MXPA98004657A - Enzymatic method for textile dyeing - Google Patents
Enzymatic method for textile dyeingInfo
- Publication number
- MXPA98004657A MXPA98004657A MXPA/A/1998/004657A MX9804657A MXPA98004657A MX PA98004657 A MXPA98004657 A MX PA98004657A MX 9804657 A MX9804657 A MX 9804657A MX PA98004657 A MXPA98004657 A MX PA98004657A
- Authority
- MX
- Mexico
- Prior art keywords
- mono
- enzyme
- activity
- wool
- aqueous solution
- Prior art date
Links
- 238000004043 dyeing Methods 0.000 title claims abstract description 41
- 239000004753 textile Substances 0.000 title description 9
- 230000002255 enzymatic Effects 0.000 title description 3
- 239000004744 fabric Substances 0.000 claims abstract description 75
- 239000000463 material Substances 0.000 claims abstract description 61
- -1 polycyclic aromatic Chemical class 0.000 claims abstract description 54
- 102000004190 Enzymes Human genes 0.000 claims abstract description 53
- 108090000790 Enzymes Proteins 0.000 claims abstract description 53
- 230000000694 effects Effects 0.000 claims abstract description 43
- MHAJPDPJQMAIIY-UHFFFAOYSA-N hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims abstract description 42
- 239000007864 aqueous solution Substances 0.000 claims abstract description 20
- 150000002390 heteroarenes Chemical class 0.000 claims abstract description 20
- 150000001491 aromatic compounds Chemical class 0.000 claims abstract description 8
- 239000000835 fiber Substances 0.000 claims abstract description 5
- 238000002791 soaking Methods 0.000 claims abstract description 5
- 210000002268 Wool Anatomy 0.000 claims description 47
- 108010029541 Laccase Proteins 0.000 claims description 45
- 229940088598 Enzyme Drugs 0.000 claims description 36
- 102000003992 Peroxidases Human genes 0.000 claims description 26
- 108090000437 Peroxidases Proteins 0.000 claims description 26
- 229940072417 Peroxidase Drugs 0.000 claims description 19
- 108020005203 Oxidases Proteins 0.000 claims description 15
- KJCVRFUGPWSIIH-UHFFFAOYSA-N 1-Naphthol Chemical compound C1=CC=C2C(O)=CC=CC2=C1 KJCVRFUGPWSIIH-UHFFFAOYSA-N 0.000 claims description 13
- CDAWCLOXVUBKRW-UHFFFAOYSA-N 2-Aminophenol Chemical compound NC1=CC=CC=C1O CDAWCLOXVUBKRW-UHFFFAOYSA-N 0.000 claims description 13
- 125000000217 alkyl group Chemical group 0.000 claims description 8
- 125000000524 functional group Chemical group 0.000 claims description 8
- 125000001424 substituent group Chemical group 0.000 claims description 8
- 210000003491 Skin Anatomy 0.000 claims description 7
- 102000031088 EC 1.10.3.1 Human genes 0.000 claims description 6
- 108010031396 EC 1.10.3.1 Proteins 0.000 claims description 6
- 125000003342 alkenyl group Chemical group 0.000 claims description 6
- 108010015428 bilirubin oxidase Proteins 0.000 claims description 6
- 125000000304 alkynyl group Chemical group 0.000 claims description 5
- 239000010985 leather Substances 0.000 claims description 5
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 claims description 5
- LSNNMFCWUKXFEE-UHFFFAOYSA-L Sulphite Chemical compound [O-]S([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-L 0.000 claims description 4
- 125000000751 azo group Chemical group [*]N=N[*] 0.000 claims description 4
- 210000004209 Hair Anatomy 0.000 claims description 3
- 229920003171 Poly (ethylene oxide) Polymers 0.000 claims description 3
- 125000003545 alkoxy group Chemical group 0.000 claims description 3
- 125000003282 alkyl amino group Chemical group 0.000 claims description 3
- 125000005277 alkyl imino group Chemical group 0.000 claims description 3
- 125000004390 alkyl sulfonyl group Chemical group 0.000 claims description 3
- 125000004414 alkyl thio group Chemical group 0.000 claims description 3
- 125000003368 amide group Chemical group 0.000 claims description 3
- 239000003945 anionic surfactant Substances 0.000 claims description 3
- 125000003917 carbamoyl group Chemical group [H]N([H])C(*)=O 0.000 claims description 3
- 239000003093 cationic surfactant Substances 0.000 claims description 3
- 239000003795 chemical substances by application Substances 0.000 claims description 3
- 125000004093 cyano group Chemical group *C#N 0.000 claims description 3
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 claims description 3
- 125000004997 halocarbonyl group Chemical group 0.000 claims description 3
- 229910052736 halogen Inorganic materials 0.000 claims description 3
- 150000002367 halogens Chemical class 0.000 claims description 3
- 125000004356 hydroxy functional group Chemical group O* 0.000 claims description 3
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 claims description 3
- 239000002736 nonionic surfactant Substances 0.000 claims description 3
- 125000005188 oxoalkyl group Chemical group 0.000 claims description 3
- 125000005740 oxycarbonyl group Chemical group [*:1]OC([*:2])=O 0.000 claims description 3
- NJRWNWYFPOFDFN-UHFFFAOYSA-L phosphonate(2-) Chemical compound [O-][P]([O-])=O NJRWNWYFPOFDFN-UHFFFAOYSA-L 0.000 claims description 3
- 125000005499 phosphonyl group Chemical group 0.000 claims description 3
- 229920000642 polymer Polymers 0.000 claims description 3
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 claims description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 claims description 3
- 239000004372 Polyvinyl alcohol Substances 0.000 claims description 2
- 150000004984 aromatic diamines Chemical class 0.000 claims description 2
- 229910001424 calcium ion Inorganic materials 0.000 claims description 2
- 125000001072 heteroaryl group Chemical group 0.000 claims description 2
- 150000002500 ions Chemical class 0.000 claims description 2
- 229910001425 magnesium ion Inorganic materials 0.000 claims description 2
- 108010064470 polyaspartate Proteins 0.000 claims description 2
- 125000003367 polycyclic group Chemical group 0.000 claims description 2
- 229920002451 polyvinyl alcohol Polymers 0.000 claims description 2
- 229920000036 polyvinylpyrrolidone Polymers 0.000 claims description 2
- 239000001267 polyvinylpyrrolidone Substances 0.000 claims description 2
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 claims description 2
- 229910001414 potassium ion Inorganic materials 0.000 claims description 2
- 229910001415 sodium ion Inorganic materials 0.000 claims description 2
- 108010061247 2-aminophenol oxidase Proteins 0.000 claims 1
- OZAIFHULBGXAKX-UHFFFAOYSA-N precursor Substances N#CC(C)(C)N=NC(C)(C)C#N OZAIFHULBGXAKX-UHFFFAOYSA-N 0.000 description 58
- 150000001875 compounds Chemical class 0.000 description 42
- 239000000243 solution Substances 0.000 description 40
- 241001313536 Thermothelomyces thermophila Species 0.000 description 34
- 108010078762 Protein Precursors Proteins 0.000 description 33
- 102000014961 Protein Precursors Human genes 0.000 description 33
- CBCKQZAAMUWICA-UHFFFAOYSA-N P-Phenylenediamine Chemical compound NC1=CC=C(N)C=C1 CBCKQZAAMUWICA-UHFFFAOYSA-N 0.000 description 28
- 235000017281 sodium acetate Nutrition 0.000 description 21
- 239000002253 acid Substances 0.000 description 19
- 239000007853 buffer solution Substances 0.000 description 16
- UIIMBOGNXHQVGW-UHFFFAOYSA-M buffer Substances [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 15
- 238000005406 washing Methods 0.000 description 15
- 239000000460 chlorine Substances 0.000 description 14
- 229940018564 M-PHENYLENEDIAMINE Drugs 0.000 description 13
- WZCQRUWWHSTZEM-UHFFFAOYSA-N M-Phenylenediamine Chemical compound NC1=CC=CC(N)=C1 WZCQRUWWHSTZEM-UHFFFAOYSA-N 0.000 description 13
- 238000000034 method Methods 0.000 description 13
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 13
- 239000000975 dye Substances 0.000 description 12
- UHOVQNZJYSORNB-UHFFFAOYSA-N benzene Chemical compound C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 10
- 239000008399 tap water Substances 0.000 description 9
- 235000020679 tap water Nutrition 0.000 description 9
- 241000222640 Polyporus Species 0.000 description 8
- 210000004027 cells Anatomy 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 7
- ZMXJAEGJWHJMGX-UHFFFAOYSA-N methyl syringate Chemical compound COC(=O)C1=CC(OC)=C(O)C(OC)=C1 ZMXJAEGJWHJMGX-UHFFFAOYSA-N 0.000 description 6
- 102000004316 Oxidoreductases Human genes 0.000 description 5
- 108090000854 Oxidoreductases Proteins 0.000 description 5
- 241000223255 Scytalidium Species 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 230000003647 oxidation Effects 0.000 description 5
- 238000007254 oxidation reaction Methods 0.000 description 5
- MYMOFIZGZYHOMD-UHFFFAOYSA-N oxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 5
- 150000002989 phenols Chemical class 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 241000228212 Aspergillus Species 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- 244000251987 Coprinus macrorhizus Species 0.000 description 4
- 235000001673 Coprinus macrorhizus Nutrition 0.000 description 4
- ILEDWLMCKZNDJK-UHFFFAOYSA-N Esculetin Chemical compound C1=CC(=O)OC2=C1C=C(O)C(O)=C2 ILEDWLMCKZNDJK-UHFFFAOYSA-N 0.000 description 4
- 241000233866 Fungi Species 0.000 description 4
- 229920001850 Nucleic acid sequence Polymers 0.000 description 4
- 239000006185 dispersion Substances 0.000 description 4
- 239000002609 media Substances 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 229910052757 nitrogen Inorganic materials 0.000 description 4
- 229910052760 oxygen Inorganic materials 0.000 description 4
- 239000001301 oxygen Substances 0.000 description 4
- 238000010186 staining Methods 0.000 description 4
- 239000004094 surface-active agent Substances 0.000 description 4
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 4
- JFGQHAHJWJBOPD-UHFFFAOYSA-N 3-hydroxy-N-phenylnaphthalene-2-carboxamide Chemical compound OC1=CC2=CC=CC=C2C=C1C(=O)NC1=CC=CC=C1 JFGQHAHJWJBOPD-UHFFFAOYSA-N 0.000 description 3
- 241000223198 Humicola Species 0.000 description 3
- 241000789035 Polyporus pinsitus Species 0.000 description 3
- 241000813090 Rhizoctonia solani Species 0.000 description 3
- 150000001408 amides Chemical class 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 150000002191 fatty alcohols Chemical class 0.000 description 3
- SIKJAQJRHWYJAI-UHFFFAOYSA-N indole Chemical compound C1=CC=C2NC=CC2=C1 SIKJAQJRHWYJAI-UHFFFAOYSA-N 0.000 description 3
- 238000007639 printing Methods 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 150000003871 sulfonates Chemical class 0.000 description 3
- GUEIZVNYDFNHJU-UHFFFAOYSA-N 1,4-Dihydroxyanthraquinone Chemical compound O=C1C2=CC=CC=C2C(=O)C2=C1C(O)=CC=C2O GUEIZVNYDFNHJU-UHFFFAOYSA-N 0.000 description 2
- OBCSAIDCZQSFQH-UHFFFAOYSA-N 2-methyl-1,4-phenylenediamine Chemical compound CC1=CC(N)=CC=C1N OBCSAIDCZQSFQH-UHFFFAOYSA-N 0.000 description 2
- MYNVJNZGTAVRJD-UHFFFAOYSA-N 4-[[2-[(3,5-dimethoxy-4-oxocyclohexa-2,5-dien-1-ylidene)methyl]hydrazinyl]methylidene]-2,6-dimethoxycyclohexa-2,5-dien-1-one Chemical compound C1=C(OC)C(=O)C(OC)=CC1=CNNC=C1C=C(OC)C(=O)C(OC)=C1 MYNVJNZGTAVRJD-UHFFFAOYSA-N 0.000 description 2
- HBZVNWNSRNTWPS-UHFFFAOYSA-N 6-amino-4-hydroxynaphthalene-2-sulfonic acid Chemical compound C1=C(S(O)(=O)=O)C=C(O)C2=CC(N)=CC=C21 HBZVNWNSRNTWPS-UHFFFAOYSA-N 0.000 description 2
- RGCKGOZRHPZPFP-UHFFFAOYSA-N Alizarin Natural products C1=CC=C2C(=O)C3=C(O)C(O)=CC=C3C(=O)C2=C1 RGCKGOZRHPZPFP-UHFFFAOYSA-N 0.000 description 2
- 241000222211 Arthromyces Species 0.000 description 2
- UJOBWOGCFQCDNV-UHFFFAOYSA-N Carbazole Chemical compound C1=CC=C2C3=CC=CC=C3NC2=C1 UJOBWOGCFQCDNV-UHFFFAOYSA-N 0.000 description 2
- HLVXFWDLRHCZEI-UHFFFAOYSA-N Chromotropic acid Chemical compound OS(=O)(=O)C1=CC(O)=C2C(O)=CC(S(O)(=O)=O)=CC2=C1 HLVXFWDLRHCZEI-UHFFFAOYSA-N 0.000 description 2
- 229920000742 Cotton Polymers 0.000 description 2
- 241000580475 Embellisia Species 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 241001480714 Humicola insolens Species 0.000 description 2
- RAXXELZNTBOGNW-UHFFFAOYSA-N Imidazole Chemical compound C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 2
- 241000223251 Myrothecium Species 0.000 description 2
- ZQPPMHVWECSIRJ-KTKRTIGZSA-N Oleic acid Chemical compound CCCCCCCC\C=C/CCCCCCCC(O)=O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 2
- WQGWDDDVZFFDIG-UHFFFAOYSA-N Pyrogallol Chemical compound OC1=CC=CC(O)=C1O WQGWDDDVZFFDIG-UHFFFAOYSA-N 0.000 description 2
- 241001361634 Rhizoctonia Species 0.000 description 2
- 229910000831 Steel Inorganic materials 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- 241000222354 Trametes Species 0.000 description 2
- 241000223259 Trichoderma Species 0.000 description 2
- 241000082085 Verticillium <Phyllachorales> Species 0.000 description 2
- HFVAFDPGUJEFBQ-UHFFFAOYSA-M alizarin red S Chemical compound [Na+].O=C1C2=CC=CC=C2C(=O)C2=C1C=C(S([O-])(=O)=O)C(O)=C2O HFVAFDPGUJEFBQ-UHFFFAOYSA-M 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- QIGBRXMKCJKVMJ-UHFFFAOYSA-N benzohydroquinone Chemical compound OC1=CC=C(O)C=C1 QIGBRXMKCJKVMJ-UHFFFAOYSA-N 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 150000007942 carboxylates Chemical class 0.000 description 2
- 229910052801 chlorine Inorganic materials 0.000 description 2
- 239000003086 colorant Substances 0.000 description 2
- 238000009833 condensation Methods 0.000 description 2
- 230000005494 condensation Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- RYGMFSIKBFXOCR-UHFFFAOYSA-N copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 2
- 229910052802 copper Inorganic materials 0.000 description 2
- 239000010949 copper Substances 0.000 description 2
- 229920003013 deoxyribonucleic acid Polymers 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
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- 230000002538 fungal Effects 0.000 description 2
- 150000002334 glycols Chemical class 0.000 description 2
- 239000001963 growth media Substances 0.000 description 2
- 238000005470 impregnation Methods 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- UFWIBTONFRDIAS-UHFFFAOYSA-N naphthalene Chemical compound C1=CC=CC2=CC=CC=C21 UFWIBTONFRDIAS-UHFFFAOYSA-N 0.000 description 2
- 230000003287 optical Effects 0.000 description 2
- IAYPIBMASNFSPL-UHFFFAOYSA-N oxane Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 229920000768 polyamine Polymers 0.000 description 2
- 210000001938 protoplasts Anatomy 0.000 description 2
- JUJWROOIHBZHMG-UHFFFAOYSA-N pyridine Chemical compound C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 2
- 239000010959 steel Substances 0.000 description 2
- 238000010998 test method Methods 0.000 description 2
- 230000001131 transforming Effects 0.000 description 2
- SQAINHDHICKHLX-UHFFFAOYSA-N 1-naphthaldehyde Chemical compound C1=CC=C2C(C=O)=CC=CC2=C1 SQAINHDHICKHLX-UHFFFAOYSA-N 0.000 description 1
- BAXOFTOLAUCFNW-UHFFFAOYSA-N 1H-indazole Chemical compound C1=CC=C2C=NNC2=C1 BAXOFTOLAUCFNW-UHFFFAOYSA-N 0.000 description 1
- GIGNQZIJYUEWTI-UHFFFAOYSA-N 2,3,5-trihydroxytoluene Chemical compound CC1=CC(O)=CC(O)=C1O GIGNQZIJYUEWTI-UHFFFAOYSA-N 0.000 description 1
- WOHLSTOWRAOMSG-UHFFFAOYSA-N 2,3-dihydro-1,3-benzothiazole Chemical compound C1=CC=C2SCNC2=C1 WOHLSTOWRAOMSG-UHFFFAOYSA-N 0.000 description 1
- BAHPQISAXRFLCL-UHFFFAOYSA-N 2,4-Diaminoanisole Chemical compound COC1=CC=C(N)C=C1N BAHPQISAXRFLCL-UHFFFAOYSA-N 0.000 description 1
- VOZKAJLKRJDJLL-UHFFFAOYSA-N 2,4-Diaminotoluene Chemical compound CC1=CC=C(N)C=C1N VOZKAJLKRJDJLL-UHFFFAOYSA-N 0.000 description 1
- 229940075142 2,5-diaminotoluene Drugs 0.000 description 1
- RLYCRLGLCUXUPO-UHFFFAOYSA-N 2,6-diaminotoluene Chemical compound CC1=C(N)C=CC=C1N RLYCRLGLCUXUPO-UHFFFAOYSA-N 0.000 description 1
- SUZRRICLUFMAQD-UHFFFAOYSA-N 2-(methylamino)ethanesulfonic acid Chemical compound CNCCS(O)(=O)=O SUZRRICLUFMAQD-UHFFFAOYSA-N 0.000 description 1
- LJCNDNBULVLKSG-UHFFFAOYSA-N 2-aminoacetic acid;butane Chemical compound CCCC.CCCC.NCC(O)=O LJCNDNBULVLKSG-UHFFFAOYSA-N 0.000 description 1
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- ULUAUXLGCMPNKK-UHFFFAOYSA-L 2-sulfobutanedioate Chemical class OS(=O)(=O)C(C([O-])=O)CC([O-])=O ULUAUXLGCMPNKK-UHFFFAOYSA-L 0.000 description 1
- CZPWVGJYEJSRLH-UHFFFAOYSA-N 289-95-2 Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
- WVWZURUEPRJFAE-UHFFFAOYSA-N 3,4-diethoxyaniline;2-methoxybenzene-1,4-diamine Chemical compound COC1=CC(N)=CC=C1N.CCOC1=CC=C(N)C=C1OCC WVWZURUEPRJFAE-UHFFFAOYSA-N 0.000 description 1
- FLROJJGKUKLCAE-UHFFFAOYSA-N 3-amino-2-methylphenol Chemical compound CC1=C(N)C=CC=C1O FLROJJGKUKLCAE-UHFFFAOYSA-N 0.000 description 1
- ZTOJFFHGPLIVKC-UHFFFAOYSA-L 3-ethyl-2-[(3-ethyl-6-sulfonato-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonate Chemical compound S1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C1=NN=C1SC2=CC(S([O-])(=O)=O)=CC=C2N1CC ZTOJFFHGPLIVKC-UHFFFAOYSA-L 0.000 description 1
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- YZJSKRBKHCLMQC-UHFFFAOYSA-N 3-hydroxy-N-(3-nitrophenyl)naphthalene-2-carboxamide Chemical compound OC1=CC2=CC=CC=C2C=C1C(=O)NC1=CC=CC([N+]([O-])=O)=C1 YZJSKRBKHCLMQC-UHFFFAOYSA-N 0.000 description 1
- ALYNCZNDIQEVRV-UHFFFAOYSA-N 4-Aminobenzoic acid Chemical compound NC1=CC=C(C(O)=O)C=C1 ALYNCZNDIQEVRV-UHFFFAOYSA-N 0.000 description 1
- ZFRBZRZEKIOGQI-UHFFFAOYSA-N 4-amino-5-hydroxynaphthalene-1,3-disulfonic acid Chemical compound C1=CC(O)=C2C(N)=C(S(O)(=O)=O)C=C(S(O)(=O)=O)C2=C1 ZFRBZRZEKIOGQI-UHFFFAOYSA-N 0.000 description 1
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- GZFGOTFRPZRKDS-UHFFFAOYSA-N 4-bromophenol Chemical compound OC1=CC=C(Br)C=C1 GZFGOTFRPZRKDS-UHFFFAOYSA-N 0.000 description 1
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- VXIXUWQIVKSKSA-UHFFFAOYSA-N 4-hydroxycoumarin Chemical compound C1=CC=CC2=C1OC(=O)C=C2O VXIXUWQIVKSKSA-UHFFFAOYSA-N 0.000 description 1
- ZFIQGRISGKSVAG-UHFFFAOYSA-N 4-methylaminophenol Chemical compound CNC1=CC=C(O)C=C1 ZFIQGRISGKSVAG-UHFFFAOYSA-N 0.000 description 1
- 229940044174 4-phenylenediamine Drugs 0.000 description 1
- KYARBIJYVGJZLB-UHFFFAOYSA-N 7-amino-4-hydroxy-2-naphthalenesulfonic acid Chemical compound OC1=CC(S(O)(=O)=O)=CC2=CC(N)=CC=C21 KYARBIJYVGJZLB-UHFFFAOYSA-N 0.000 description 1
- PAJJWOCZRXFBJD-UHFFFAOYSA-N 8-amino-1-hydroxynaphthalene-2,6-disulfonic acid Chemical compound C1=C(S(O)(=O)=O)C(O)=C2C(N)=CC(S(O)(=O)=O)=CC2=C1 PAJJWOCZRXFBJD-UHFFFAOYSA-N 0.000 description 1
- GGZZISOUXJHYOY-UHFFFAOYSA-N 8-amino-4-hydroxynaphthalene-2-sulfonic acid Chemical compound C1=C(S(O)(=O)=O)C=C2C(N)=CC=CC2=C1O GGZZISOUXJHYOY-UHFFFAOYSA-N 0.000 description 1
- CYJJLCDCWVZEDZ-UHFFFAOYSA-N 8-aminonaphthalene-1-sulfonic acid Chemical compound C1=CC(S(O)(=O)=O)=C2C(N)=CC=CC2=C1 CYJJLCDCWVZEDZ-UHFFFAOYSA-N 0.000 description 1
- ZTOJFFHGPLIVKC-CLFAGFIQSA-N ABTS Chemical compound S/1C2=CC(S(O)(=O)=O)=CC=C2N(CC)C\1=N\N=C1/SC2=CC(S(O)(=O)=O)=CC=C2N1CC ZTOJFFHGPLIVKC-CLFAGFIQSA-N 0.000 description 1
- 238000010269 ABTS assay Methods 0.000 description 1
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- VQOIVBPFDDLTSX-UHFFFAOYSA-M sodium;3-dodecylbenzenesulfonate Chemical class [Na+].CCCCCCCCCCCCC1=CC=CC(S([O-])(=O)=O)=C1 VQOIVBPFDDLTSX-UHFFFAOYSA-M 0.000 description 1
- GGHPAKFFUZUEKL-UHFFFAOYSA-M sodium;hexadecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCCCOS([O-])(=O)=O GGHPAKFFUZUEKL-UHFFFAOYSA-M 0.000 description 1
- NWZBFJYXRGSRGD-UHFFFAOYSA-M sodium;octadecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCCCCCOS([O-])(=O)=O NWZBFJYXRGSRGD-UHFFFAOYSA-M 0.000 description 1
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 125000000472 sulfonyl group Chemical group *S(*)(=O)=O 0.000 description 1
- 239000000988 sulfur dye Substances 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- YTPLMLYBLZKORZ-UHFFFAOYSA-N thiophene Chemical compound C=1C=CSC=1 YTPLMLYBLZKORZ-UHFFFAOYSA-N 0.000 description 1
- YXFVVABEGXRONW-UHFFFAOYSA-N toluene Substances CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 108020003112 toxins Proteins 0.000 description 1
- BSUNTQCMCCQSQH-UHFFFAOYSA-N triazine Chemical compound C1=CN=NN=C1.C1=CN=NN=C1 BSUNTQCMCCQSQH-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229940005267 urate oxidase Drugs 0.000 description 1
- 239000011364 vaporized material Substances 0.000 description 1
- 239000000984 vat dye Substances 0.000 description 1
Abstract
The present invention relates to methods for dyeing a material, comprising (a) soaking the material in an aqueous solution comprising one or more mono-, di- or polycyclic aromatic or heteroaromatic compounds, and (b) treating the material soaked in an aqueous solution with (i) a source of hydrogen peroxide and an enzyme showing perosidase activity or (ii) an enzyme showing oxidasase activity on one or more aromatic or heteroaromatic compounds, wherein the material is a fabric , filament, fiber, clothing or film made of fur, fur, silk or
Description
ENZYMATIC METHOD FOR TEXTILE DYEING
Field of the Invention The present invention relates to methods for dyeing a material, comprising (a) soaking the material in an aqueous solution comprising one or more mono-, di- or polycyclic aromatic or heteroaromatic compounds, and (b) ) treating the soaked material in an aqueous solution with (i) a source of hydrogen peroxide and an enzyme showing peroxidase activity or (ii) an enzyme showing oxidases activity on one or more aromatic or heteroaromatic compounds; wherein the material is a fabric, filament, fiber, garment or film made of fur, leather, fur, silk or wool.
BACKGROUND OF THE INVENTION Textile dyeing is often considered as the most important and expensive simple stage in the manufacture of textile fabrics and garments. In the textile industry, two main types of processes are currently used for dyeing, that is, intermittent and continuous. In the interim process among others, propellers, drums and teddo in Cuba are used. In the continuous processes among others, they are. impregnation systems
REF: 27501 per mordant. See, eg, I.D. Rattee, in C.M. Carr (De.), "The Chemistry of the Textile Industry", Blackie Academic and Professional, Glasgow, 1995, p. 276
The main classes of dyes are azo (mono-, di-, tri-, etc.), carbonyl (derivatives of anthraquinone and indigo), cyanine, di- and triphenylmethane and phthalocyanine. All these dyes contain chromophoric groups that give rise to color. There are three types of dyes that involve an oxidation / reduction mechanism, that is, vat, sulfur and azo dyes. The purpose of the oxidation / reduction step in these dyes is to change the dye between a soluble and insoluble form.
Oxidoreductases, e.g., oxidases and peroxidases, are well known in the art.
One class of oxidoreductases are the laccases (benzenediol oxidoreductases: oxygen) which are multicobber-containing enzymes, which catalyze the oxidation of phenols and related compounds. Laccase-mediated oxidation results in the production of aromatic radical intermediates from appropriate substrates; the final coupling of the intermediates thus produced provides a combination of dimeric, polymeric and oligomeric reaction products. Such reactions are important in nature in the biosynthetic trajectories that lead to the formation of melanin, alkaloids, toxins, lignins and humic acids.
Another class of oxidoreductases are peroxidases that oxidize compounds in the presence of hydrogen peroxide.
The laccases have been found useful for dyeing hair. See, eg, PCT applications series PCT / US95 / 06815 and PCT / US95 / 06816. European Patent No. 0504005, discloses that laccases can be used to dye wool at a pH in the range between 6.5 and 8.0.
Saunders et al., Peroxidase, London, 1964, p. 10 ff., Describes that peroxidases act on various amino and phenolic compounds that result in the production of a color.
Japanese Patent Application Publication No. 6-316874 discloses a method for dyeing cotton, which comprises treating the cotton with an oxygen-containing medium, wherein an oxidation reduction enzyme is selected from the group consisting of Ascorbate, bilirubin oxidase, catalase, laccase, peroxidase and polyphenol oxidase, is used to generate oxygen.
WO 91/05839 discloses that oxidases and peroxidases are useful for inhibiting the transfer of textile dyes.
It is an object of the present invention to provide an enzymatic method for dyeing fabrics.
Brief Description of the Invention The present invention relates to methods for dyeing a material, comprising (a) soaking the material in an aqueous solution comprising one or more polycyclic or heteroaromatic mono-, di-, or aromatic compounds, each one of which is optionally substituted with one or more functional groups or substituents, wherein each functional group or substituent is selected from the group consisting of halogen; sulfo; sulfonate; sulfamino; Sulfanyl; Not me; amido; nitro; azo; imino carboxy; cyano; formyl; hydroxy; halocarbonyl; carbamoyl; carbamidoyl; phosphonate; phosphonyl; C? -i8 alkenyl C? _? 8 alkyl, C? _ 8 alkynyl; Alkoxy C? _? S; Ci-iß oxycarbonyl; oxoalkyl Ci-iß; alkyl sulfanyl C? _18;
Ci-iß alkyl sulfonyl; alkyl imino or amino C? _? 8 which is substituted with one, two or three C? _? 8 alkyl groups; and (b) treating the material soaked in an aqueous solution with (i) a source of hydrogen peroxide and an enzyme showing peroxidase activity or (ii) an enzyme showing oxidases activity on one or more aromatic or heteroaromatic compounds; wherein the material is a fabric, filament, fiber, garment or film made of fur, leather, fur, silk or wool.
Detailed description of the invention. The use of oxidoreductases for dyeing materials has several important advantages. For example, the dyeing system used in the process of the present invention uses inexpensive color precursors. Moreover, moderate conditions in the process will result in less damage to the fabric.
The methods of the present invention can be used to dye materials such as fabrics, filaments, garments and films. Preferably, the material is made of hair skin. In another preferred embodiment, the material is made of leather. In another preferred embodiment, the material is made of skin. In another preferred embodiment, the material is made of silk. In another preferred embodiment, the material is made of wool.
In the methods of the present invention, the material is soaked in an aqueous solution comprising one or more mono-, di-, or polycyclic aromatic or heteroaromatic compounds, each of which is optionally substituted with one or more functional groups or substituents , wherein each functional group or substituent is selected from the group consisting of halogen; sulfo; sulfonate; sulfamino; Sulfanyl; Not me; amido; nitro; azo; imino carboxy; cyano; formyl; hydroxy; halocarbonyl; carbamoyl; carbamidoyl; phosphonate; phosphonyl; C? _? 8 alkyl, C? _ 8 alkenyl, C? _ 8 alkynyl; C 1 - 8 alkoxy; oxycarbonyl C? -? S; Cdia oxoalkyl; alkyl sulfanyl C? -? 8; alkyl sulfonyl Ci-is; alkyl imino or amino C? _? 8 which is substituted with one, two or three C? -? 8 alkyl groups. All C alquilo-β8 alkyl, C? _? 8 alkenyl and C? _? 8 alkynyl groups can be mono-, di- or poly-substituted by any of the appropriate functional groups or substituents. A polycyclic compound for the purposes of the present invention has 2, 3 or 4 aromatic rings. Examples of such mono-, di-, or polycyclic aromatic or heteroaromatic compounds include, but are not limited to, acridine, anthracene, azulene, benzene, benzofuran, benzothiazole, benzothiazoline, carboline, carbazole, cinnoline, chroman, chromene, chrysene, fulvene , furan, imidazole, indazole, indene, indole, indoline, indolizine, isothiazole, isoquinoline, isoxazole, naphthalene, naphthylene, naphthylpyridine, oxazole, perylene, phenanthrene, phenazine, phtalizine, pteridine, purine, pyrano, pyrazole, pyrene, pyridazine, pyridazone , pyridine, pyrimidine, pyrrole, quinazoline, quinoline, quinoxaline, sulfonyl, thiophene and triazine, each of which is optionally substituted. Examples of such compounds include, but are not limited to, aromatic diamines, aminophenols, phenols and naphthols.
Examples of the aromatic and heteroaromatic compounds for use in the present invention include, but are not limited to:
3, 4-diethoxyaniline 2-methoxy-p-phenylenediamine 1-amino-4-b-methoxyethylamino-benzene (Nb-methoxyethyl p-phenylenediamine) l-amino-4-bis- (b-hydroxyethyl) -aminobenzene (N, N -bis (b-hydroxyethyl) -p-phenylenediamine), 2-methyl-l, 3-diamino-benzene (2,6-diaminotoluene), 2,4-diaminotoluene, 2,6-diaminopyridine, l-amino-4- sulfonate-benzene, 1-N-methylsulfonate-4-aminobenzene, l-methyl-2-hydroxy-4-amino-benzene (3-amino o-cresol), l-methyl-2-hydroxy-4-b-hydroxyethylamino- benzene (2-hydroxy-4-b-hydroxyethylamino-toluene), l-hydroxy-4-methylamino-benzene (p-methylaminophenol), l-methoxy-2,4-diamino-benzene (2,4-diaminoanisole), l -ethoxy-2, 3-diamino-benzene (2,4-diaminophenethol), 1-b-hydroxyethyloxy-2,4-diamino-benzene (2), 4-diaminophenoxyethanol), 1,3-dihydroxy-2-methylbenzene (2-methyl resorcinol), 1,2,4-trihydroxybenzene, 1,2,4-trihydroxy-5-methylbenzene (2,4,5-trihydroxytoluene) , 2,3,5-trihydroxytoluene, 4,8-disulfonate-1-naphthol, 3-sulfonate-6-amino-1-naphthol (J acid), 6,8-disulfonate-2-naphthol, 1-phenylenediamine 2 , 5-diaminotoluene 2-Chloro-l, 4-phenylenediamine 2-Aminophenol 3-aminophenol 4-aminophenol 1,3-phenylenediamine 1-Naphthol 2-Naphthol 4-Chlororesorcinol 1,2,3-benzenetriol (Pyrogallol; 1, 3-Benzenediol (Resorcinol) 1,2-Benzenediol (Pyrocatechol) 2-Hydroxy-cinnamic acid 3-Hydroxy-cinnamic acid 4-Hydroxy-cinnamic acid 2,3-diaminobenzoic acid 2,4-diaminobenzoic acid 3, 4-diaminobenzoic acid -diaminobenzoic acid 3, 5-diaminobenzoic acid Methyl 2, 3-diaminobenzoate Ethyl 2, 3-diaminobenzoate Isopropyl 2, 3-diaminobenzoate Methyl 2, 4-diaminobenzoate Ethyl 2, 4-diaminobenzoate Isopropyl 2,4-diaminobenzoate Methyl 3, 4-diaminobenzoate Ethyl 3, 4-diaminobenzoate Isopropyl 3, 4-diaminobenzoate Methyl 3, 5-diaminobenzoate Ethyl 3, 5-diaminobenzoate Isopropyl 3, 5-diaminobenzoate N, N-dimethyl-3, 4-diaminobenzoic acid amide N, N acid amide -diethyl-3, 4-diaminobenzoic acid N, N-dipropyl-3, 4-diaminobenzoic acid amide N, N-dibutyl-3,4-diaminobenzoic acid amide 4-chloro-1-naphthol N-phenyl-p-phenylenediamine 3, 4-Dihydroxybenzaldehyde Pyrrol-pyrrol-2-isoimidazole 1,2,3-Triazole Benzotriazole Benzimidazole Imidazole Indole l-amino-8-hydroxynaphthalene-4-sulfone acid ico (S acid)
4, 5-Dihydroxynaphthalene-2,7-disulfonic acid (Chromotropic acid) Anthranilic acid 4-Aminobenzoic acid (PABA) 2-Amino-8-naphthol-6-sulfonic acid (Gamma acid) 5-Amino-l-naphthol- 3-sulfonic acid (M acid) 2-Naphthol-3,6-disulfonic acid (R acid) l-Amino-8-naphthol-2,4-disulfonic acid (Chicago acid) 1-Naphthol-4-sulfonic acid (Neville acid) -winther) Acid Peri Acid N-Benzoyl J Acid N-phenyl J-acid 1,7-Cleves Acid 1,6-Cleves Acid Bon Naphthol AS Dispersion black 9 Naphthol AS OL Naphthol AS PF Naphthol AS KB Naphthol AS BS Naphthol AS D Naphthol AS Bl Mordente Black 3 Cl 14640 (Black Blue Eirochrome B)
4-Amino-5-hydroxy-2,6-naphthalene disulfonic acid (acid H) Coffee Fat RR Solvent Coffee 1 (Cl 11285) Hydroquinone Mandelic Acid Melamine o-Nitrobenzaldehyde 1,5-Dihydroxynaphthalene 2,6-Dihydroxynaphthalene 2, 3- Dihydroxynaphthalene Benzylimidazole 2,3-Diaminonaphthalene 1,5-Diaminonaphthalene 1,8-diaminonaphthalene Salicylic acid 3-aminosalicylic acid 4-aminosalicylic acid 5-aminosalicylic acid Methyl-3-aminosalicylate Methyl-4-aminosalicylate Methyl-5-aminosalicylate Ethyl-3 Aminosalicylate Ethyl-4-aminosalicylate Ethyl-5-aminosalicylate Propi1-3-aminosalicylate Propyl-4-aminosalicylate Propyl-5-aminosalicylate Amide Salicylic 4-Aminothiophenol 4-Hydroxythiophenol Aniline Sulfate 4,4 '-Diaminodiphenylamine 4-Phenylazoaniline 4-Nitroaniline N , N-dimethyl-1, 4-phenylenediamine N, -diethyl-1,4-phenylenediamine Dispersion Orange 3 Dispersion Yellow 9 Dispersion Blue 1 N-Phenyl-1,2-phenylenediamine 6-Amino-2-naphthol 3-Amino-2 -naphthol 5-Amino-l-naphthol 1, 2-Phenylenediamine 2-Aminopyrimidine 4-Aminoquinaldine 2-Nitroaniline 3-Nitroaniline 2-Chloroaniline 3-Chloroaniline 4-Chloroaniline 4- (phenylazo) resorcinol (Orange Sudan G, Cl 11920) Red Sudan B, Cl 26110 Red Sudan 7B, Cl 26050 4'-aminoacetanilide Alizarin 1-Anthramin (1-aminoanthracene) 1-Aminoanthraquinone Anthraquinone 2,6-Dihydroxyanthraquinone (anthraflavic acid) 1,5-Dihydroxyanthraquinone (antrarufin) 3-Amidopyridine (Nicotinamide) Pyridine-3-carboxylic acid (acid nicotinic) Yellow Mordent 1, Yellow Alizarin GG, Cl 14025 Gray Coomassie, Black Acid 48, Cl 65005 Black Fast Palantine WAN, Black Acid 52, Cl 15711 Black Chromium Palantine 6BN, Cl 157, Black Blue Eriochrome R Black Mordant 11 , Black Eriochrome T Naphthol blue black, Black Acid 1, Cl 20470 1, 4-dihydroxyanthraquinone (Quinizarin) 4-Hydroxycoumarin Umbelliferone, 7-hydroxycoumarin Esculetin 6, 7-Dihydroxycoumarin Cromotrope Cumarin 2B Red Acid 176, Cl 1657 Cro motropo 2R Red Acid 29, Cl 16570 Chromotrope FB Red Acid 14, Cl 14720 Acid 2, 6-dihydroxiisonicotinic acid, citracinic acid
2, 5-Dichloroaniline 2-Amino-4-chlorotoluene 2-Nitro-4-chloroaniline 2-Methoxy-4-nitroaniline and p-Bromophenol.
After soaking the material in an aqueous solution, with one or more of the mono-, di- or polycyclic aromatic or heteroaromatic compounds, the material is treated in an aqueous solution with a source of hydrogen peroxide and an enzyme showing activity of peroxidase or an enzyme showing oxidase activity on one or more of the aromatic or heteroaromatic compounds. In a preferred embodiment, the same aqueous solution is used to soak and stain the material. The aqueous solution, that is, the dyeing liquor, used to dye the material in the methods of the present invention, may have a water / material ratio in the range of from about 0.5: 1 to about 200: 1, preferably around 5: 1 to around 20: 1.
In the methods of the present invention, the one or more mono-, di- or polycyclic aromatic or heteroaromatic compounds can be oxidized by (a) a source of hydrogen peroxide and an enzyme showing peroxidase activity or (b) an enzyme which shows an activity of oxidases on one or more mono-, di- or polycyclic aromatic or heteroaromatic compounds, eg, phenols and related substances. Enzymes showing peroxidase activity include, but are not limited to, peroxidase (EC 1.11.1.7) and haloperoxidase, eg, chloro- (EC 1.11.1.10), bromo- (EC 1.11.1) and iodoperoxidase (EC 1.11.1.8). Enzymes exhibiting oxidase activity include but are not limited to, bilirubin oxidase (EC 1.3.3.5), catechol oxidase (EC 1.10.3.1), laccase (EC 1.10.3.2), or oesophenol oxidase (EC 1.10. 3.4), and polyphenol oxidase (EC 1.10.3.2). Assays to determine the activity of these enzymes are well known to persons of ordinary skill in the art.
Preferably, the enzyme is a laccase obtained from a genus selected from the group consisting of Aspergillus, Botrytis, Collybia, Fom.es, Lentinus,
Myceliophthora, Neurospora, Pleurotus, Podospora, Polyporus, Scytalidium, Trametes, and Rhizoctonia. In a preferred embodiment, the laccase is obtained from species selected from the group consisting of Humicola brevis var, thermoidea, Humicola brevispora, Humicola grisea var. thermoidea, Humicola insolens, Humicola lanuginosa and (also known as Thermomyces lanuginosus), Myceliophthora thermophila, Myceliophthora vellerea, Polyporus pinsi your, Scytalidum thermophila, Scytalidium indonesiacum, Torula thermophila and. The laccase can be obtained from other species of Scytalidium, such as Scytalidium acidophilum, Scytalidium album,
Scytalidium aurantiacum, Scytalidium circinatum,
Scytalidium flaveobrunneum. , Scytalidium hyalinum,
Scytalidium lignicola, and Scytalidium uredinicolum. Laccase may be obtained from other species of Polyporus, such as Polyporus area your, Polyporus alveolaris, Polyporus arcularius, australiensis Polyporus, Polyporus badius Polyporus biformis, Polyporus brumalis, Polyporus ciliatus, Polyporus colensoi, Polyporus eucalyptorum, Polyporus meridionalis, Polyporus varius , Polyporus pal ustris, Polyporus rhizophilus, Polyporus rugulosus, Polyporus squamosus, Polyporus tuberaster, and Polyporus tumulosus. The laccase can also be obtained from a species of Rhizoctonia, p. ex. , Rhizoctonia solani. The laccase may also be a laccase modified by at least one amino acid residue in a type I (TI) copper site, wherein the modified oxidase has an altered pH and / or a specific activity relative to the wild type oxidase. . For example, the modified laccase can be modified in segment (a) of the TI copper site.
The peroxidases that can be employed for the present purpose can be isolated from and are produced by plants (eg, horseradish peroxidase) or microorganisms such as fungi or bacteria. Some preferred fungi include strains belonging to the subdivision Deuteromycotina class Hyphomycetes, eg, Fusarium, Humicola, Trichoderma, Myrothecium,
Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii, Myrothecium verrucana (IFO 61113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754 ), Caldariomyces fumago, Ulocladium chartarum, Embellisia alli or Dreschlera halodes.
Other preferred fungi include strains belonging to the subdivision Basidiomycotina Basidiomycetes, eg Coprinus, Phanerochaete, Coriolus or Trametes, Coprinus cinereus f particular. Microsporus (IFO 8371), coprinus macrorhizus, Phanerochaete chrysosporium (e.g., (NA-12) or Coliolus versicolor (e.g., PR4 28-A).
The most preferred fungi include strains belonging to the subdivision Zygomycotina, class Mycoraceae, eg, Rhizopus or Mucor, in particular Mucor hiemalis.
Some preferred bacteria include strains of the order Actinomycetales, eg Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. Verticillium
Other preferred bacteria include Bacillus pumillus (ATCC 12905), Bacillus stearothermophilus, Rhodobacter sphaeroides, Rhodomonas palustri, Streptococcus lactis, Pseudomonas purrocina (ATCC 15958) or Pseudomonas fluorescens (NRRL B-ll).
Other potential sources of peroxidases are listed in B.C. Saunders et al., Op. Cit., Pp. 41-43.
Methods for the production of enzymes to be used according to the invention are described in the art, e.g., FEBS LETTERS 1625, 173 (1) Applied and Environmental Microbiology, Feb. 1985, pp, 273-278, Applied Microbiol. Biotechnol. 26, 1987, pp. 158-163, Biotechnology Letters 9 (5), 1987, pp. 357-360, Nature 326, April 2, 1987, FEBS Letters 4270, 209 (2), p. 321, EP 179 486, EP 200 565, GB 2 167 421, EP 171 074, and Agrie. Biol. Chem.50 (1), 1986, p. Particularly preferred enzymes are those that are active at a pH in the range of from about 2.5 to about 12, preferably in the range of from about 4 to about 10, more preferably in the range of about 4.0 to about of 7.0 and in the range of around 7.0 to around 10.0. Such enzymes can be isolated by screening for the production of relevant enzymes by alkalophilic microorganisms, e.g., using the ABTS assay described in R.E. Childs and W.G. Bardsley, Biochem. J. 145, 1975, pp. 93-1C3.
Other preferred enzymes are those which show a good thermostability, as well as a good stability towards the commonly used coloring additives such as non-ionic, cationic or anionic surfactants, chelating agents, salts, polymers, etc.
Enzymes can also be produced by a method comprising culturing a host cell transformed with a recombinant DNA vector carrying a DNA sequence encoding the enzyme, as well as the DNA sequences encoding the functions that allow expression of the DNA sequence encoding the enzyme, in a culture medium under conditions that allow the expression of the enzyme and the recovery of the enzyme from the culture.
A DNA fragment encoding the enzyme can, for example, be isolated by establishing a cDNA or genomic collection of a microorganism that produces the enzyme of interest, such as one of the above-mentioned organisms, and screening the positive clones by conventional methods such as hybridization to oligonucleotide probes synthesized on the basis of the complete or partial amino acid sequence of the enzyme, or by selecting clones expressing the appropriate activity of enzymes, or by selecting clones that produce a protein that is reactive with an antibody against the native enzyme.
Once selected, the DNA sequence can be inserted into an appropriate reproducible expression vector, comprising appropriate promoter, operator or terminator sequences, which allow the enzyme to be expressed in a particular host organism, as well as an origin of the replication that allows the vector to replicate in the host organism in question.
The resulting expression vector can then be transformed into an appropriate host cell, such as a fungal cell, preferred examples of which are a species of Aspergillus, more preferably Aspergillus aryzae or Aspergillus niger. The fungal cells can be transformed by a process that involves the formation of protoplasts and the transformation of the protoplasts followed by the regeneration of the cell wall in a manner known per se. The use of Aspergillus as a host microorganism is described in patent EP 238,023 (from Novo Industri A / S), the content of which is incorporated herein by reference.
Alternatively, the host organisms can be a bacterium, in particular strains of Streptomyces, Bacillus or E. coli. The transformation of the bacterial cells can be carried out in accordance with conventional methods, eg, as described in T. Maniatis et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor, 1982.
The screening of the appropriate sequences of DNA and the construction of vectors can also be carried out by standard procedures, cf. T. Maniatis et al., Op. cit.
The medium used to cultivate the transformed host cells can be any conventional means appropriate for the growth of the host cells in question. The expressed enzyme can be conventionally secreted into the culture medium, and can be recovered therefrom by well-known methods including separation of the cells from the medium by centrifugation or filtration, precipitating the proteinaceous components of the medium by means of a salt such as ammonium sulfate, followed by chromatographic procedures such as ion exchange chromatography, affinity chromatography or the like.
When the enzyme used in the invention is a peroxidase, a source of hydrogen peroxide, e.g., hydrogen peroxide itself, should be used. The source of hydrogen peroxide may be added at the beginning or during the process, eg, in an amount of 0.001-5 mM, particularly 0.01-1 mM.
A source of hydrogen peroxide includes hydrogen peroxide precursors, e.g., a perborate or a percarbonate. Another source of hydrogen peroxide includes enzymes that are capable of converting molecular oxygen into an organic or inorganic substrate within hydrogen peroxide and the oxidized substrate respectively. These enzymes produce only low levels of hydrogen peroxide, but can be used with a great advantage in the process of the invention since the presence of the peroxidase ensures an efficient utilization of the produced hydrogen peroxide. Examples of enzymes that can produce hydrogen peroxide include, but are not limited to, glucose oxidase, urate oxidase, galactose oxidase, alcohol oxidase, amine oxidase, amino acid oxidase and cholesterol oxidase.
In the methods of the present invention, the material is dyed at a temperature in the range of about 5 to about 120 ° C, preferably in the range of about 5 to about 80 ° C, and more preferably in the range from about 15 to about 70 ° C, and a pH in the range of from about 2.5 to about 12, preferably between about 4 and about 10, more preferably in the range of about 4.0 to about 7.0 or in the range of around 7.0 to around 10.0. More preferably, a pH below 6.5 is used (e.g., a pH in the range of 3-6, preferably in the range of 4-6 and more preferably in the range of 4.5-5.5) or above 8.0 ( eg, a pH in the range of 8-10, preferably in the range of 8.5-10 and more preferably in the range of 9-10). Surprisingly, the colors of the materials dyed by the methods of the present invention at a pH below 6.5 and above 8.0, are different from the colors of the same materials dyed by the methods at a pH in the range of 6.5-8.0. In a more preferred embodiment, a temperature and a pH close to the optimum temperature and pH of the enzyme are used respectively.
In a preferred embodiment, the methods of the present invention further comprise the addition to the aqueous solution of a mono- or divalent ion including, but not limited to, sodium, potassium, calcium and magnesium ions (0-3 M, preferably 25 mM-1M), a polymer which includes, but is not limited to, polyvinylpyrrolidone, polyvinyl alcohol, polyaspartate, polyvinylamide, polyethylene oxide (0-50 g / 1, preferably 1-500 mg / l) and a surfactant (10 mg-5 g / 1).
Examples of such surfactants are anionic surfactants such as carboxylates, for example, a metal carboxylate of a long-chain fatty acid; N-acyl sarcosinates; mono- or di-esters of phosphoric acid with ethoxylates of a fatty alcohol or salts of such esters; fatty alcohol sulfates such as sodium dodecyl sulfate, sodium octadecyl sulfate or sodium cetyl sulfate; ethoxylated sulfates of fatty alcohols; ethoxylated alkyl phenol sulphates; lignin sulfonates; petroleum sulfonates; alkyl aryl sulfonates such as alkyl benzene sulfonates or lower alkylnaphthalene sulfonates, eg, butyl naphthalene sulfonate; sulphonated salts or condensates of naphthalene formaldehyde; salts of sulfonated condensates of phenol-formaldehyde, or more complex sulfonates such as amide sulfonates, eg, the sulphonated product of the condensation of oleic acid and N-methyl taurine or the dialkyl sulfosuccinates, eg, the sulfonate of sodium or dioctyl succinate. Additional examples of such surfactants are nonionic surfactants such as condensation products of fatty acid esters, fatty alcohols, fatty acid amides or phenols substituted by fatty alkyl or alkenyl with ethylene oxide, block copolymers of ethylene oxide and oxide of propylene, acetylenic glycols such as 2, 4,7, 9-tetraethyl-5-decin-4,7-diol, or acetylenic glycols ethoxylated. Additional examples of such surfactants are cationic surfactants such as mono-, di- or polyamines, such as acetates, naphthenates or oleates; amines containing oxygen such as a polyoxyethylene alkylamine amine oxide; amines linked with amide, prepared by the condensation of a carboxylic acid with a di- or polyamine; or quaternary ammonium salts.
In another preferred embodiment, the methods of the present invention further comprise adding to the aqueous solution, an agent that increases the activity of the enzyme showing peroxidase activity or the enzyme showing oxidase activity. Enrichment agents are well known in the art. For example, the organic chemical compounds described in WO 95/01426, are known to increase the activity of a laccase. Additionally, the chemical compounds described in WO 94/12619 and WO 94/12621 are known to increase the activity of a peroxidase.
The invention is further illustrated by the following non-limiting examples.
EXAMPLES Example 1 DETERMINATION OF THE LACQUER ACTIVITY The laccase activity was determined from the oxidation of syringaldazine under aerobic conditions.
The violet color produced was measured by spectrophotometry at 530 nm. The analytical conditions were 19 μM of syringaldazine, 23.2 mM of acetate buffer, pH 5.5, 30 ° C and 1 minute of reaction time. A laccase unit (LACU) is the amount of laccase that catalyzes the conversion of 1 mmol of syringaldazin per minute to these conditions.
DETERMINATION OF PEROXIDASE ACTIVITY One unit of peroxidase (POXU) is the amount of enzyme that catalyzes the conversion of 1 μmol of hydrogen peroxide per minute to the following analytical conditions: 0.88 mM hydrogen peroxide, 1.67 mM 2, 2 '-azinobis (3-ethylbenzothiazolin-6-sulfonate), 0.1 M phosphate buffer (containing Triton X405 (1.5 g / 1000 ml), pH 7.0, incubated at 30 ° C, followed photometrically at 418 nm (the coefficient of ABTS extinction was established at 3.6 l / mmol * mm)).
DYEING FABRICS Five mg of a first compound (p-phenylenediamine)
("A"), p-toluenediamine ("B") or o-aminophenol ("C")) and 5 mg of a second compound (m-phenylenediamine ("D"), α-naphthol ("E") or 4-chlororesorcinol ("F")) (or 10 mg of the first compound in experiments without the second compound) were dissolved in 10 ml of 0.1 M K2HP04, pH 7.0, buffer solution. A laccase of Polyporus pinsi tus ("PpL") with an activity of 71.7 LACU / ml (deposited in the Centraal Bureau voor Schimmelcultures and given accession number CBS 678.70) or a laccase of Myceliophthora thermophila ("MtL") with an activity of 690 LACU / ml
(deposited in the Centraal Bureau voor Schimmelcultures and given the access number CBS 117.65) was diluted in the same buffer solution to an activity of 10
LACU / ml.
Multifiber cloth samples, Style 10A (4x10 cm) obtained from Test Fabrics Inc. (Middlesex, New Jersey) were rolled and placed in a test tube. The fabric samples contained a strip of a fiber made of wool. 4.5 ml of the precursor / coupler solution and 1 ml of laccase solution were added to the test tubes. The test tubes were closed, mixed and mounted in a test tube agitator and incubated for 60 minutes in a dark cabinet. After incubation, the fabric samples were rinsed in hot tap water for about 30 seconds.
The results of the experiment are provided in the following tables: Table 1
Table 2
Table 3
The results show that the color is formed in wool in the presence of the precursor and laccase of Polyporus pinsitus. Similar results are obtained with the laccase of Myceliophthora thermophila.
Example 2 Various materials were stained on an Atlas Launder-0 ("LOM") at 30 ° C for 1 hour at a pH in the range of 4-10. The dyed materials (all obtained from Test Fabrics Inc.) were wool in yarn (Style 526, 7 cm x 7 cm), and chlorinated braided wool (Style 530, - 7 cm x 7 cm).
A 0.1 M Britten-Robinson buffer solution was prepared at an appropriate pH, by mixing solution A (0.1 M H3P0, 0.1 M CH3COOH, 0.1 M H3BO3) and B (0.5 M NaOH). In order to produce buffer solutions at pH's of 4, 5, 6, 7, 8, 9 and 10, 806 ml, 742 ml, 706 ml, 656 ml, 626 ml, 596 ml and 562 ml of solution A were diluted respectively, in one liter with solution B.
To 75 ml of each buffer was added 0.5 mg / ml of a compound selected from p-phenylenediamine, o-aminophenol and m-phenylenediamine. The pH was checked and adjusted if necessary. Solutions of 75 ml of compound / buffers were combined to form 150 ml of each buffer / compound combination solution, which was added to a LOM beaker.
They were soaked after fabric samples of the materials, in each buffer / compound combination solution. A volume corresponding to the volume of laccase to be added was then separated. A laccase of Myceliophthora thermophila ("MtL") with an activity of 690 LACU / ml in the buffer solution was diluted to an activity of 300 LACU / ml. Two LACU / ml were added for each pH, except the pH of 7.0. At a pH of 7.0, 0, 1, 2, 4 LACU / ml was added for the dose profile. The LOM beakers were then mounted on the LOM. After 1 hour at 42 RPM and 30 ° C, the LOM was stopped. The liquid was emptied and the fabric samples were rinsed in the beaker circulating deionized water for about 15 minutes. The fabric samples were dried and the CIELAB values were measured using a ColorEye 7000 instrument. The CIELAB results are given in Tables 4-7.
Table 4 Dyeing with precursors of p-phenylenediamine and m-phenylenediamine (pH profile, 2 LACU / ml) pH4 pH5 pH6 pH7 pH8 pH9 pHIO Stamen L * 41.57 28.21 20.25 14.73 18.94 35.06 13.52 wool a * 2.71 1.24 0.43 1.63 3.56 - 1.92 1.79 b * -0.75 -2.09 -5.76 -5.84 -17.52 -14.05 -4.28
Wool L * 18.46 16.05 15.04 14.19 15.47 31.44 13.84 chlorinated to * 2.32 1.01 0.88 1.83 2.78 -3.05 2.97 b * 0.09 0.87 1.03 1.53 -11.43 -13.27 2.06
Table 5 Staining with p-phenylenediamine and m-phenylenediamine precursors (dose profile-pH 7) 0 LACU L LACU 4 LACU Wool staple L * 54.97 14.52 14.27 a * 1.48 1.55 1.49 b * 1.26 -6.09 -5.6 Chilled Wool L * 43.2 14.42 14.33 a * 1.79 1.75 1.69 b * 1.61 1.5 1.65
Table 6 Dyeing with o-aminophenol and m-phenylenediamine precursors (pH profile, 2 LACU / ml) pH4 pH5 pH6 pH7 pH8 pH9 pH
Stamen of L * 33.68 33.05 35.96 37.42 42.55 59.24 49. wool a * 3.77 5.35 8.56 10.07 8.75 10.53 8. b * 8.26 11.03 18.83 22.33 22.82 37.2 34.
Chlorinated wool L * 21.07 19.11 21.01 24.7 34.42 59.9 48 a * 3.14 2.77 4.82 7.22 6.88 10.08 10 b * 4.23 4.31 8.04 12.64 18.08 36.78 34.
Table 7 Staining with precursors of o-aminophenol and m-phenylenediamine (dose profile - pH 7) 0 LACU 1 LACU 4 LACU Stamen of L * 80.23 38.57 36.18 wool a * 1.1 9.21 10.8 b * 20.09 21.33 22.76 Wool Chlorinated L * 77.36 27.1 26.33 a * 0.86 7.92 6.92 b * 19.53 14.8 13.5
The parameters "L", "a" and "b" used in the tables, are used to quantify the color and are well known by people with ordinary skill in the art of color science. See for example, Billmeyer & Saltzman, Principies of Color Technology, Second Edition, John Wiley & Sons, New York, 1981, p. 59
The results show that wool in yarn and wool in chlorinated yarn were stained at all pH's, with strong shades from gray at a low pH to dark blue and black at a high pH with the combination of p-phenylenediamine and m- phenylenediamine, and shades from coffee at a low pH to orange / yellow at a high pH with the combination of o-aminophenol and m-phenylenediamine.
In all the dosing experiments, no noticeable difference was observed from the dosage of 1, 2 or 4 LACU / ml. The control experiment with 0 LACU / ml clearly demonstrates that the dyeing is catalyzed by the laccase.
Example 3 The time profile for dyeing was determined using the procedure described in Example 2, except that the experiments were conducted only at pH 5.0 and 8.0, over time intervals of 0, 5, 15, 35 and 55 minutes . In each experiment, 2 LACU / ml of the laccase of Myceliophtora thermophila was added. The results are shown in Tables 8-11.
Table 8 Dyeing with precursors of p-phenylenediamine and m-phenylenediamine Time Profile, 2 LACU / ml, pH 5 0 min 5 min 15 min 35 min 55 min
Stamen of L * 76.48 52.08 36.3 27.02 26.56 wool a * .02 1.35 1.96 1.3 1.18 b * 8 -0.02 -1.39 -1.68 -2.03
Lana L * 63.73 19.23 16.81 16.48 16.75
Chlorine Wool a * 0.1 1.86 1.28 0.77 1.11 b * 10.3 -0.68 0.49 1.04 1.03
Table 9 Dyeing with precursors of p-phenylenediamine and m-phenylenediamine Time Profile, 2 LACU / ml, pH8 0 min 5 min 15 min 35 min 55 min Stamen of L * 64.43 23.66 14.57 13.11 13.06 wool a * -3.03 1.05 2.14 1.49 1.2 b * -3.32 -15.45 -8.72 -4.52 -3.68
Lana L * 58.96 17.36 14.09 13.89 13.66
Chlorinated to * -1.66 0.57 1.9 2.71 2.64 b * 2.68 -3.98 0.14 2.21 1.99
Table 10 Staining with precursors of o-aminophenol and m-phenylenediamine Time profile, 2 LACU / ml, pH 5 0 min 5 min 15 min 35 min 55 min Stamen of L * 79.4 50.67 35.94 32.4 32.89 wool a * 1.54 6.47 7.11 6.08 5.98 b * 16.02 20.88 18.43 14.28 12.52
Chlorinated wool L * 76.72 39.53 22.12 18.82 19.58 a * 2.33 6.81 4.21 2.88 3.1 b * 18.26 16.48 8.23 4.89 4.77 Table 11 Dyeing with o-aminophenol and m-phenylenediamine precursors Time Profile, 2 LACU / ml, pH 8 0 min 5 min 15 min 35 min 55 min Stamen of L * 80.06 63.03 49.37 42.51 41.24 wool a * 1.63 15.71 17.1 12.32 9.97 b * 25.87 43.37 38.69 30.26 25.78
Chlorinated Wool L * 79.6 62.87 47.88 36.72 33.62 a * 0.57 13.17 14.46 10.26 7.88 b * 24.63 41.64 34.34 24.47 19.7 The results show that most of the color is formed within the first 15 minutes. They stained wool in yarn and wool in chlorinated stamen at both pH's.
Example 4 Wool was dyed on an Atlas Launder-O- ("LOM") at 30 ° C for one hour at a pH of 5.5. The dyed material (obtained from Test Fabrics Inc.) was wool in yarn (Style 526, 8cm x 8 cm).
A solution of 0.5 mg / ml of a first compound (p-phenylenediamine "A") and a 0.5 mg / ml solution of a second compound (1-naphthol, "B"), was prepared by dissolving the compound in an amount appropriate CH3COONa 0.1 M, pH 5.5, buffer. A total volume of 100 ml was used in each LOM beaker. 100 ml of "A" was added to a beaker and 50 ml of "A" and 50 ml of "B" were combined to form 100 ml in a second beaker. The fabric samples of the materials listed above were moistened in DI water and soaked in the precursor solutions. A laccase of Myceliophthora thermophila ("MtL") with an activity of 690 LACU / ml? 80 LACU / mg) was added to each beaker at a concentration of 12.5 mg / l. The LOM beakers were sealed and mounted in the LOM.
After 1 hour at 42 RPM and 30 ° C, the LOM stopped. The spent liquor was emptied and the fabric samples were rinsed in cold water from the tap for about 15 minutes. The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth Color Eye 7000. The results are given in Tables 12 and 13.
Table 12 Stained with the p-phenylenediamine precursor (pH 5.5, 12.5 mg / l MtL)
Table 13 Dyeing with precursors of p-phenylenediamine and 1-naphthol (pH 5.5, 12.5 mg / l MtL)
The results show that the wool can be dyed using a precursor and laccase of Myceliphthora thermophila (nuances brown with A, and purple nuances with A / B).
Example 5 Wool was dyed on an Atlas Launder-0- ("LOM") at 30 ° C for one hour at a pH of 5.5. The dyed material (obtained from Test Fabrics Inc.) was wool in yarn (Style 526, 8 cm x 8 cm)
A solution of 0.5 mg / ml of a first compound (p-phenylenediamine "A") and a 0.5 mg / ml solution of a second compound (1-naphthol, "B"), was prepared by dissolving the compound in an amount Appropriate CH3COONa 0.1 M, pH 5.5, buffer. A total volume of 100 ml was used in each LOM beaker. 100 ml of "A" was added to a beaker and 50 ml of "A" and 50 ml of "B" were combined to form 100 ml in a second beaker The fabric samples of the materials listed above were were moistened in DI water and rinsed in precursor solutions.A polyporus pinsitus ("PpL") laccase with an activity of 70 LACU / ml (100 LACU / mg) was added to each beaker at a concentration of 12.5 mg / 1. The LOM beakers were sealed and mounted on the LOM.After 1 hour at 42 RPM and 30 ° C, the LOM was stopped.The spent liquor was emptied and the fabric samples rinsed in cold tap water for about 15 minutes The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth Color Eye 7000. The results are given in Tables 14 and 15.
Table 14 Dyeing with p-phenylenediamine precursor (pH 5.5, 12.5 mg / l PpL)
Table 15 Dyeing with precursors of p-phenylenediamine and 1-naphthol (pH 5.5, 12.5 mg / l PpL)
The results show that the wool can be dyed (nuances brown with A, and shades purple with A / B) using the precursor and laccase of Polyporous pinsitus (PpL).
Example 6 Wool was dyed on an Atlas Launder-0- ("LOM") at 30 ° C for one hour at a pH of 5.5. The dyed material (obtained from Test Fabrics Inc.) was wool in yarn (Style 526, 8 cm x 8 cm) A solution of 0.5 mg / ml of a first compound (p-phenylenediamine "A") and a solution of 0.5 mg / ml of a second compound (1-naphthol "B") was prepared by dissolving the compound in the appropriate amount of CH3COONa 0.1 M, pH 5.5, buffer. A total volume of 100 ml was used in each LOM beaker. 100 ml of "A" was added to a beaker and 50 ml of "A" and 50 ml of "B" were combined to form 100 ml in a second beaker. The fabric samples of the materials listed above were moistened in DI water and soaked in the precursor solutions. A bilirubin oxidase from Myrothecium verrucaria ("BiO") with an activity of 0.04 LACU / mg (1 mg / ml) was added to each beaker at a concentration of 12.5 mg / l. The LOM beakers were sealed and mounted in the LOM. After 1 hour at 42 RPM and 30 ° C, the LOM was stopped. The spent liquor was emptied and the fabric samples were rinsed in cold water from the tap for about 15 minutes. The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth Color Eye 7000. The results are given in Tables 16 and 17.
Table 16 Dyeing with p-phenylenediamine precursor
Table 17 Dyeing with precursors of p-phenylenediamine and 1-naphthol
The results show that the wool can be dyed (nuances brown with A, and shades purple with A / B) using the precursor and the bilirubin oxidase.
Example 7 It was dyed. wool on an Atlas Launder-O- ("LOM") at 30 ° C for one hour at a pH of 5.5. The dyed material (obtained from Test Fabrics Inc.) was wool in yarn (Style 526, 8 cm x 8 cm)
A 0.5 mg / ml solution of a first compound (p-phenylenediamine "A") and a 0.5 mg / ml solution of a second compound (1-naphthol "B") was prepared by dissolving the compound in the appropriate amount of CH3COONa 0.1 M, pH 5.5, buffer. A total volume of 100 ml was used in each LOM beaker. 100 ml of "A" was added to a beaker and 50 ml of "A" and 50 ml of "B" were combined to form 100 ml in a second beaker. The fabric samples of the materials listed above were moistened in DI water and soaked in the precursor solutions. A laccase of Rhizoctonia solani ("RsL") with an activity of 5.2 LACU / mg (2 mg / ml) was added to each beaker at a concentration of 12.5 mg / l. The LOM beakers were sealed and mounted in the LOM. After 1 hour at 42 RPM and 30 ° C, the LOM was stopped. The spent liquor was emptied and the fabric samples were rinsed in cold water from the tap for about 15 minutes. The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth Color Eye 7000. The results are given in Tables 18 and 19. Table 18 Dyeing with p-phenylenediamine precursor (pH 5.5., 12.5 mg / l RsL)
Table 19 Dyeing with precursors of p-phenylenediamine and 1-naphthol (pH 5.5., 12.5 mg / l RsL)
The results show that wool can be dyed (coffee nuances with A, and purple shades with A / B) using Rhizoctonia solani precursor and laccase.
Exercise 8 The dyed material (obtained from Test Fabrics, Inc.) was wool (style 526, 8 cm x 8 cm), on an Atlas Launder-O- meter ("LOM") at 60 ° C and pH of 5.5.
A solution of 0.25 mg / ml of a first compound (p-phenylenediamine "A") and a solution of 0.25 mg / ml of a second compound (2-aminophenol "B") was prepared by dissolving the compound in the appropriate amount of CH3COONa of 2 g / L, pH 5.5, buffer. A total volume of 100 ml was used in each LOM beaker. 50 ml of "A" and 50 ml of "B" were combined to form 100 ml in a LOM beaker. The fabric samples of the materials listed above were moistened in DI water and soaked in the precursor solutions. The LOM beakers were sealed and mounted in the LOM. After an incubation time of 10, 15 or 30 minutes in the LOM (42 RPM), the LOM was stopped and a laccase of Myceliophthora thermophila ("MtL") was added with an activity of 690 LACU / ml (80 LACU / mg) to each beaker at a concentration of 1 LACU / ml. After 50, 45 or 30 minutes at 42 RPM and 60 ° C, the LOM was stopped and the sample separated. Two controls were prepared without pre-incubation by adding the precursor solution, cloth samples, and enzymes to the LOM beaker. The beakers were mounted in the LOM. After 15 minutes at 42 RPM and 60 ° C a beaker was separated. The other control was operated for a total of 60 minutes at 42 RPM and 60 ° C and then separated. The spent liquor was emptied of the samples, and the fabric samples were rinsed in cold tap water for about 15 minutes. The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth Color Eye 7000. The results are given in Tables 20-24.
Table 20 Control dyeing with precursors A and B, 0 min./30 min.
Table 21 Control dyeing with precursors A and B, 0 min./60 min.
Table 22 Stained with precursors A and B, 10 min./50 min.
Table 23 Dyeing with precursors A and B, 15 min./45min.
Table 24 Tinting with precursors A and B, 30 min./30 min.
The color fastness to wash (wash firmness) for these fabric samples was evaluated using the Test Method of the American Textile and Color Chemicals Association (AATCC) 61-1989, 2A. The Launder-O- meter was preheated to 49 ° C and 200 ml of the 0.2% AATCC Standard WOB Reference Detergent (without optical brightener) and 50 steel balls were placed in each LOM beaker. The beakers were sealed and mounted in the LOM and operated at 42 RPM for 2 minutes to preheat the beakers to the test temperature. The rotor stopped and the beakers separated. The fabric samples were added to the beakers and the LOM was operated for 45 minutes. The beakers were separated and the fabric samples were rinsed in hot tap water for 5 minutes, with occasional squeezing. The fabric samples were then dried at room temperature and evaluated by the Macbeth Color Eye 7000. A grading scale (1-5) was assigned to each fabric sample using the AATCC Evaluation Procedure 1, Scale. of Gray for Color Change. The results are given in Tables 25-29.
Table 25 Results of washing firmness for A and B, 0 min./30min.
Table 26 Results of washing firmness for A and B, 0 min./60min,
Table 27 Results of washing firmness for A and B, 15 min./45 min.
Table 28 Washing firmness results for A and B, 10 min./50 min.
Table 29 Washing firmness results for A and B, 30 min./30 min.
The results show that the wool can be dyed using a precursor and laccase from Mycelioph thora thermophila (MtL). From the grading of the gray scale and L, it is evident that the color intensity and the wash-io firmness are improved by incubating the fabric samples in the precursor solution before adding the enzyme.
Example 9 The dyed materials (all obtained from Test Fabrics Inc.) were wool in yarn (Style 526, 7 cm x 7 cm), and chlorinated braided wool (Style 530, 7 cm x 7 cm) in an Atlas Launder meter -0 ("LOM") at 40 ° C for 1 hour at a pH of 5.5.
Two mediators were evaluated in this experiment and each was dissolved in a buffer solution. Three buffer solutions were made: a buffer solution of 2 g / L of CH3C00Na, pH 5.5 ("1"), a buffer solution of 2 g / L of CH3COONa, pH 5.5 containing 100 mM of 10-propionic phenothiazine (PPT) ("2") and a buffer solution of 2 g / L of CH3COONa containing lOOmM of methyl syringate ("3").
Three solutions of 0.25 mg / ml of a compound (p-phenylenediamine "A") were prepared by dissolving the compound in the appropriate amount of the buffer solution (1, 2 or 3). A total volume of 120 ml was used in each LOM beaker. 60 ml of A and 60 ml of B were combined to form 120 ml (for each buffer: 1.2 or 3). The fabric samples of the materials listed above were moistened in DI water and rinsed in the precursor solutions. The LOM beakers were sealed and mounted in the LOM. After 10 minutes at 42 RPM and 40 ° C, the LOM stopped. A laccase of Myceliophthora thermophila ("MtL") with an activity of 690 LACU / ml (80 LACU / mg) was added to each beaker at an activity of 0.174 LACU / ml. The beakers were sealed again and mounted in the LOM and operated for 50 minutes (42 RPM) at 40 ° C. The beakers were separated and the spent liquor was emptied and the fabric samples were rinsed in cold tap water for about 15 minutes. The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth ColorEye 7000. The results are given in Tables 30, 31 and 32.
Table 30 Dyeing with precursors A and B (2g / L CH3COONa, pH 5.5., MtL)
Table 31 Dyeing with precursors A and B (2 g / L CH3COONa, pH 5.5, 100 μM PPT, MtL)
Table 32 Dyeing with precursors A and B (2 g / L CH3COONa, pH 5.5, 100 μM methyl syringate, MtL)
The color fastness for washing (washing firmness) of these fabric samples was evaluated using the Test Method of the American Association of Textile and Color Chemicals (AATCC) 61-1989, 2A. The Launder-O- meter was preheated to 49 ° C and 200 ml of the 0.2% AATCC Standard WOB Reference Detergent (without optical brightener) and 50 steel balls were placed in each LOM beaker. The beakers were sealed and mounted in the LOM and operated at 42 RPM for 2 minutes to preheat the beakers to the test temperature. The rotor stopped and the beakers separated. The fabric samples were added to the beakers and the LOM was operated for 45 minutes. The beakers were separated and the fabric samples were rinsed in hot tap water for 5 minutes, with occasional squeezing. The fabric samples were then dried at room temperature and evaluated by the Macbeth Color Eye 7000. A grading scale (1-5) was assigned to each fabric sample using the AATCC Evaluation Procedure 1, Scale. of Gray for Color Change. The results are given in Tables 33-35.
Table 33 Washing firmness results for precursors A and B (2 g / L CH3COONa, pH 5.5, MtL)
Table 34 Washing firmness results for precursors A and B (2 g / L CH3COONa, pH 5.5, 100 μM PPT, MtL)
Table 35 Washing firmness results for precursors A and B (2 g / L CH3COONa, pH 5.5, 100 μM methyl syringate, MtL)
The same experiment was repeated except that a third compound (2-aminophenol, "C") and a fourth compound (m-phenylenediamine, "D") were used. The temperature used was 50 ° C. The results are given in Tables 36-41 Table 36 Dyeing with precursors C and D (2 g / L CH3COONa, pH 5.5, MtL)
Table 37 Dyeing with precursors C and D (2 g / L CH3COONa, pH 5.5, 100 μM PPT, MtL)
Table 38 Dyeing with precursors C and D (2 g / L CH3COONa, pH 5.5, 100 μM methyl syringate, MtL)
Table 39 Washing firmness results for precursors C and D (2 g / L CH3COONa, pH 5.5, MtL)
Chlorinated wool 51.35 7.04 13.16
Table 40 Washing firmness results for precursors C and D (2 g / L CH3C00Na, pH 5.5, 100 μM PPT, MtL)
Table 41 Results of washing firmness for precursor C (2 g / L CH3COONa, pH 5.5, 100 μM methyl syringate, MtL)
The results of these two groups of experiments show that a mediator can be used for dyeing and to obtain improved washing firmness. In both experiments, the wool yarn and the chlorinated wool yarn were stained at a pH of 5.5 in a buffer solution of CH3COONa, in a buffer solution of CH3COONa containing PPT and in a buffer solution of CH3COONa containing methyl syringate. . However, the mediator resulted in improved washing firmness only in the first experiment.
Example 10 Wool was dyed on an Atlas Launder-O- ("LOM") at 30 ° C for one hour at a pH of 5.5. The dyed material (obtained from Test Fabrics, Inc.) was woolen yarn (Style 526, 8 cm x 8 cm).
A 0.5 mg / ml solution of a first compound (p-phenylenediamine "A") and a 0.5 mg / ml solution of a second compound (1-naphthol "B") was prepared by dissolving the compound in the appropriate amount of CH3C00Na 0.1 M, pH 5.5, buffer. A total volume of 100 ml was used in each LOM beaker. 100 ml of "A" was added to a beaker and 50 ml of "A" and 50 ml of "B" were combined to form 100 ml in a second beaker. The fabric samples of the materials listed above were moistened in DI water and soaked in the precursor solutions. A Coprinus cinereus peroxidase ("CiP") with an activity of 180, 000 POXU / ml, was added to each beaker at a concentration of 0.05 POXU / ml. LOM hydrogen peroxide either 200 or 500 mM was added to each beaker. The LOM beakers were sealed and mounted in the LOM. After 1 hour at 42 RPM and 30 ° C, the LOM was stopped. The spent liquor was emptied and the fabric samples were rinsed in cold water from the tap for about 15 minutes. The fabric samples were dried at room temperature and the CIELAB values were measured for all fabric samples using the Macbeth Color Eye 7000. The results are given in Tables 42-45.
Table 42 Staining with precursor A, 200 μM H202
Table 43 Tinting with precursor A, 500 μM H202
Table 44 Dyeing with precursor A and B, 200 μM H202
Table 45 Dyeing with precursors A and B, 500 μM H202
The results show that the wool can be dyed (purple shades with A and A / B) using precursor, peroxide or peroxidase Coprinus cinereus (CiP).
EXAMPLE 11 A batch of chrome-plated skin in blue (Prime Tanning Corp., St. Joseph, MO) was stained in a test tube at room temperature for 16 hours at a pH of 5, 7 and 9.
Three solutions of 0.5 mg / ml of a first compound (p-phenylenediamine, "A"), (pH of 5, 7 and 9), three solutions of 0.5 mg / ml of a second compound (1-naphthol, "B" ) and three 0.5 mg / ml solutions of a third compound (4-hydroxycinnamic acid, "C"), were prepared by dissolving each compound in the appropriate amount of a 0.1 M Britten-Robinson buffer solution (BR buffer).
The skin substrate (1.5 cm x 4 cm) was rolled up and placed in a 10 cm test tube. A total volume of 7 ml was used in each test tube. 6 ml of A (or 6 ml of C) was added to a test tube, and 3 ml of A and 3 ml of B (or 3 ml of A and 3 ml of C) were combined to form 6 ml in one second. test tube. A laccase of Myceliophthora thermophila ("MtL") with an activity of 690 LACU / ml (80 LACU / mg) was added to each beaker at a concentration of 2 LACU / ml (1 ml of enzyme solution added to each tube test to give a total of 7 ml per test tube). The test tubes were closed, mixed and mounted on a test tube rotator. The test tubes were incubated for 16 hours in a dark cabinet at room temperature. After incubation, the fabric samples were rinsed in cold tap water for 1 minute and dried at room temperature.
The results of the experiments are given in Table 46: Table 46
These results show that dyes are formed on skin in the presence of Mycelioph thora thermophila laccase and different types of precursors over a range of pH conditions.
Example 12 Silk was dyed in a test tube at room temperature for 16 hours at a pH of 5, 7 and 9. The dyed material (obtained from Test Fabrics, Inc.) was silk china crepe (Style 601, 1.5 cm x 4 cm).
Three solutions of 0.5 mg / ml of a first compound (p-phenylenediamine, "A") (pH of 5, 7 and 9) and three solutions of 0.5 mg / ml of a second compound (1-naphthol, "B") were prepared by dissolving each compound in an appropriate amount of 0.1 M Britton-Robinson buffer (BR buffer).
The silk substrate was rolled up and placed in a 10 cm test tube. A total volume of 7 ml was used in each test tube. 6 ml of A were added to a test tube and 3 ml of A and 3 ml of B were combined to form
6 ml in a second test tube. A laccase of Myceliophthora thermophila ("MtL") with an activity of 690 LACU / ml (80 LACU / mg) was added to each beaker at a concentration of 2 LACU / ml (an enzyme solution of 1 ml added to each test tube to give a total of
7 ml per test tube). The test tubes were closed, mixed and mounted on a test tube rotator. The test tubes were incubated for 16 hours in a dark cabinet at room temperature. After incubation, the fabric samples were rinsed in cold tap water for 1 minute and dried at room temperature.
The results of the experiments are given in Table 47. Table 47
These results demonstrate that dyes are formed in the silk in the presence of Myceliophthora thermophila laccase, and of different types of precursors over a range of pH conditions.
Example 13 A printing paste was made by dissolving 5 mg / ml paraphenylenediamine in 0.1 M sodium phosphate, pH 5.5, buffer, and adding 2.5% gum arabic.
The printing paste was transferred manually to a woolen cloth using a printing screen and a scraper.
The portions of cloth that were not going to be printed were covered with a mask.
The fabric was then steamed for 10 minutes in a steam chamber and allowed to dry.
The color was developed by immersing the fabric in a laccase solution of 2 LACU / ml followed by an incubation for one hour.
Example 14 A mono-, di- or polycyclic aromatic or heteroaromatic compound can be applied to the material by mordant impregnation. For example, 0.5 mg / ml of p-phenylenediamine was dissolved in 500 ml of 0.1 M K2P04, pH 7, buffer. A laccase was diluted in the same buffer solution. The p-phenylenediamine solution is impregnated onto the material using a standard laboratory pad at 60 ° C. The fabric is steamed for 10 minutes. The vaporized material can then be impregnated a second time with an enzyme solution. The dye is allowed to develop when the fabric samples are incubated at 40 ° C. After incubation, the fabric samples are rinsed in hot tap water for about 30 seconds.
It is noted that with respect to this date, the best method known to the applicant to carry out the invention is that which is clear from the present description of the invention.
Having described the invention as above, the content of the following is claimed as property
Claims (21)
1. A method for dyeing a material, characterized in that it comprises: (a) soaking the material in an aqueous solution comprising one or more polycyclic or heteroaromatic mono-, di-, or aromatic compounds, each of which is optionally substituted with one or more functional groups or substituents, wherein each functional group or substituent is selected from the group consisting of halogen; sulfo; sulfonate; sulfa ino; Sulfanyl; Not me; amido; nitro; azo; imino carboxy; cyano; formyl; hydroxy; halocarbonyl; carbamoyl; carbamidoyl; phosphonate; phosphonyl; C? _? 8 alkyl, C? _ 8 alkenyl, C? -? 8 alkynyl; C 8 alkoxy; oxycarbonyl C? _? 8; oxoalkyl C? _? 8; alkyl sulfanyl C? _? 8; alkyl sulfonyl C? -? 8; alkyl imino or amino C? _? 8 which is substituted with one, two or three C? _? 8 alkyl groups; wherein each C? -? 8 alkyl, C? _? 8 alkenyl or C? _ 8 alkynyl group can be mono-, di or poly-substituted by any of the appropriate functional groups or substituents; and (b) treating the soaked material in an aqueous solution with (i) a source of hydrogen peroxide and an enzyme showing peroxidase activity or (ii) an enzyme showing oxidases activity on one or more aromatic or heteroaromatic compounds; wherein the material is a fabric, filament, fiber, garment or film made of fur, leather, fur, silk or wool.
2. The method according to claim 1, characterized in that the one or more mono-, di- or polycyclic aromatic or heteroaromatic compound is a naphthol.
3. The method according to claim 1, characterized in that the one or more mono-, di- or polycyclic aromatic or heteroaromatic compound is an aromatic diamine.
4. The method according to claim 1, characterized in that the one or more mono-, di- or polycyclic aromatic or heteroaromatic compound is an aminophenol.
5. The method according to claim 1, characterized in that the one or more mono-, di- or polycyclic aromatic or heteroaromatic compound is a phenol.
6. The method according to claim 1, characterized in that the material is made of hair skin.
7. The method according to claim 1, characterized in that the material is made of leather.
8. The method according to claim 1, characterized in that the material is made of skin.
9. The method according to claim 1, characterized in that the material is made of silk fabric.
10. The method according to claim 1, characterized in that the material is made of wool.
11. The method according to claim 1, characterized in that the soaked material is treated with an enzyme showing a peroxidase activity on the one or more mono-, di- or polycyclic aromatic or heteroaromatic compounds and a source of hydrogen peroxide.
12. The method according to claim 11, characterized in that the enzyme is a peroxidase or haloperoxidase.
13. The method according to claim 1, characterized in that the soaked material is treated with an enzyme showing an oxidase activity on the one or more mono-, di- or polycyclic aromatic or heteroaromatic compounds.
14. The method according to claim 13, characterized in that the enzyme is selected from the group consisting of bilirubin oxidase, catechol oxidase, laccase, o-aminophenol oxidase and polyphenol oxidase.
15. The method according to claim 1, characterized in that the material is dyed at a temperature in the range of about 5 to about 120 ° C.
16. The method according to claim 1, characterized in that it further comprises adding to the aqueous solution in step (b), a mono or divalent ion selected from the group consisting of sodium, potassium, calcium and magnesium ions.
17. The method according to claim 1, characterized in that it also comprises adding to the aqueous solution in step (b), a polymer selected from the group consisting of polyvinylpyrrolidone, polyvinyl alcohol, polyaspartate, polyvinylamide and polyethylene oxide.
18. The method according to claim 1, characterized in that it further comprises adding to the aqueous solution in step (b), an anionic, nonionic or cationic surfactant.
19. The method according to claim 1, characterized in that the material is dyed at a pH in the range of 2.5-12.
20. The method according to claim 1, characterized in that it further comprises adding to the aqueous solution in step (b), an agent that increases the activity of the enzyme.
21. The method according to claim 1, characterized in that the aqueous solutions used in steps (a) and (b) are the same.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US009198 | 1995-12-22 | ||
US016729 | 1996-05-02 |
Publications (1)
Publication Number | Publication Date |
---|---|
MXPA98004657A true MXPA98004657A (en) | 1999-07-06 |
Family
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