, triisopropanolamine, etc. [4] Anti-restaining agent Furthermore, one or more of the following compounds can be contained in the composition in an amount of 0.1 to 5% as an anti-staining agent. polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone,
carboxymethylcellulose etc. Among these, the combined use of carboxymethyl cellulose or polyethylene glycol with the present invention has a synergistic effect in removing muddy dirt. 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] Bleach agents Bleaching agents such as sodium percarbonate, sodium perborate, sodium sulfate hydrogen peroxide adduct, sodium chloride hydrogen peroxide adduct, sodium chloride hydrogen peroxide adduct, and/or sulfonated phthalocyanine zinc salt Alternatively, the combined use of the alkaline cellulase of the present invention with a photosensitive bleaching dye such as an aluminum salt further improves the cleaning effect. [6] Enzymes (Enzymes that perform their original enzymatic action during the washing process, excluding cellulase, β-glucosidase, and glucose oxidase) Classified based on enzyme reactivity: hydrolases, lyases, and oxidoreductases 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, carboxypeptidase A and B, aminopeptidase, aspargylopeptidase A and B. Specific examples of esterases include gastric lipase, plant lipases, phospholipases, cholinesterases, and phosphotases. Carbohydrases other than cellulase and β-glucosidase that are characteristic of the present invention include:
Examples include conventional general maltase, satucalase, amylase, pectinase, lysozyme, and α-glycosidase. [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 chelating agents and metal precipitating agents 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, glycol 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, bluing agents, fluorescent dyes, anti-caking agents, antioxidants, solubilizers, etc. may also be added as necessary. [Function] As described above, the present invention is characterized by using cellulase and glucose oxidase, or these and β-glucosidase as components of a detergent composition, but surprisingly, the present invention has no relation to cellulase activity at all. It exhibits remarkable cleaning properties for inorganic stains, particularly collar stains that change over time due to a mixture of inorganic stains and oil secreted on the skin surface. 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, protease is known to fight protein stains, amylase is known to fight starch stains, and lipase is known to fight oil stains, all of which are enzymes that directly attack stains. Although the cleaning action of the enzyme in the present invention has not yet been completely elucidated, by allowing glucose oxidase to act on the glucose produced by the action of cellulase or cellulase and β-glucosidase, it is possible to eliminate the excess produced by the oxidation of glucose. It is thought that hydrogen oxide bleaches stains etc. on the fibers. That is, the cleaning action of the present invention is not based on the mere swelling action of the 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 glucose oxidase or both thereof and β-glucosidase, the pH of the cleaning bath can be excellent in a wide range of areas. A cleaning effect can be obtained. As is well known, enzymes exhibit their maximum enzymatic activity at an optimum pH, but even cellulases, which exhibit an optimum pH in an acidic region, can exhibit sufficient activity even in alkaline conditions when used in combination with glucose oxidase or β-glucosidase. Cleaning performance can be obtained. 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 provides an effect that 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. [Example] Next, the present invention will be specifically explained using 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 #2023 cloth is sewn onto the collar of a dress shirt and an adult male wears it for 3 days. 25 days after wearing
After leaving it for one month at ℃ and 65% RH, the degree of staining is divided into three levels, and from among the most heavily soiled fabrics, the fabric with the stains symmetrical to the center point is selected, and the fabric is cut in half at the symmetrical point of the stains. It was used for experiments. (2) Cleaning conditions and methods When cleaning naturally contaminated fabrics, cut a 9 cm x 30 cm naturally contaminated fabric in half at symmetrical positions, and wash one of the 9 cm x 15 cm pieces of contaminated fabric with a standard detergent without enzyme additives. One side was washed with a comparative detergent, the detergent of the present invention. First, a piece of naturally contaminated cloth.
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. 20 c.c. for liquid detergent.
After 10 minutes, the detergent solution was evenly applied to the contaminated cloth, and after 10 minutes, it was combined with cotton underwear to make a total weight of 1 kg.The cloth was transferred to a Toshiba washing machine "Ginga", the total volume was adjusted to 30 kg, and the cloth was washed for 10 minutes on a strong reverse rotation, and after drying. Submitted for judgment. 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.Feikoken Bacillus No. 1138,
16900HU/gsolid) Cellulase (SIGMA, Type, Origin
Aspergillus niger) β-glucosidase (SIGMA, Type
, origin Almond) Glucose oxidase (Oriental yeast origin Microorganisms) Lipase (Gist Procheites NV,
Origin: R.Oryzae) Amylase (Novo Industries, Inc.)
Termamil 60G) Protease (Novo Industries, Alcalase 2.0M) Example 1 A highly alkaline powder laundry detergent was prepared using the following detergent formulation. The pH of a 0.665% aqueous solution of detergent is
It was 11.3. Straight-chain sodium dodecylbenzenesulfonate 20% Soap (sodium tallow fatty acid) 2 Sodium orthophosphate 20 Sodium metasilicate 10 Sodium carbonate 15 Carboxymethylcellulose 1 Polyethylene glycol 1 Fluorescent dye 0.4 Sodium salt Balance enzyme 0 or 2% water 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. Alpha olefin sodium sulfonate 10% Linear sodium dodecylbenzenesulfonate 10〃 Soap 1〃 Sodium tripolyphosphate 20〃 Sodium silicate (JIS No. 2 Keiso) 10〃 Soda carbonate 5〃 Carboxymethylcellulose 1〃 Polyethylene glycol 1〃 Fluorescent dye 0.4〃 Glauber's Salt Balance Enzyme 0 or 2% Water 10〃 A cleaning test was conducted in the same manner as in Example 1, and the results are shown in Table 2.

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[Table] Example 3 A neutral powder laundry detergent was prepared using the following formulation. The pH of a 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〃 Sodium salt Balance enzyme 0 or 2〃 Moisture 5〃 The results of the cleaning test for each detergent are shown in Table 3.

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[Table] Example 4 A phosphorus-free, weakly alkaline detergent was prepared using the following formulation. Linear sodium dodecylbenzenesulfonate 15% Sodium alkyl ethoxy sulfate (C ₁₄ - C ₁₅ , =
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〃 Sodium salt balance moisture 5〃 Results of cleaning test It is shown in Table 4.

[Table] Example 5 In the formulation of Example 2, detergents were prepared using various combinations of enzymes. Table 5 shows the results of the cleaning test for each detergent obtained.

[Table] Example 6 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〃 Soybean salt Balance magnesium silicate 1% Water 5〃 Enzyme 2. Sodium percarbonate 15. Table 6 shows the results of the cleaning test for each detergent obtained.

[Table] Example 7 A weakly alkaline liquid laundry detergent was prepared using the following formulation. The pH of the detergent stock solution was 9.5. Secondary alcohol ethoxylate (=13.5,
=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 meta-xylene sulfonate 5 Enzyme 2 Water Balance Total 100% Table 7 shows the results of the cleaning test for each detergent obtained.

[Table] Example 8 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 (C _14-15 , = 3.0
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 8 shows the results of the cleaning test for each detergent obtained.

[Table] Example 9 Under the following conditions, the cleaning and bleaching ability of stains containing pigments was investigated using a combination of cellulase and glucose oxidase or a combination of cellulase, β-glucosidase and glucose oxidase. (Detergent formulation) Same as Example 1 (black tea contaminated cloth) After boiling 80 g of Nitto black tea (yellow package) in ion-exchanged water from Step 3 for about 15 minutes, strain it through a desiccated dry cotton cloth, and add cotton gold cloth # to this liquid. 2003 Soak cloth;
Boil for about 15 minutes. The sample was removed from the heat, left to stand for about 2 hours, then air-dried, washed with water until the washing solution became colorless, dehydrated, and pressed into a 10 cm x 10 cm test piece, which was used for experiments. (Washing conditions, method and evaluation method) Dissolve detergent in 4°DH hard water to prepare 0.133% detergent aqueous solution 1. Add 5 black tea contaminated cloths to the detergent aqueous solution and let stand at 40℃ for 2 hours. Transfer the detergent solution and black tea contaminated cloth to a stainless steel beaker for a Targotometer, and rinse at 100 rpm using a Tergotometer.
Wash with stirring at 20℃ for 10 minutes. After rinsing under running water, it was iron pressed and subjected to reflectance measurement. The washing bleaching rate was measured according to the following formula; 460 mμ of the original cloth before washing and the contaminated cloth before and after washing.
The reflectance was measured using a self-recording colorimeter (manufactured by Shimadzu Corporation), and the washing bleaching rate (%) was calculated using the following formula. Washing bleaching rate (%) = reflectance after washing and bleaching - reflectance before washing and bleaching/reflectance of original fabric - reflectance before washing and bleaching x 100 Table 9 shows the average value of five sheets.

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Claims (1)

[Claims] 1. A cleaning composition containing cellulase and glucose oxidase, or cellulase, β-glucosidase, and glucose oxidase.