JPH027999B2 - - Google Patents

Description

[Detailed description of the invention]

The present invention relates to cleaning compositions. More specifically, the present invention relates to an excellent phosphorus-free detergent composition containing specific enzymes and fluorescent dyes. The philosophy behind the current development of laundry detergents is
1) By adsorbing the dirt and/or surfactant and builder on the fiber surface, dirt and/or
and lowering the interfacial tension between fibers and water to physically and chemically separate dirt and fibers; 2) dispersing and solubilizing dirt with surfactants and inorganic builders;
3) Chemically decompose stains with enzymes such as protease, 4) Bleach colored stains with bleach, etc., 5)
By adsorbing fluorescent dye etc. on the fiber surface, whitening is achieved.
6) It can be summarized as using a chelating agent to prevent precipitation of components effective for cleaning due to divalent metal ions. The present invention was created as a result of focusing on improvements related to 5) above. The inventors of the present invention 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.
Completely unexpectedly, the inventors happened to discover the effect of enhancing the whitening effect of fluorescent dyes, which is completely unrelated to the enzymatic activity of an enzyme, cellulase, and completed the present invention. Fluorescent dyes are the most effective whitening agents and traditionally
An effective use of this expensive compound was proposed. Among these, various agents have been proposed that increase the amount of fluorescent dyes adsorbed onto clothing in a cleaning bath. However, even if an increase in adsorption is observed in a simple system of fluorescent dye and an adsorption promoter, the expected effect is not observed in a complex, multi-component detergent system, and it is said that there are almost no effective adsorption promoters. is the reality. Practical clothing is treated with a fluorescent agent to give it a beautiful white color, but washing usually causes the fluorescent agent to peel off and reduce its whiteness. Generally, a fluorescent agent is added to a laundry detergent to compensate for this peeling. Compounds that have the effect of even slightly increasing the dyeability of fluorescent agents during long washing cycles are of great practical importance. The reality is that almost no conventional technology has passed the barrier of evaluating long washing cycles. The present invention is an epoch-making technology that embodies the earnest needs of those skilled in the art, and the phosphorus-free detergent composition of the present invention is characterized by containing cellulase and fluorescent dye. . The details of the mechanism of the synergistic whitening effect of cellulase and fluorescent dye are unknown, but as a result of cellulase acting on fibers (especially cellulose fibers), the properties of the fiber surface change, making it easier for fluorescent dye to adsorb. I'm guessing that he may have gotten tired. Another great advantage of the present invention is that it is very useful in improving the detergency of phosphorus-free detergents. Phosphate was effective in removing fine scale dirt that got between the fibers. However, due to the problem of eutrophication, the amount of phosphate blended has been gradually decreasing, and as a result, it has been forced to eliminate phosphorus in some products.As a result, it has become extremely difficult to remove muddy stains, and the whitening effect of fluorescent dyes has become necessary. has finally become a demand. The cleaning agent of the present invention brings light to the solution of such problems. That is, when cleaning cellulose fibers and fabrics blended with other types of fibers, for example, by applying the present invention to 1) alkaline non-phosphorus detergents, 2) weak alkaline or neutral liquid non-phosphorus detergents. By applying the present invention to the above, it is possible to obtain an excellent finishing effect equivalent to or better than that of a weakly alkaline powder detergent containing a sufficient amount of phosphate. One of the other advantages of the present invention is that the whitening enhancement effect is not affected by the PH of the cleaning composition.
As is well known, enzymes exhibit their maximum enzymatic activity at an optimum pH; however, even if a cellulase that exhibits an optimum pH in an acidic region is used, a sufficient whitening enhancement effect can be obtained in an alkaline environment. . Furthermore, no difference in influence on the strength of the fibers to be washed was observed compared to conventional detergents. Another great advantage of the present invention is that it can be applied to any form of cleaning agent. spray dried powder,
Cellulases can be added to various forms such as spray-chilled powders, powder blends, tablets, liquids, etc. to obtain the products of the present invention. 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, but the optimum pH is 8.
Less than or equal to Examples of sources of cellulases with an optimum pH of less than 8 include those shown below. (a) Originating from protozoa (ciliates, flagellates, amoebae, etc.) (1) Endoplodinum neglectum, (2) Trichomonas thermocidus
termopsidus) (b) Originating from molluscs (snails, skull snails, giant snails, sea bream beetles, etc.) (1) Helix ponateia
(2) Stromona gigas, (3) Dolabella auricula
Solander), (4) Mytilus Ostera, (5) Xylopnaga dorsalis, (6) Cryptochiton stelleri, (7)
Pterocera crocata,
(8) Caelatura hautecoeuri ruellani, (9) Melanoides
tuberoulata), (10) Mia arenaria (Mya
(11) Mactra solidlssima, (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 auricula, (23) Homoiodoris japonica,
(24) Dendrodoris ruba var.
nigromaculata), (25) Cnchidium verruculatum, (26)
Euhadra bellionhuara (Euhadra)
peliomphala), (27) Mytilus edulis, (28) Meretrix meretrix
lusoria), (29) Venerupis phillppinarum, (30) Octopus sp. (c) Ditylenchus destructor, (2) Deitelenchus destructor, (2) Ditylenchus dipsaci) (d) As originating from annelids (1) Eunice aphrodite
aphroditois), (2) Tylorrhynchus heterochaetus, (3) Glycera 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
milians) (f) Originated from shellfish: (1) Mitella mitella, (2) Megaligia exoteica.
exotica), (3) Calappa lohus (Calappa
lophus), (4) Gaetice depressus, (5) Pachygrapsus crassipes, (6) Plagusia dentipes,
(7) Charybdis Mires
(8) Carcinoplax longimanus, (9) Tiarinia cornigera, (10) Leptomithrax edwardsi, (11) Naxioides hystrix ), (12)
Hapalogaster dentata
dentata), (13) Aniculus aniculus, (14) Dardanus crassimanus, (15)
Upogebia major,
(16) Panulirus japonicus
japonicus), (17) Panaeus japonicus, (18) Siladeides
Scyllarides sieboldi, (19)
Procambarus clarkii (Procambarus
clarkii) (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)
Stromatius fulvum
fulvum), (8) Dixippus morosus, (9) Limnoria Lignorum (h) Bacterial origin: (1) Bacillus hydrolyteix
hvdrolyticus), (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
(14) Ruminococcus albus, (15) Ruminococcus flabefuaciens
flavafaciens), (16) Sorangium compositum, (17) Butyrivibrio, (18) Clostridium sp., (19) Xanthomnas
cyamopsidis), (20) Sclerotium bataticola, (21) Bacillus sp., (22) Thermoactinomyces sp.,
(23) Actinobifida sp.
sp.) (i-) Bacterial species; those originating from actinomycetes: (1) Actinomyces sp.
(2) Streptomyces sp. (i-) Fungi; filamentous fungi (deuteromycetes, algae,
(1) Arthrobotrys superba, (2) Aspergillus aureus, (3) Aspergillus flavipes, etc.
(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, (11) Aspergillus tamarii, (13) Aspergillus tellurois
terreus), (14) Aspergillus unguis, (15) Aspergillus ustus, (16) Takamine-
(17) Aspergillus saitoi, (18) Botrytis cinerea, (19) Botryodiplodia theobromae, (20) Cladosporium
cucumerium), (21) Cladosporium herbarum, (22) Coccospora
agricola), (23) Curvularia Lunata, (24) Chaetomium
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,
(31) Marbranch Air Brutiera Bar
Sulfuria (Malbranchea pulchella var.
sulfurea), (32) Myriococcum albomyces, (33) Stilbella
thermophile), (34) Torula thermophila, (35) Chaetomium
Globosum (Chaetomium globosum), (36)
Diotyostelium discoideum, (37) Fusarium sp., (38) Fusarium bulbigenum, (39)
Fusarium equisetei (Fusarium
equiseti), (40) Fusarium lateritium, (41) Fusarium lateritium
Fusarium lini, (42) Fusarium oxysporum, (43)
Fusarium basinfuectum (Fusarium
vasinfectum), (44) Fusarium dimerum, (45) Fusarium japonicum, (46) Fusarium scirpi, (47)
Fusarium solani,
(48) Fusarium moniliforme (Fusarium
moniliforme), (49) Fusarium roseum, (50) Helminthosporium sp., (51) Memnoniella
echinata), (52) Humicola fucoatra, (53) Humicola grisea, (54) Monilia
Monilia sitophila, (55) Monotospora brevis,
(56) Mucor pusillus,
(57) Mycosphaerella citrullina, (58) Myrothecium
verrcaria), (59) Papulaspora sp., (60) Penicillium sp., (61) Penicillium capsulatum, (62)
Penicillium chrysogenum
chrysogenum), (63) Penicillium frequentans, (64)
Penicillium
janthinellum), (65) Penicillum luteum, (66) Penicillium luteum
Pisarium (Penicillium Piscarium), (67)
Penicillium soppi,
(68) Penicillium spinulosum, (69) Penicillium turbatum,
(70) Penicillium digitatum, (71) Penicillium expansum
expansum), (72), Penicillium pusillum, (73) Penicillium rubrum, (74)
Penicillium waltmannii
wortmanii), (75) Penicillium variabile, (76) Pestalotia palmarum,
(77) Pestalotiopsis westerdijkii, (78) Phoma sp., (79) Schizophyllum sp.
Schizophyllum commune, (80) Scopulariopsis brevicaulis, (81) Rhizopus sp., (82) Sporotrichum
Sporotricum carnis, (83) Sporotrichum pruinosum
prulnosum), (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
Mucor mucedo, (93) Rhizopus
Rhyzopus chinensis, (94) Coremiella sp., (95) Karlingia rosea, (96) Phytophthora
cactorum), (97) Phytophthora citricola, (98) Phytophthora parasitica
(99) Pythium spp.
sp.), (100) Saprolegniaceae, (101) Ceratocystisulmi, (102) Chaetomium
globosum), (103) Chaetomium indicum, (104) Neurospora crassa, (105)
Sclerotium rolfsi (Sclerotium
rolfsii), (106) Aspergillus sp., (107) Chrysosporium lignorum,
(108) Penicillium notatum
notatum), (109) Pyricularia oryzae, (i-) Fungi; as originating from the basidiomycete species (1) Collybia verteipes
veltipes), (2) Coprinus sclerotigenus, (3) Hydnum.
Hydnum henningsii, (4) Irpex lacteus, (5)
Polyporus sulfurois
sulphreus), (6) Polyporus betreus, (7) 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
(16) Polyporus annosus, (17) Polyporus versicolor, (18) Polystictus sanguineus, (19) Poria vailantii, ( 20) Puccinia gramiis, (21)
Tricholoma humosum
fumosum), (22) Tricholoma nudum, (23) Trametes sanguinea, (24) Polyporus scubainichii - FR.
schweinitzii FR.), (25) Konideio Ouora
Conidiophora cerebella (j) Of algal origin: (1) Cladophora rupestris, (2) Ulva lactuca, (3) Laminaria digitata, (4) Rodeimenia
Rhodymenia palmata (k) Originated from lichens: (1) Usneaceae, (2) Cladoniaceae, (3) Parmeliaceae, (4) Umbillicariaceae. (l) Originating from terrestrial green plants: (1) Tobacco, (2) Pineapple stems.
(3) Acerpseudoplatanus stem, (4) French bean leaf, (5) Swiss chard, (6) Spinach, (7) Solanum dulcamara root.
root), (8) Western squash, (9) end of asparagus,
(10) Barley, (11) Malt (m) Cellulase cultured and collected from a bacterium belonging to the genus Aeromonas with the microorganism deposit number No. 2306 (see JP-A-50-76287). Cellulases of the origin described in (a) to (l) generally have an optimum pH of acidic or neutral,
Suitable for acidic to neutral laundry detergents. The cellulase originating from (m) maintains high cellulase activity even at relatively high temperatures of around 40°C, and is suitable for weakly alkaline laundry detergents or laundry detergents that require long-term storage. Suitable. Compared to proteases that have conventionally been added to detergent systems, cellulase has a slightly lower optimal temperature, so it also has the advantage of low-temperature washing in terms of energy savings. In the present invention, for example, the following commercially available cellulases using these various sources can be used. (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 (Cellulase-Onozuka) Kinki Yakult Manufacturing Co., Ltd. (5) Pencellulase (Pancellase) Kinki Yakult Manufacturing Co., Ltd. (6) Macerozyme (Macerozyme) Kinki Yakult Manufacturing Co., Ltd. Co., Ltd., (7) Meicelase, Meiji Seika Co., Ltd., (8) Celluzyme, Nagase Co., Ltd., (9) Soluble,
sclase) Sankyo Co., Ltd., (10) Sanzyme Sankyo Co., Ltd., (11) Cellulase A-
12-C) (Cellulase A-12-C) Takeda Pharmaceutical Co., Ltd., (12) Toyo-Cellulase (Toyo-
Cellulase) Toyo Jozo Co., Ltd., (13) Driserase Kyowa Hakko Kogyo Co., Ltd., (14) Luizyme Luipold Werk, (15) Takamine-Cellulase Chemistry Fabric. (16) Walerstein-Cellulase
Sigma Chemicals,
(17) Cellulase Type
) Sigma Chemicals
Chemicals), (18) Cellulase Serva, Serva Laboratory, (19) Cellulase 36
(Cellulase 36) Rohm and Haas, (20) Milcs Cellulase 4000 (Miles), (21) R&H Cellulase 35, 36, 38 Conc. 36, 38 CONC)
Philip Morris, (22)
Combizym (Mysco Laboratory), (23) Cellulase (Makor)
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.
Solid content (1 unit/mg solid content = from carboxymethyl cellulose in 1 hour at 37°C and pH 5)
Produces 1.0 micromole (μMole) of glucose. ) or more is preferably contained in an amount of 0.01 to 70% by weight in the composition, more preferably,
It is 0.1-10% by weight. Alternatively, the content of cellulase should be determined so that the enzymatic activity of cellulase is 0.1~
An amount of 1000 units/unit is preferred, more preferably 1 to 100 units/unit. The fluorescent dye, which is another essential component of the present invention, is selected from compounds (a) to (f) represented by the following formulas. (However, X is

[Formula] Y is

[expression]) (However, X is

[Formula] Y is

[expression]) (However, X is

[Formula] Y is

[expression]) The content of fluorescent dye in the composition of the present invention is 0.01 to 5.
% by weight, preferably 0.1-2% by weight. In addition to these essential components, the detergent composition of the present invention may optionally use components of known phosphorus-free detergent compositions depending on the purpose. Examples of surfactants include the following. 1 Straight chain or branched chain alkylbenzene sulfonate having an alkyl group having an average carbon number of 10 to 16. 2 Contains a linear or branched alkyl group or alkenyl group with an average carbon number of 10 to 20, and an average of
0.5 to 8 moles of ethylene oxide or propylene oxide or butylene oxide or ethylene oxide/propylene oxide = 0.1/9.9 to 9.9/0.1 ratio or ethylene oxide/butylene oxide =
Alkyl or alkenyl ether sulfate added in a ratio of 0.1/9.9 to 9.9/0.1. 3. Alkyl or alkenyl sulfate having an alkyl group or alkenyl group having an average carbon number of 10 to 20. 4 Olefin sulfonate having an average of 10 to 20 carbon atoms in one molecule. 5 Alkanesulfonate having an average of 10 to 20 carbon atoms in one molecule. 6 Saturated or unsaturated fatty acid salt having an average of 10 to 24 carbon atoms in one molecule. 7 Having an alkyl group or alkenyl group with an average carbon number of 10 to 20, and an average of 0.5 to 8 moles of ethylene oxide, propylene oxide, or butylene oxide in one molecule, or ethylene oxide/propylene oxide = 0.1/
At a ratio of 9.9 to 9.9/0.1 or ethylene oxide/butylene oxide = 0.1/9.9 to 9.9/0.1
an alkyl or alkenyl ether carboxylate added in a ratio of 8 α-sulfo fatty acid or ester represented by the following formula. (In the formula, Y is an alkyl group having 1 to 3 carbon atoms or a counter ion, Z is a counter ion, and R is an alkyl group having 1 to 3 carbon atoms.
20 alkyl or alkenyl groups. ) Here, the counter ions of the anionic surfactant include alkali metal ions such as sodium and potassium, alkaline earth metal ions such as calcium and magnesium, ammonium ions, and 1 to 3 alkanol groups having 2 or 3 carbon atoms. Examples include alkanolamines (eg, monoethanolamine, diethanolamine, triethanolamine, triisopropanolamine, etc.) having 9 Amino acid type surfactant represented by the following general formula. (Here, R ₁ is an alkyl or alkenyl group having 8 to 24 carbon atoms, and R ₂ is hydrogen or a carbon number 1 to 2
_R3 represents an amino acid residue, and X represents an alkali metal or alkaline earth metal ion. ) (R ₁ , R ₂ and X are as described above. n is 1 to
Indicates an integer of 5. ) (R ₁ is as described above. m indicates an integer from 1 to 8.) (R ₁ , R ₃ and X are as described above. _{R 4} represents hydrogen or an alkyl or hydroxyalkyl group having 1 to 2 carbon atoms.) (R ₂ , R ₃ and X are as described above. R ₃ represents a β-hydroxyalkyl or β-hydroxyalkenyl group having 6 to 28 carbon atoms.) (R ₃ , R ₅ and X are as described above.) 10 Phosphate ester activator. No.1 Alkyl (or alkenyl) acidic phosphate ester (R' is an alkyl group or alkenyl group having 8 to 24 carbon atoms, n'+m'=3, n'=1 to 2) No.2 Alkyl (or alkenyl) phosphate ester (R′ is as mentioned above, n″+m″=3, n″=1
~3) No.3 Alkyl (or alkenyl) phosphate ester salt (R′, n″, m″ are as mentioned above, M is Na,
K, Ca) 11 A sulfonic acid type amphoteric surfactant represented by the following general formula. (Here, R ₁₁ is an alkyl or alkenyl group having 8 to 24 carbon atoms, R ₁₂ is an alkylene group having 1 to 4 carbon atoms, R ₁₃ is an alkyl group having 1 to 5 carbon atoms, R ₁₄
represents an alkylene or hydroxyalkylene group having 1 to 4 carbon atoms. ) (Here, R ₁₁ and R ₁₄ are as mentioned above, R ₁₅ ,
_R16 represents an alkyl or alkenyl group having 8 to 24 carbon atoms or 1 to 5 carbon atoms. ) (Here, R ₁₁ and R ₁₄ are as mentioned above, and n ₁ is 1
Indicates an integer between ~20. ) 12 Betaine type amphoteric activator represented by the general formula below. (Here, R ₂₁ is alkyl or alkenyl having 8 to 24 carbon atoms, β-hydroxyalkyl or β
-Hydroxyalkenyl group, _R22 has 1 or more carbon atoms
The alkyl group of 4 and _R23 represent an alkylene or hydroxyalkylene group having 1 to 6 carbon atoms. ) (Here, R ₂₁ and R ₂₃ are as mentioned above, and n ₂ is 1
Indicates an integer between ~20. ) (Here, R ₂₁ and R ₂₃ are as described above. _{R 24} represents a carboxyalkyl or hydroxyalkyl group having 2 to 5 carbon atoms.) 13 has an alkyl group or alkenyl group having an average of 10 to 20 carbon atoms, and 1 Polyoxide ethylene alkyl or alkenyl ether with ~20 moles of ethylene oxide added. 14 It has an alkyl group with an average carbon number of 6 to 12, and 1 to
Polyoxyethylene alkyl phenyl ether with 20 moles of ethylene oxide added. 15 Polyoxypropylene alkyl or alkenyl ether having an alkyl group or alkenyl group having an average carbon number of 10 to 20 and to which 1 to 20 moles of propylene oxide are added. 16 Polyoxybutylene alkyl or alkenyl ether having an alkyl group or alkenyl group having an average carbon number of 10 to 20 and added with 1 to 20 moles of butylene oxide. 17 Nonionic activator having an alkyl group or alkenyl group with an average carbon number of 10 to 20 and a total of 1 to 30 moles of ethylene oxide and propylene oxide or ethylene oxide and butylene oxide (ethylene oxide and propylene oxide or The ratio with butylene oxide is 0.1/9.9 to 9.9/0.1). 18 Higher fatty acid alkanolamide or its alkylene oxide adduct represented by the following general formula. (In the formula, R′ ₁₁ is an alkyl group having 10 to 20 carbon atoms,
or an alkenyl group, R' ₁₂ is H or CH ₃ , n ₃ is an integer of 1 to 3, and m ₃ is an integer of 0 to 3. ) 19 A sucrose fatty acid ester consisting of a fatty acid with an average carbon number of 10 to 20 and sucrose. 20 A fatty acid glycerin monoester consisting of a fatty acid with an average carbon number of 10 to 20 and glycerin. 21 Alkylamine oxide represented by the general formula below. (In the formula, R' ₁₃ is an alkyl group or alkenyl group having 10 to 20 carbon atoms, and R' ₁₄ and R' ₁₅ are each having 1 to 20 carbon atoms.
3 is an alkyl group. ) 22 A cationic surfactant represented by the general formula below. (Here, at least one of R' ₁ , R' ₂ , R' ₃ , and R' ₄ represents an alkyl or alkenyl group having 8 to 24 carbon atoms, and the others represent an alkyl group having 1 to 5 carbon atoms.X' indicates halogen.) (Here, R′ ₁ , R′ ₂ , R′ ₃ and X′ are as described above.) (Here, R′ ₁ , R′ ₂ , and X′ are as described above.
R′ ₅ is an alkylene group having 2 to 3 carbon atoms, and n ₄ is 1 to 20
indicates an integer. ) at least 10 surfactants in the composition.
It is preferable to contain it in an amount of % by weight or more from the viewpoint of effectiveness. Preferred surfactants include 1), 2), 3),
4), 5), 6), 11) No. 2, 12) No. 1, 13),
14), 15), 17), and 18). Furthermore, the following components are blended according to purpose and necessity. [1] Divalent metal ion scavenger 0 to 50 builder components of one or more of the following various alkali metal salts and alkanolamine salts.
It can also be contained in a weight percent. 1 Salts of amino acids such as aspartic acid, glutamic acid, and glycine. 2 Aminopolyacetates such as nitrilotriacetate, ethylenediaminetetraacetate, diethylenetriaminepentaacetate, iminodiacetate, glycol ether diaminetetraacetate, hydroxyethyliminodiacetate, diencholate, etc. 3 Polyacrylic acid, polyaconitic acid, polyitaconic acid, polycitraconic acid, polyfumaric acid,
Polymaleic acid, polymethaconic acid, poly-α-
Hydroxyacrylic acid, polyvinylphosphonic acid, sulfonated polymaleic acid, maleic anhydride-diisobutylene copolymer, maleic anhydride-styrene copolymer, maleic anhydride-methyl vinyl ether copolymer, maleic anhydride-ethylene copolymer , maleic anhydride-ethylene crosslink copolymer, maleic anhydride-vinyl acetate copolymer, maleic anhydride-acrylonitrile copolymer, maleic anhydride-acrylic ester copolymer, maleic anhydride-butadiene copolymer , maleic anhydride-isoprene copolymer, poly-β-ketocarboxylic acid derived from maleic anhydride and carbon monoxide, itaconic acid-ethylene copolymer, itaconic acid-aconitic acid copolymer, itaconic acid-maleic acid Copolymer, itaconic acid-acrylic acid copolymer, malonic acid-methylene copolymer, methaconic acid-fumaric acid copolymer, ethylene glycol-ethylene terephthalate copolymer, vinylpyrrolidone-vinyl acetate copolymer, 1- Butene-2,3,4-tricarboxylic acid-itaconic acid-acrylic acid copolymer, polyester polyaldehyde carboxylic acid with quaternary ammonium group, cis of epoxysuccinic acid
-isomer, poly[N,N-bis(carboxymethyl)acrylamide], poly(oxycarboxylic acid), starch succinic acid or maleic acid or terephthalic acid ester, starch phosphate ester, dicarboxystarch, dicarboxymethyl starch, Polymer electrolytes such as cellulose and succinate esters. 4 Non-dissociable polymers such as polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone, cold water soluble urethanized polyvinyl alcohol. 5 Salts of dicarboxylic acids such as oxalic acid, malonic acid, succinic acid, glutaric acid, adipic acid, pimelic acid, suberic acid, azelaic acid, decane-1,10-dicarboxylic acid; diglycolic acid, thiodiglycolic acid, oxal Salts of acetic acid, oxydisuccinic acid, carboxymethyloxysuccinic acid, carboxymethyltartronic acid, etc.; glycolic acid, malic acid, hydroxybivalic acid, tartaric acid, citric acid, lactic acid, gluconic acid, mucic acid,
Salts of hydroxycarboxylic acids such as glucuronic acid, dialdehyde starch oxide; itaconic acid,
Methylsuccinic acid, 3-methylglutaric acid, 2,
2-dimethylmalonic acid, maleic acid, fumaric acid, glutamic acid, 1,2,3-propanetricarboxylic acid, aconitic acid, 3-butene-1,
2,3-tricarboxylic acid, butane-1,2,
3,4-tetracarboxylic acid, ethanetetracarboxylic acid, etenetetracarboxylic acid, n-alkenyl aconitic acid, 1,2,3,4-cyclopentanetetracarboxylic acid, phthalic acid, trimesic acid, hemimellitic acid, pyromellitic acid , benzenehexacarboxylic acid, tetrahydrofuran-
Salts of 1,2,3,4-tetracarboxylic acid, tetrahydrofuran-2,2,5,5-tetracarboxylic acid, etc.; Sulfonation of sulfoitaconic acid, sulfotricarballylic acid, cysteic acid, sulfoacetic acid, sulfosuccinic acid, etc. Salts of carboxylic acids;
Carboxymethylated products such as sucrose, lactose, and raffinose, carboxymethylated pentaerythritol, carboxymethylated gluconic acid, condensates of polyhydric alcohols or sugars with maleic anhydride or succinic anhydride, oxycarboxylic acid and maleic anhydride Organic acid salts such as acids or condensates with succinic anhydride, CMOS, and Builder M. 6 Aluminosilicate. No. 1 Crystalline aluminosilicate x′(M′ ₂ O or M″O)・Al ₂ O ₃・y′(SiO ₂ )・
w′(H ₂ O) (In the formula, M′ is an alkali metal atom, M″ is an alkaline earth metal atom exchangeable with calcium, x′, y′, and w′ represent the number of moles of each component, and Specifically, 0.7≦x′≦1.5, 0.8≦y′≦
6, w' is any positive number. ) No. 2 As the detergent builder, those represented by the following general formula are particularly preferred. Na ₂ O・Al ₂ O ₃・nSiO ₂・wH ₂ O (Here, n represents a number from 1.8 to 3.0, and w represents a number from 1 to 6.) No. Amorphous aluminosilicate expressed by the cubic formula x (M ₂ O)・Al ₂ O ₃・y(SiO ₂ )・w(H ₂ O) (In the formula, M represents a sodium and/or potassium atom, and x, y, and w are within the following numerical range. It represents the number of moles of each component. 0.7≦x≦1.2 1.6≦y≦2.8 w is any positive number including 0) No. 4 Amorphous aluminosilicate x (M ₂ O )_{・ Al2O3}・Y( _SiO2 )・Z
(P ₂ O ₅ )・ω(H ₂ O) (In the formula, M is Na or K, X, Y, Z, ω
represents the number of moles of each component within the following numerical range. 0.20≦X≦1.10, 0.20≦Y≦4.00, 0.001≦Z≦0.80, any positive number including ω=0) [2] Alkaline agent or inorganic electrolyte In addition, various alkalis of the following as an alkaline agent or inorganic electrolyte The amount of one or more metal salts in the composition is 1 to 50% by weight, preferably 5 to 30% by weight.
% by weight. Silicates, carbonates, sulfates, and organic alkaline agents such as triethanolamine, diethanolamine, monoethanolamine, triisopropanolamine, etc. [3] 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-restaining agent. Polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone, carboxymethyl cellulose, etc. Among these, the combination of carboxymethyl cellulose or polyethylene glycol with the cellulase 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. [4] Bleaching agents Bleaching agents such as sodium percarbonate, sodium perborate, sodium sulfate hydrogen peroxide adduct, sodium chloride hydrogen peroxide adduct, and/or light bleaching agents such as sulfonated phthalocyanine zinc salt, aluminum salt, etc. The combined use of sensitive bleaching dyes and the like with the cellulase of the present invention further improves the cleaning effect. [5] Blue-tinging agent Various types of blue-tinging agents can be added as necessary. For example, the following structure is recommended: (In the formula, D represents a blue to purple monoazo/disazo or anthraquinone dye residue; Aliphatic amino group: An aromatic amino group or a cycloaliphatic amino group that may be substituted with a halogen atom, hydroxyl group, sulfonic acid group, carboxylic acid group, lower alkyl group, or lower alkoxy group.R is a hydrogen atom or a lower alkyl group.However, when R represents a hydrogen atom, and when X and Y simultaneously represent a hydroxyl group or an alkanolamino group, and when either one of X and Y is a hydroxyl group and the other is an alkanolamino group, (Except when n represents an integer of 2 or more.) (In the formula, D represents a blue to purple azo or anthraquinone dye residue, and X and Y represent the same or different alkanol amino residues or hydroxyl groups.) [6] Anti-caking agent In the case of powder detergent The following anti-caking agents can also be added. paratoluenesulfonate,
Xylene sulfonate, acetate, sulfosuccinic acid, talc, finely powdered silica, clay, calcium.
Silicates (such as Tohns Manvill's maleic acid microcells), calcium carbonate, magnesium oxide, etc. [7] An inhibitor of factors that inhibit cellulase activity. Cellulase activity may be inactivated in 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 [1], magnesium silicate, magnesium sulfate, and the like. Cellbiose, glucose and gluconolactone are also sometimes inhibitors. Try to make these types of saccharides and cellulases coexist as much as possible, or if coexistence cannot be avoided, take measures to avoid direct contact between these saccharides and cellulases, such as:
A method of coating each is required. 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 Although it depends on the type of cellulase, when proteins, cobalt and its salts, calcium and its salts, potassium and its salts, sodium and its salts, monosaccharides such as mannose and xylose are allowed to coexist,
Cellulase is activated and the cleaning effect is dramatically improved.

[9] Antioxidants Tert-butylated hydroxytoluene, 4,4'-butylidene bis-(6-tert-butyl-3-methylphenol), 2,2'-butylidene bis-(6-tert-butylidene bis-(6-tert-butyl-3-methylphenol)
butyl-4-methylphenol), monostyrenated cresol, distyrenated cresol, monostyrenated phenol, distyrenated phenol,
Antioxidants such as 1,1'-bis-(4-hydroxyphenyl)cyclohexane. [10] Solubilizers Lower alcohols such as ethanol, benzenesulfonates, lower alkylbenzenesulfonates such as p-toluenesulfonates, glycols such as propylene glycol, acetylbenzenesulfonates, acetamides, Solubilizing agents such as pyridine dicarboxylic acid amides, benzoates or urea. [11] Enzyme Hydrolytic enzymes other than cellulase can also be added.
Examples of such hydrolytic enzymes include the following. First, carboxylic acid ester hydrolase, thiol ester hydrolase, which act on ester bonds,
Phosphate monoester hydrolase, phosphodiester hydrolase, glycoxide hydrolase that acts on glycoxy compounds, enzyme that hydrolyzes N-glycosyl compounds, thioether and hydrolase that acts on ether bonds, α that acts on peptide bonds
-Amino-acyl-peptide hydrolase, peptidyl-amino acid hydrolase, acyl-amino acid hydrolase, dipeptide hydrolase, peptidyl-
Examples include peptide hydrolases, and carboxylic acid ester hydrolases, glycoside hydrolases, and peptidyl-peptide hydrolases are preferred. These suitable hydrolytic enzymes are further exemplified as follows. 1 Protease belonging to peptidyl-peptide hydrolase Examples suitable for the present invention include pepsin, pepsin B, rennin, trypsin, chymotrypsin A, chymotrypsin B, elastase, enterokinase, cathepsin C, papain, chymopapain, huicin, thrombin, fibrinolysin,
These include renin, subtilisin, aspergilopeptidase A, collagenase, clostridiopeptidase B, kallikrein, gastricin, cathepsin D, promelain, keratinase, chymotrypsin C, pepsin C, cocoonase, aspergilopeptidase B, urokinase, and the like. Other proteases include carboxypeptidases A and B and aminopeptidases. 2 Glycoside Hydrolases Cellulases are excluded from this group because they are other essential components. α-amylase, β-amylase, glucoamylase, invertase, lysozyme, pectinase, chitinase, dextranase, etc. are preferred, and amylases such as α-amylase and β-amylase are particularly preferred. These originally function in acidic to neutral systems, but among those obtained from bacteria, those that are highly active in alkaline conditions are also preferably used. 3. Carboxylic ester hydrolase Examples of carboxylic ester hydrolases suitable for the present invention include carboxyesterase, lipase, pectin esterase, chlorophyllase, etc., of which lipase is effective. Specific examples of commercially available enzyme products and their manufacturers include "Alcalase", "Esperase",
"Savinase", "AMG", "BAN", "Juangamil", "Sweetzyme", "Termamil" (Novo Industri, Copenhagen, Denmark), "Maxatase-P", "High Alkaline
Protease”, “Amylase THC”, “Lipase”
(Gist Brocades, Delft, Netherlands)
n.v.), “Protease B-400”, “Protease B-4000”, “Protease AP” and “Protease AP2100” (Silibeitzeritzsche Ferment A.G., Basel, Switzerland)
), “CRD-Protease” (Monsanto Company, St. Louis, Missouri, USA),
“Piocase” (Biovin Corporation, Monticello, Illinois, USA), “Pronase-P”, “Pronase-AS” and “Pronase-AF” (Kaken Kagaku, Japan), “Lapitase P-
2000' (Lapidus, Secran, France), a proteolytic enzyme product manufactured by Clinton Corn Products (Standard Brands, Daivisillon, New York) (100% passing through Tyler standard 16 mesh sieves to 100% passing through Tyler standard 150 mesh sieves) % residual particle size), ``Takamine'', ``Promelain 1:10'', ``HT Proteolytic Enzyme''
200'', ``Enzyme L-W'' (obtained from mold rather than bacteria) (Miles Chemical Company, Elkhart, Indiana, USA), ``Rozyme P-11 Concentrate'', ``Pectinol'', `` Lipase B”, “Rozyme PF”, “Rozyme J-25” (Philadelphia, USA,
Rohm & Haas), “Amprozyme”
200” (Jacques Wolf & Company, a subsidiary of Nobuco Chemical Company, Newark, New Jersey, USA),
"ATP40", "ATP120", "ATP160" (France,
Secran, Etsu Rapidaz) and ``Olipase'' (Nagase Sangyo, Japan). Hydrolytic enzymes other than cellulase are blended into the cleaning composition in the required amount depending on the purpose, but the amount is 0.001 to 5% by weight (preferably 0.02% 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, as a purified enzyme, 0.001 to 5
Crude enzyme or granules are used so that the amount is 0.002 to 10% by weight, for example, preferably
The purified enzyme is diluted to 0.1-5% by weight. 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. Next, the present invention will be specifically explained with reference to Examples. The percentages in the examples are by weight unless otherwise specified. In the following examples, the whitening effect of detergents was determined by the following experiment: [1] Washing conditions Clothing: 10 pieces of 100% cotton knitted underwear or 4 pieces of polyester/cotton blend Y shirts. However, all of them are unworn clothes. Washing method: Dissolve 20 c.c. for liquid detergent or 40 g for powder detergent in 5 parts tap water, initial temperature 40°C.
After 2 hours, add tap water at room temperature and wash for 10 minutes in a commercial washing machine equipped with an agitation pulsator. After washing, dehydrate in a dehydrator for 1 minute. Dehydrate clothing with 30 ml of tap water,
Rinse in the washing machine for 3 minutes. Therefore, after rinsing one more time, it is dehydrated for 1 minute and dried in an electric dryer. After repeating this washing cycle 50 times, the whiteness was evaluated. [2] Determination of whiteness Fluorescent agents used in laundry detergents generally have a wavelength of 380nm.
absorbs light and emits fluorescent light with maximum intensity between 430 and 440 nm. Therefore, when a xenon lamp is used as the irradiation light containing ultraviolet rays, the fluorescence intensity (whiteness) can be expressed by the Z value having the maximum stimulation value at 440 nm among the spectral tristimulus values X, Y, and Z. Therefore, the amount of fluorescent agent dyeing on clothing was determined by measuring the Z value using a xenon digital colorimeter (Suga Test Instruments Co., Ltd.). Example 1 Detergent formulation

【table】 Result

[Table] Examples and comparative examples showing that among various fluorescent dyes, the fluorescent dye used in the present invention is particularly preferable are listed below. The whitening effect of the detergent was determined by the following experiment. [1] Washing conditions Clothing: 10 pieces of 100% cotton knitted underwear Wearing and washing method: The above underwear was worn by an adult male in his 20s.
10 people wore the clothes for 24 hours, washed and dried them. The washing method is to dissolve 40g of detergent in 5 parts of tap water.
Clothes are soaked at an initial temperature of 40°C, and after 2 hours, tap water at room temperature is added and washed for 10 minutes in a practical washing machine with an agitation pulsator at 30 minutes. After washing, dehydrate in a dehydrator for 1 minute. Rinse the dehydrated clothes in the washing machine for 3 minutes in 30°C of tap water. Therefore, after rinsing one more time,
Dehydrate for 1 minute and air dry outdoors. After drying, the same subject wears it again for 24 hours, then washes and dries it repeatedly. After repeating this washing cycle 10 times, the whiteness was evaluated. [2] Judgment of whiteness Same as above. Example 2 Detergent formulation linear dodecylbenzenesulfonate sodium
20% by weight Tallow soap 2 Zeolite 20 Sodium silicate 10 Sodium carbonate 10 Carboxymethyl cellulose 1 Protease 0.5 (NOVO, Alcalase 1.5M) Glauber's salt Balanced fluorescent dye* ² 0.3% by weight Cellulase* ¹ 2.5 Water 10 (Note) *1 The microorganism deposit number is the microorganism deposit number.
Cellulase cultured and collected from bacteria belonging to the genus Aeromonas No. 2306. *2 Result

【table】

[Table] From the above, it can be seen that only when the fluorescent dye specified in the present invention is blended with a cellulase-containing detergent, the effect of suppressing the decrease in whiteness of clothing is large.

Claims (1)

[Scope of Claims] 1. 0.01 to 70% by weight of a cellulase having a maximum enzyme activity of 0.001 unit/mg solid content or more and an optimum pH of less than 8.0, and compounds (a) to (f) represented by the following formulas. A phosphorus-free detergent composition comprising: 0.01 to 5% by weight of a fluorescent dye selected from the group consisting of; one or more surfactants; and other detergent components. . (However, X represents [formula] and Y represents [formula]) (However, X represents [formula] and Y represents [formula]) (However, X represents [formula] and Y represents [formula])