US20020004958A1 - Dyeing substrates - Google Patents
Dyeing substrates Download PDFInfo
- Publication number
- US20020004958A1 US20020004958A1 US09/802,189 US80218901A US2002004958A1 US 20020004958 A1 US20020004958 A1 US 20020004958A1 US 80218901 A US80218901 A US 80218901A US 2002004958 A1 US2002004958 A1 US 2002004958A1
- Authority
- US
- United States
- Prior art keywords
- substrate
- enzyme
- oxidation
- amino
- peroxidase
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 239000000758 substrate Substances 0.000 title claims abstract description 79
- 238000004043 dyeing Methods 0.000 title claims abstract description 42
- 210000004209 hair Anatomy 0.000 claims abstract description 47
- 238000007254 oxidation reaction Methods 0.000 claims abstract description 38
- 230000003647 oxidation Effects 0.000 claims abstract description 37
- 239000000203 mixture Substances 0.000 claims abstract description 34
- 238000000034 method Methods 0.000 claims abstract description 28
- 239000004753 textile Substances 0.000 claims abstract description 5
- 239000000835 fiber Substances 0.000 claims abstract description 4
- 102000004190 Enzymes Human genes 0.000 claims description 74
- 108090000790 Enzymes Proteins 0.000 claims description 74
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims description 42
- 108010029541 Laccase Proteins 0.000 claims description 38
- 102000003992 Peroxidases Human genes 0.000 claims description 38
- 108040007629 peroxidase activity proteins Proteins 0.000 claims description 30
- 150000001875 compounds Chemical class 0.000 claims description 26
- 239000003607 modifier Substances 0.000 claims description 21
- -1 amino benzoic acid compound Chemical class 0.000 claims description 19
- 102000004316 Oxidoreductases Human genes 0.000 claims description 18
- 108090000854 Oxidoreductases Proteins 0.000 claims description 18
- 239000000463 material Substances 0.000 claims description 17
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 claims description 11
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 claims description 9
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 claims description 9
- 125000003277 amino group Chemical group 0.000 claims description 8
- 239000000427 antigen Substances 0.000 claims description 8
- 102000036639 antigens Human genes 0.000 claims description 8
- 108091007433 antigens Proteins 0.000 claims description 8
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 8
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical group [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 claims description 7
- 239000001301 oxygen Substances 0.000 claims description 7
- 229910052760 oxygen Inorganic materials 0.000 claims description 7
- 125000000217 alkyl group Chemical group 0.000 claims description 6
- 229960004050 aminobenzoic acid Drugs 0.000 claims description 6
- 239000003550 marker Substances 0.000 claims description 6
- 150000003839 salts Chemical class 0.000 claims description 6
- 108700020962 Peroxidase Proteins 0.000 claims description 5
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 5
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 claims description 4
- 125000003342 alkenyl group Chemical group 0.000 claims description 4
- 125000000304 alkynyl group Chemical group 0.000 claims description 4
- 125000001188 haloalkyl group Chemical group 0.000 claims description 4
- JGJLWPGRMCADHB-UHFFFAOYSA-N hypobromite Chemical compound Br[O-] JGJLWPGRMCADHB-UHFFFAOYSA-N 0.000 claims description 4
- 229920002994 synthetic fiber Polymers 0.000 claims description 4
- 108010031396 Catechol oxidase Proteins 0.000 claims description 3
- 102000030523 Catechol oxidase Human genes 0.000 claims description 3
- 241001330975 Magnaporthe oryzae Species 0.000 claims description 3
- 241001203365 Myceliophthora sp. Species 0.000 claims description 3
- 241001565691 Polyporus sp. Species 0.000 claims description 3
- 241000684075 Rhizoctonia sp. Species 0.000 claims description 3
- 238000004458 analytical method Methods 0.000 claims description 3
- WQYVRQLZKVEZGA-UHFFFAOYSA-N hypochlorite Inorganic materials Cl[O-] WQYVRQLZKVEZGA-UHFFFAOYSA-N 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 108010061247 2-aminophenol oxidase Proteins 0.000 claims description 2
- 241000003910 Baronia <angiosperm> Species 0.000 claims description 2
- VTLYFUHAOXGGBS-UHFFFAOYSA-N Fe3+ Chemical compound [Fe+3] VTLYFUHAOXGGBS-UHFFFAOYSA-N 0.000 claims description 2
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- 241000619663 Pyricularia sp. Species 0.000 claims description 2
- 241000223255 Scytalidium Species 0.000 claims description 2
- 241000222355 Trametes versicolor Species 0.000 claims description 2
- 239000001257 hydrogen Substances 0.000 claims description 2
- 229910052739 hydrogen Inorganic materials 0.000 claims description 2
- 150000002484 inorganic compounds Chemical class 0.000 claims description 2
- 229910010272 inorganic material Inorganic materials 0.000 claims description 2
- 229910052742 iron Inorganic materials 0.000 claims description 2
- 238000004451 qualitative analysis Methods 0.000 claims description 2
- 238000004445 quantitative analysis Methods 0.000 claims description 2
- PXQLVRUNWNTZOS-UHFFFAOYSA-N sulfanyl Chemical class [SH] PXQLVRUNWNTZOS-UHFFFAOYSA-N 0.000 claims description 2
- 150000005415 aminobenzoic acids Chemical class 0.000 claims 3
- 229940052295 esters of aminobenzoic acid for local anesthesia Drugs 0.000 claims 2
- 241000205003 Methanothrix thermoacetophila Species 0.000 claims 1
- 241000208227 Toxicodendron vernicifluum Species 0.000 claims 1
- SOCTUWSJJQCPFX-UHFFFAOYSA-N dichromate(2-) Chemical compound [O-][Cr](=O)(=O)O[Cr]([O-])(=O)=O SOCTUWSJJQCPFX-UHFFFAOYSA-N 0.000 claims 1
- 230000001900 immune effect Effects 0.000 claims 1
- 239000000975 dye Substances 0.000 description 37
- 239000000243 solution Substances 0.000 description 31
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 30
- 239000002243 precursor Substances 0.000 description 24
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 19
- 230000000694 effects Effects 0.000 description 19
- 238000006243 chemical reaction Methods 0.000 description 14
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 12
- 150000002148 esters Chemical class 0.000 description 12
- 239000000047 product Substances 0.000 description 11
- 230000003505 mutagenic effect Effects 0.000 description 10
- ALYNCZNDIQEVRV-UHFFFAOYSA-N 4-aminobenzoic acid Chemical compound NC1=CC=C(C(O)=O)C=C1 ALYNCZNDIQEVRV-UHFFFAOYSA-N 0.000 description 9
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- 239000000872 buffer Substances 0.000 description 9
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 9
- 238000005259 measurement Methods 0.000 description 9
- WZCQRUWWHSTZEM-UHFFFAOYSA-N 1,3-phenylenediamine Chemical compound NC1=CC=CC(N)=C1 WZCQRUWWHSTZEM-UHFFFAOYSA-N 0.000 description 8
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- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- KKTUQAYCCLMNOA-UHFFFAOYSA-N 2,3-diaminobenzoic acid Chemical compound NC1=CC=CC(C(O)=O)=C1N KKTUQAYCCLMNOA-UHFFFAOYSA-N 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 7
- 230000008018 melting Effects 0.000 description 7
- 238000002844 melting Methods 0.000 description 7
- 230000001590 oxidative effect Effects 0.000 description 7
- CDAWCLOXVUBKRW-UHFFFAOYSA-N 2-aminophenol Chemical compound NC1=CC=CC=C1O CDAWCLOXVUBKRW-UHFFFAOYSA-N 0.000 description 6
- 239000012131 assay buffer Substances 0.000 description 6
- 125000004494 ethyl ester group Chemical group 0.000 description 6
- 210000002966 serum Anatomy 0.000 description 6
- 239000012086 standard solution Substances 0.000 description 6
- 238000010521 absorption reaction Methods 0.000 description 5
- 150000004982 aromatic amines Chemical class 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 238000009835 boiling Methods 0.000 description 5
- 231100000219 mutagenic Toxicity 0.000 description 5
- 239000007800 oxidant agent Substances 0.000 description 5
- 210000002268 wool Anatomy 0.000 description 5
- 0 *C(=O)C1=C(*)C(N)=C([Y])C=C1C Chemical compound *C(=O)C1=C(*)C(N)=C([Y])C=C1C 0.000 description 4
- HEMGYNNCNNODNX-UHFFFAOYSA-N 3,4-diaminobenzoic acid Chemical group NC1=CC=C(C(O)=O)C=C1N HEMGYNNCNNODNX-UHFFFAOYSA-N 0.000 description 4
- PLIKAWJENQZMHA-UHFFFAOYSA-N 4-aminophenol Chemical compound NC1=CC=C(O)C=C1 PLIKAWJENQZMHA-UHFFFAOYSA-N 0.000 description 4
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- QIGBRXMKCJKVMJ-UHFFFAOYSA-N Hydroquinone Chemical compound OC1=CC=C(O)C=C1 QIGBRXMKCJKVMJ-UHFFFAOYSA-N 0.000 description 4
- 125000003118 aryl group Chemical group 0.000 description 4
- 230000008033 biological extinction Effects 0.000 description 4
- 230000000711 cancerogenic effect Effects 0.000 description 4
- 231100000315 carcinogenic Toxicity 0.000 description 4
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 description 4
- 230000032050 esterification Effects 0.000 description 4
- 238000005886 esterification reaction Methods 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 150000002978 peroxides Chemical class 0.000 description 4
- 239000008363 phosphate buffer Substances 0.000 description 4
- WQGWDDDVZFFDIG-UHFFFAOYSA-N pyrogallol Chemical compound OC1=CC=CC(O)=C1O WQGWDDDVZFFDIG-UHFFFAOYSA-N 0.000 description 4
- CBCKQZAAMUWICA-UHFFFAOYSA-N 1,4-phenylenediamine Chemical compound NC1=CC=C(N)C=C1 CBCKQZAAMUWICA-UHFFFAOYSA-N 0.000 description 3
- CWLKGDAVCFYWJK-UHFFFAOYSA-N 3-aminophenol Chemical compound NC1=CC=CC(O)=C1 CWLKGDAVCFYWJK-UHFFFAOYSA-N 0.000 description 3
- JQVAPEJNIZULEK-UHFFFAOYSA-N 4-chlorobenzene-1,3-diol Chemical compound OC1=CC=C(Cl)C(O)=C1 JQVAPEJNIZULEK-UHFFFAOYSA-N 0.000 description 3
- PAYRUJLWNCNPSJ-UHFFFAOYSA-N Aniline Chemical compound NC1=CC=CC=C1 PAYRUJLWNCNPSJ-UHFFFAOYSA-N 0.000 description 3
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- 238000002965 ELISA Methods 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 241001313536 Thermothelomyces thermophila Species 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000005755 formation reaction Methods 0.000 description 3
- 239000000118 hair dye Substances 0.000 description 3
- 230000000984 immunochemical effect Effects 0.000 description 3
- 238000011835 investigation Methods 0.000 description 3
- IOPLHGOSNCJOOO-UHFFFAOYSA-N methyl 3,4-diaminobenzoate Chemical compound COC(=O)C1=CC=C(N)C(N)=C1 IOPLHGOSNCJOOO-UHFFFAOYSA-N 0.000 description 3
- 150000004702 methyl esters Chemical class 0.000 description 3
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- 239000004033 plastic Substances 0.000 description 3
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- GHMLBKRAJCXXBS-UHFFFAOYSA-N resorcinol Chemical compound OC1=CC=CC(O)=C1 GHMLBKRAJCXXBS-UHFFFAOYSA-N 0.000 description 3
- 230000000087 stabilizing effect Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000004809 thin layer chromatography Methods 0.000 description 3
- DLURHXYXQYMPLT-UHFFFAOYSA-N 2-nitro-p-toluidine Chemical compound CC1=CC=C(N)C([N+]([O-])=O)=C1 DLURHXYXQYMPLT-UHFFFAOYSA-N 0.000 description 2
- ZZNAYFWAXZJITH-UHFFFAOYSA-N 4-amino-3-nitrobenzoic acid Chemical class NC1=CC=C(C(O)=O)C=C1[N+]([O-])=O ZZNAYFWAXZJITH-UHFFFAOYSA-N 0.000 description 2
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- 241000231139 Pyricularia Species 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 241000813090 Rhizoctonia solani Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241001557894 Scytalidium sp. Species 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 241000217816 Trametes villosa Species 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- YRRFBANPGRXQNJ-UHFFFAOYSA-M acetyl(trimethyl)azanium;bromide Chemical compound [Br-].CC(=O)[N+](C)(C)C YRRFBANPGRXQNJ-UHFFFAOYSA-M 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 230000004931 aggregating effect Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001448 anilines Chemical class 0.000 description 1
- 239000012062 aqueous buffer Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 235000010233 benzoic acid Nutrition 0.000 description 1
- 150000001558 benzoic acid derivatives Chemical class 0.000 description 1
- 239000007844 bleaching agent Substances 0.000 description 1
- 230000005587 bubbling Effects 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 239000000386 donor Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- NUJBTXFFJUGENN-UHFFFAOYSA-N ethyl 3,4-diaminobenzoate Chemical compound CCOC(=O)C1=CC=C(N)C(N)=C1 NUJBTXFFJUGENN-UHFFFAOYSA-N 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 231100000221 frame shift mutation induction Toxicity 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 210000004919 hair shaft Anatomy 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- 239000000852 hydrogen donor Substances 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 150000002505 iron Chemical class 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 231100000299 mutagenicity Toxicity 0.000 description 1
- 230000007886 mutagenicity Effects 0.000 description 1
- XWLUFINGMMDFPD-UHFFFAOYSA-N naphthalen-1-ol Chemical compound C1=CC=C2C(O)=CC=CC2=C1.C1=CC=C2C(O)=CC=CC2=C1 XWLUFINGMMDFPD-UHFFFAOYSA-N 0.000 description 1
- 150000004780 naphthols Chemical class 0.000 description 1
- 231100001223 noncarcinogenic Toxicity 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- ATGUVEKSASEFFO-UHFFFAOYSA-N p-aminodiphenylamine Chemical compound C1=CC(N)=CC=C1NC1=CC=CC=C1 ATGUVEKSASEFFO-UHFFFAOYSA-N 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000001024 permanent hair color Substances 0.000 description 1
- QWUFXJHVFNRNCU-UHFFFAOYSA-N phenazin-1-amine Chemical compound C1=CC=C2N=C3C(N)=CC=CC3=NC2=C1 QWUFXJHVFNRNCU-UHFFFAOYSA-N 0.000 description 1
- VZPGINJWPPHRLS-UHFFFAOYSA-N phenazine-2,3-diamine Chemical compound C1=CC=C2N=C(C=C(C(N)=C3)N)C3=NC2=C1 VZPGINJWPPHRLS-UHFFFAOYSA-N 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 150000008442 polyphenolic compounds Chemical class 0.000 description 1
- 229920002635 polyurethane Polymers 0.000 description 1
- 239000004814 polyurethane Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 229940079877 pyrogallol Drugs 0.000 description 1
- 230000036632 reaction speed Effects 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 210000004761 scalp Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000002453 shampoo Substances 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 229920002545 silicone oil Polymers 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 238000000870 ultraviolet spectroscopy Methods 0.000 description 1
- 238000002211 ultraviolet spectrum Methods 0.000 description 1
- 231100000925 very toxic Toxicity 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
- A61Q5/10—Preparations for permanently dyeing the hair
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/40—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing nitrogen
- A61K8/44—Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof
- A61K8/445—Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof aromatic, i.e. the carboxylic acid directly linked to the aromatic ring
-
- C—CHEMISTRY; METALLURGY
- C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
- C09B—ORGANIC DYES OR CLOSELY-RELATED COMPOUNDS FOR PRODUCING DYES, e.g. PIGMENTS; MORDANTS; LAKES
- C09B17/00—Azine dyes
- C09B17/02—Azine dyes of the benzene series
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
- D06P1/32—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using oxidation dyes
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/531—Production of immunochemical test materials
- G01N33/532—Production of labelled immunochemicals
- G01N33/535—Production of labelled immunochemicals with enzyme label or co-enzymes, co-factors, enzyme inhibitors or enzyme substrates
Definitions
- the present invention concerns the use of aminobenzoic acid (DABA) as a substitute for e.g. o-phenylendiamine (OPD) in analyses based on peroxidases as well as a dyeing substrate (i.e. a dye precursor) in dyeing compositions, and as an substrate for dyeing natural and synthetic fibres including textiles, thread and yarns.
- DABA aminobenzoic acid
- OPD o-phenylendiamine
- the invention also relates to a composition adapted for dyeing keratinous fibres, e.g. hair, wool, fur and hides, and a method for dyeing such keratinous fibres.
- ELISA Enzyme Linked Immuno Sorbent Assay
- the main principle is that in a much diluted solution many antigens will become bound to the surface of plastic. Thus, if a much diluted solution of antigens is incubated for a time in plastic trays it is possible to wash the cavities in a buffer solution and still retain the film of antigens on the surface of the plastic. If it is required to determine the amount of antibodies in, for instance, serum then the trays with their deposits of antigens are incubated with the serum.
- the antibodies attach themselves to the antigens and, after thorough washing the trays are again incubated this time with a marker, for example anti-immune globulin serum to which there is attached a suitable enzyme by covalent bonding.
- a marker for example anti-immune globulin serum to which there is attached a suitable enzyme by covalent bonding.
- peroxidase is used.
- the peroxidase-marker complex will attach itself to those locations where there is already a deposit of antibodies. After thorough washing to remove all un-combined material the enzyme activity is measured, normally by the use of a suitable colour indicator. Enzyme activity may be determined by the addition of a cromogenetic substrate (i.e. colour producing compound) and hydrogen peroxide. The enzyme catalyses the reduction of the substrate to a coloured compound and the resultant degree of absorbency provides a measure of the enzyme activity. If the serum contains no antibodies there will be no enzyme activity, on the other hand if there is much antibody present there will be very considerable enzyme activity. A standard curve can be drawn showing enzyme activity as a function of the concentration of antibodies. This may be used to estimate the content of antibodies in unknown serum samples by interpolation.
- peroxidase substrates are aromatic amines and include diaminobenziden (DAB), 3,3′-diamino benzid tetra hydrochloride, 3,3′,5,5′-tetra methyl benzidin (TMD).
- DAB diaminobenziden
- TMD 3,3′-diamino benzid tetra hydrochloride
- TMD 3,3′,5,5′-tetra methyl benzidin
- OPD o-phenylendiamine
- OPD In addition to being used as a substrate in immuno-chemical assays OPD is used to dye hair. In this connection too it is desirable to substitute a dangerous material with one less dangerous so that the user is not exposed to danger by coming into contact with it. To protect the hands against the dangerous material it is normal for gloves to be used while the hair dye is being applied. Gloves cannot, of course, protect the scalp of the person to whom the dye is applied.
- the temporary hair dyes are only intended to change the natural hair colour for a short period of time and usually functions by depositing dyes on the surface of the hair. Such hair dyes are easy to remove with normal shampooing.
- the colour of the dyed hair can survive for five or more shampooings. This is achieved by using dyes having a high affinity for hair keratin and which is able penetrate into the interior of the hair shaft.
- Permanent hair dyes are very durable to sunlight, shampooing and other hair treatments and need only to be refreshed once a month as new hair grows out. With these dyeing systems the dyes are created directly in and on the hair.
- Small aromatic colourless dye precursors e.g. p-phenylene-diamine, o-aminophenol, o-phenylendiamine (OPD)
- OPD o-phenylendiamine
- modifiers or couplers
- a number of hair colour tints can be obtained.
- Cathecol and Resorcinol are examples of such modifiers.
- H 2 O 2 is used as the oxidizing agent (colour builder), but also as a bleaching agent.
- Dyeing compositions comprising H 2 O 2 are often referred to as “lightening dyes” due to this lightening effect of H 2 O 2 .
- H 2 O 2 damages the hair. Further, oxidative dyeing often demands high pH (normally around pH 9-10), which also inflicts damage on the hair and on the skin. Consequently, if using dye compositions comprising H 2 O 2 it is not recommendable to dye the hair often.
- U.S. Pat. No. 3,251,742 (Revlon) describes a method for dyeing human hair by dye formation in situ (i.e. on the hair).
- An oxidation enzyme is used for the colour formation reactions at a substantially neutral pH (7-8.5). Laccases, tyrosinases, polyphenolases and catacolases are mentioned as suitable oxidation enzymes.
- the hair colour pigment is formed by controlled oxidation of various quinone-forming compounds and mono or poly aromatic amines having the amino groups on the aromatic rings to form natural appearing pigments.
- dye precursors are 2-amino-4-nitrophenol, p-phenylene diamine, m-phenylene diamine, o-phenylene diamine, 2-amino-1,4-naphthoquenone, m-aminophenol, p-aminophenol, o-aminophenol, 2-amino resorcinol, 1,2,4-benzene triamine, nitro-p-phenylene diamine, 2-amino-5-diethyl amino toluene.
- EP patent no. 504.005 (Perma S.A.) concerns dyeing compositions for keratinous fibres, in particular hair, which do not require the presence of H 2 O 2 (hydrogen peroxide).
- the composition comprises an enzyme capable of catalysing the formation of the polymeric dyes and also dye precursors, such as bases and couplers, in a buffer solution wherein the pH of said composition is between 6.5 and 8 and said enzyme has an optimal activity in the pH range between 6.5 and 8.
- Rhizoctonia praticola laccase and Rhus vernicifera laccase are exemplified as the oxidation enzyme to oxidize the dye precursor(s).
- dye precursors are specifically mentioned: p-phenylene diamine, o-aminophenol, p-methylaminophenol, p-aminophenol, p-toluylenediamine and N-phenyl-p-phenylene diamine.
- the aim of the present invention is to use the present findings to make available a substrate which to all intents and purposes is non-toxic, non-mutagenic and/or non-carcinogenic and which may be used in immuno-chemical assays, for the dying of keratinous fibres, in particular hair and for dying both natural and synthetic fibres, e.g. textiles.
- This aim is achieved by utilising the discovery of a substrate which includes the group with the general formulae shown in 1.
- R is an amino, mono- or a distributed amino or OR′, where R is H, alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl or substituted phenyl.
- X, Y and Z may each be any one of the following: alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl, substituted phenyl, amino, hydroxy or mercapto with the proviso that at least one of the groups X, Y and Z is an amino group or an amino salt.
- a substrate is made available which includes a connection with formula 1 where R′ is a methyl, ethyl or isopropyl group.
- the substrate is a benzoic acid ester, in particular 3,4-diaminobenzoic acid methyl ester (DABA-Me), 3,4-diaminibenzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester.
- DABA-Me 3,4-diaminobenzoic acid methyl ester
- ethyl ester 3,4-diaminibenzoic acid ethyl ester
- 3,4-diamino benzoic acid isopropyl ester isopropyl ester.
- PABA p-amino benzoic acid
- 3,4-DABA is a considerably poorer substrate for peroxidase than is OPD.
- 3,4-DABA has a higher K m -value at the same V max when compared with OPD.
- This effect can be countered by modifying the carboxyl group, for example by esterification with an alcohol.
- the preferred alcohols are methanol, ethanol and isopropanol.
- Methyl, ethyl and isopropyl esters were examined in connection with enzymes and the materials were shown to have significantly improved properties than 3,4-DABA.
- ethyl ester was found to have a very high V max , i.e. at the same concentration it gives a very much higher reaction speed than OPD.
- the product of oxidation is also an amino phenazine.
- the oxidation product is 4,7-dicarboxy-1,2-diamino phenazine as shown in the following equation.
- the substrate should have two amino groups at the 3,4-location for the reaction to take place.
- substrates which have the amino groups at either the 2,3-location or the 2,3,4-location may be used but only if the carboxyl group does not hinder the reaction.
- Substrates which have the amino group at the para location may also be used to produce a coloured product.
- An example of this is 3,6-DABA.
- Compounds with the general formulae 1 are preferably dissolved in DMF (Dimethyl formamide) but other organic solvents may be used for this purpose. If a compound with the general formulae 1 is in the form of a salt it can be dissolved in water and this is preferred when using organic solvents.
- DMF Dimethyl formamide
- the invention in another aspect relates to a method for quantitative and/or qualitative analysis of a material of biological interest.
- a peroxidase enzyme together with a marker is bound to the compound in question.
- Hydrogen peroxide is then converted with a cromogenetic substrate (i.e. colour forming compound) in the presence of the peroxidase, the substrate includes a bond with the general formulae 1.
- one of the following substrates are used: the methyl, propyl or isopropyl ester of amino benzoic acid.
- the coloured product produced by the method of the invention is especially suited to the dying of textiles, thread, yarn, wool, hides and skins and human hair.
- Other natural fibres such as cotton and silk may also be dyed with the product as may synthetic fibres such as polyamides, polyurethane and polyester.
- the coloured product may either be made immediately before it is to be used for dying or it may be synthesised in the immediate vicinity of the substance to be dyed. For example this may be done by mixing the substrate and the oxidation system in a person's hair.
- the dying process may be carried out rinsing the person's hair with a mixture of the substrate of the invention and hydrogen peroxide or an oxidation enzyme. A peroxidase is then added and distributed in the hair. When the desired degree of colouring has been obtained the hair is rinsed with water.
- the substrate may be mixed with the oxidation system before it is applied to the hair.
- the substrate may be oxidised with hydrogen peroxide or an oxidation enzyme generating hydrogen peroxidase in the presence of a peroxidase.
- Peroxidases belongs to the group of enzymes which is known as the oxidoreductases.
- the group also includes the classes of enzymes dehydrogenase, oxygenase, oxidase, laccase and related enzymes. These enzymes may also be used for as an oxidation system/agent for e.g. dyeing keratinous fibres, such as hair, wool, fur and hides and the like. Dyeing composition and preferred oxidation enzymes will be described further below.
- oxygen donor is hydrogen peroxide which is used as an electron acceptor.
- Oxidases employ oxygen as an electron acceptor.
- Suitable oxidases include catecholoxidase, laccase and o-amino phenoloxidase.
- Oxidation systems which may be used for the oxidation of the substrate in this connection therefore include peroxidase and hydrogen peroxide as well as oxidases, laccases and related enzymes and oxygen.
- peroxidase and hydrogen peroxide as well as oxidases, laccases and related enzymes and oxygen.
- oxygen When the system consists of only an oxidase and oxygen it is only necessary to add the oxidase to the substrate as the oxygen in the air is used as an oxidant.
- the invention relates to a composition in particular adapted for dyeing keratinous fibres comprises, e.g. hair, fur, hide or wool.
- a composition in particular adapted for dyeing keratinous fibres comprises, e.g. hair, fur, hide or wool.
- a preferred use of the composition is as a permanent dye for the dyeing of human hair.
- the oxidation enzyme is as also indicated above an oxidoreductase, i.e. an enzyme classified under the Enzyme Classification number E.C. 1 (Oxidoreductases) in accordance with the Recommendations (1992) of the International Union of Biochemistry and Molecular Biology (IUBMB)) which catalyses oxidoreduction reactions.
- E.C. 1 Oxidoreductases
- oxidoreductase enzymes which catalyse the oxidation of a substrate (an electron or hydrogen donor) by acting on oxygen (O 2 ) and/or a peroxide as the acceptor.
- Such enzymes include enzymes classified within the enzyme classes comprising oxidases, including E.C. 1.1.3. E.C. 1.2.3, E.C. 1.3.3, E.C. 1.4.3, E.C. 1.5.3, E.C. 1.7.3, E.C. 1.8.3 and E.C. 1.9.3, laccases and related enzymes in E.C. 1.10.3, and peroxidases in E.C. 1.11.
- Laccases or related enzymes which act on molecular oxygen and yield water (H 2 O) without any need for peroxide (e.g. H 2 O 2 ),
- Oxidases which act on molecular oxygen (O 2 ) and yield peroxide (H 2 O 2 ), and
- Peroxidases which act on peroxide (e.g. H 2 O 2 ) and yield water (H 2 O).
- enzyme systems which comprise a combination of more than one enzyme from a single class or from different classes among the three types of enzymes are contemplated.
- a single enzyme for the sake of simplicity, it is to be understood that the description is generally applicable to such combinations of more than one enzyme.
- the invention is generally described in terms of the preferred aspect relating to the dyeing of hair, it is to be understood that the description is generally applicable to compositions according to the invention adapted for dyeing of other types of keratinous fibres.
- laccases and related enzymes are laccases and related enzymes, the term “laccases and related enzymes” including enzymes comprised by the enzyme classification E.C. 1.10.3.2 (laccases) and catechol oxidase enzymes comprised by E.C. 1.10.3.1, bilirubin oxidase enzymes comprised by the enzyme classification E.C. 1.3.3.5 and mono-phenol mono-oxygenase enzymes comprised by the enzyme classification E.C. 1.14.99.1. Laccases are multi-copper containing enzymes that catalyze the oxidation of phenols and aromatic amines.
- Laccase-mediated oxidation results in the production of aryloxy-radical intermediates from suitable phenolic substrates; the ultimate coupling of the intermediates so produced provides a combination of dimeric, oligomeric, and polymeric reaction products. Certain reaction products can be used to form dyes suitable for dyeing hair.
- the laccase employed may be derived from a strain of Polyporus sp., in particular a strain of P. pinsitus or P. versicolor , a strain of Myceliophthora sp., e.g. M. thermophila, a strain of Rhizoctonia sp., in particular a strain of Rh. praticola or Rh. solani, a strain of a Rhus sp., in particular Rhus vernicifera, a strain of Pyricularia sp, in particular P. oryzae, or a strain of Scytalidium, such as S. thermophilium.
- the oxidoreductase is a laccase such as a Polyporus sp. laccase, especially the Polyporus pinisitus laccase (also called Trametes villosa laccase) described in WO 96/00290 (from Novo Nordisk Biotec Inc.) or a Myceliophthora sp. laccase, especially the Myceliophthora thermophila laccase described in WO 95/33836 (from Novo Nordisk Biotech Inc.).
- a laccase such as a Polyporus sp. laccase, especially the Polyporus pinisitus laccase (also called Trametes villosa laccase) described in WO 96/00290 (from Novo Nordisk Biotec Inc.) or a Myceliophthora sp. laccase, especially the Myceliophthora thermophila laccase described in WO 95/33836 (from Novo Nordisk Biotech Inc.).
- the laccase may be a Scytalidium sp. laccase such as the S. thermophilium laccase described in WO 95/33837 and WO 97/19998 (from Novo Nordisk Biotech Inc.), the contents of which is incorporated herein by reference, or a Pyricularia sp. laccase, such as the Pyricularia oryzae laccase which can be purchased from SIGMA under the trade name SIGMA No. L5510, or a Coprinus sp. laccase, such as a C. cinereus laccase, especially a C. cinereus IFO 30116 laccase, or a Rhizoctonia sp. laccase, such as a Rh. solani laccase, especially the neutral Rh. solani laccase described WO 95/07988 (from Novo Nordisk A/S) having a pH optimum in the range from 6.0 to 8.5.
- a Pyricularia sp. laccase such as the Pyricularia oryzae laccase which can be
- the laccase may also be derived from a fungus such as Collybia, Fomes, Lentinus, Pleurotus, Aspergillus, Neurospora, Podospora, Phlebia, e.g. P. radiata (WO 92/01046), Coriolus sp., e.g. C. hirsitus (JP 2-238885), or Botrytis.
- a fungus such as Collybia, Fomes, Lentinus, Pleurotus, Aspergillus, Neurospora, Podospora, Phlebia, e.g. P. radiata (WO 92/01046), Coriolus sp., e.g. C. hirsitus (JP 2-238885), or Botrytis.
- Bilirubin oxidase may preferably be derived from a strain of Myrothecium sp., such as M. verrucaria.
- the substrates i.e. dye precursors
- the substrates may according to the dyeing composition of the invention be any of the above within the definition of the general formulae 1.
- Preferred dye precursors are benzoic acid esters, especially diamino benzoic acid esters, in particular 3,4-diamino benzoic acid methyl ester (DABA-Me), 3,4-diamino benzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester.
- DABA-Me 3,4-diamino benzoic acid methyl ester
- ethyl ester 3,4-diamino benzoic acid isopropyl ester.
- the substrate may also be oxidised by a number of inorganic compounds, among these are compounds which include hypochlorite (ClO ⁇ ), hypobromite (BrO ⁇ ), permanganate (MnO 4 ⁇ ) dicromate (Cr 2 O 7 2 ⁇ ) and the iron ion (Fe 3+ ).
- inorganic compounds among these are compounds which include hypochlorite (ClO ⁇ ), hypobromite (BrO ⁇ ), permanganate (MnO 4 ⁇ ) dicromate (Cr 2 O 7 2 ⁇ ) and the iron ion (Fe 3+ ).
- Oxidation systems are taken to be either an oxidant per se or a combination of an enzyme and an oxidant.
- Modifiers typically incorporation in a dye compositions include m-aromatic diamines, m-aminophenols, polyphenols, amino naphthalines or naphthols.
- the modifier reacts with the dye precursor in the presence of the oxidative enzyme or the like, converting it into a coloured compound.
- Couplers examples include m-phenylene-diamine, 2,4-diaminoanisole, 1-hydroxynaphthalene ( ⁇ -naphthol), 1,4-dihydroxybenzene(hydroquinone), 1,5-dihydroxynapthalene, 1,2-dihydroxybenzene(pyrocatechol), 1,3-dihydroxybenzene (resorcinol), 1,3-dihydroxy-2-methylbenzene, 1,3-dihydroxy-4-chlorobenzene(4-chlororesorcinol), 1,2,3,trihydroxybenzene, 1,2,4-trihydroxybenzene, 1,2,4-trihydroxy-5-methylbenzene, and 1,2,4-trihydroxytoluene.
- the invention relates to a method for dyeing keratinous fibres, in particular hair, fur, hide and wool, using a composition as described above.
- the dyeing method can be conducted with one or more dye precursors (i.e. substrates of the invention) and optionally in combination with one or more modifiers.
- the amount of dye precursor(s) and other ingredients used in the composition of the invention for this purpose are in accordance with usual commercial amounts and therefore known for the skilled person.
- Hair dyeing is typically carried out at or near room temperature, preferably around the optimum temperature of the enzyme being used, and at a pH in the range of from 3.0 to 9.0, preferably 4.0 to 8.5, especially 6.0 to 8.0.
- Dye precursors (i.e. substrates of the invention) and optional modifiers are described above.
- esters were made starting from 4-amino-3-nitrotoluene, followed by the esterification and reduction of 4-amino-3-nitrobenzoicacid esters to 3,4-diamino benzoic acidester. The reactions are shown below.
- methyl ester may be prepared by bubbling hydrochloric acid gas through a solution of 3,4-DABA containing methanol. This last method finds only limited use in the production of the ethyl ester and cannot be used to produce the isopropyl ester.
- UV spectra were taken of OPD as well as the methyl, ethyl and isopropyl esters.
- esters absorb at the same wavelength. At 237.5 nm there is a slight increase in extinction with increasing molecular weight of the alkyl group. 3,4-DABA-esters show a typical maximum at 277.5 nm. This maximum is not found in OPD because of the ester carbonyl group.
- Absorbancy at 492 nm was used as a measure of the course of the reaction. The initial velocity was taken to be the absorbancy at 492 nm two minutes after the addition of the peroxidase to a mixture of the substrate and hydrogen peroxide in a buffer with a pH of 5.0.
- the wavelength of 492 nm was chosen because it is employed in the standard assay procedures for OPD. None of the substrates has a specially high absorption at this wavelength.
- V init V max 1 + K m [ S ]
- K m is defined as the concentration of the substrate at V max /2. A small K m value will therefore be characteristic for an enzyme system where a low concentration of the substrates produces saturation of the enzyme.
- the peroxidase system has an extremely complicated energy balance (Arnoa et al. (1990)) for short periods of less than a minute the system may nevertheless be described in terms of the above given formulae.
- a 50 mM phosphate/citrate buffer with a pH of 5.0 was made by mixing a 50 mm Na 2 HPO 4 solution and a 50 mm solution of citric acid. The pH was measured while mixing was in progress.
- the stabilizing buffer for peroxidase i.e. a buffer which stabilizes the enzyme, was prepared according to the method of Olsen and Little (1983). A 0.1M Na-acetate buffer, which was 0.5M in terms of CaCl 2 was adjusted to pH 5.6.
- the standard peroxidase solution was diluted to 1:1000 with the 10 ml assay-buffer solution in 10 ⁇ l standard solution.
- the standard solutions were diluted by 1:10 with the assay buffer. Before being used the substrate solutions were diluted by 1:10. 0.5 ml of the standard solution was thinned down with 4.5 ml of the assay buffer.
- the total volume is then as follows: 300 ⁇ I DMF and substrate solution, 1550 ⁇ l buffer, 100 ⁇ l bench solution of peroxidase and 50 ⁇ l hydrogen peroxide solution. That is 2000 ⁇ l in total.
- TABLE 4 Substrate ⁇ l substrate ⁇ l 10% DMF- concentration solution solution ( ⁇ mol/l) 0 300 0 5 295 25 10 290 50 15 285 75 20 280 100 25 275 125 30 270 150 35 265 175 40 260 200 50 250 250 60 240 300 80 220 400 100 200 500 150 150 750 200 100 1000 300 0 1500
- Table 5 contains information about the values measured for K m , V max and K kat for the five compounds. TABLE 5 K m V max K kat Substrate ( ⁇ mol/ ⁇ l) (min ⁇ 1 ) (1*mol ⁇ 1 *min ⁇ 1 ) OPD 47.35 0.16 1.6 * 10 8 3,4-DABA 251.22 0.20 2.0 * 10 8 methyl 125.97 0.22 2.2 * 10 8 ester ethyl 212.39 0.27 2.7 * 10 8 ester isopropyl 118.46 0.22 2.2 * 10 8 ester
- FIG. 1 +L-5 is a graphic representation of the result of the measurement of initial velocity on OPD, 3,4-DABA, 3,4-DABA-methyl ester, 3,4-DABA-ethyl ester, 3,4-DABA-isopropyl ester.
- the Ames test (Maron and Ames (1983)) was used to determine the mutagenic properties of the compounds. Nutrient media were prepared in the manner described by Venitt and Parry (1984). To 3 ⁇ 2 ml melted agar at 45° C. were added 100 ⁇ l of 50, 100 and 200 mM of solutions of the compounds dissolved in DMSO. By means of a pipette 100 ⁇ l of a well-grown culture of Salmonella tphimurium TA 98 (BIO-TEST gl. skolevej 47, 6731 Tiaereborg) were added to the same test-tube.
- the bacteria contain a frameshift mutation on the histinol-dehydrogenase gene and require histidin in order to grow. Mutagenic aromatic amines can cause the bacteria to mutate to His+ and they can then grow on the nutrient medium. The number of colonies after incubation therefore give a quantitative measure of the ability of the added compound to cause mutation. In all trials spontaneous mutations take place in the absence of a mutagen. These provide a measure of “background” mutation.
- OPD is not a direct mutagen, it must first be activated by the liver enzyme system P450. All trials were therefore carried out both with and without the addition of “S9-mix” from the livers of rats, this contains the P450 system. 0.5 ml of “59-mix” was added to each test-tube. The criteria for mutation are that increasing concentrations of the compound under investigation give a marked increase in the number of His+ mutants. The results of these trial are given in FIG. 7 +L-11. It may be seen from this figure that only OPD has mutagenic properties.
- Dye precursor solutions were prepared by mixing the indicated modifier so that the final concentration in the dyeing solution was 0.1% w/w with respect to dye precursor (i.e. substrate of the invention) and 0.1% w/w with respect to modifier.
- the hair tresses were then rinsed with running water, washed with shampoo, rinsed with water, combed, and air dried.
- the keratinous fibers can be dyed using DABA-Me and a modifier.
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Abstract
Description
- The present invention concerns the use of aminobenzoic acid (DABA) as a substitute for e.g. o-phenylendiamine (OPD) in analyses based on peroxidases as well as a dyeing substrate (i.e. a dye precursor) in dyeing compositions, and as an substrate for dyeing natural and synthetic fibres including textiles, thread and yarns. The invention also relates to a composition adapted for dyeing keratinous fibres, e.g. hair, wool, fur and hides, and a method for dyeing such keratinous fibres.
- Immuno-chemical Assays
- Several different substrates are known in the part to be used for enzyme systems in connection with peroxidase-based immuno- hemical assays, for example ELISA. These substrates are often toxic, mutagenic or carcinogenic.
- ELISA (Enzyme Linked Immuno Sorbent Assay) is a method used to assess the amount of antibody in serum. The main principle is that in a much diluted solution many antigens will become bound to the surface of plastic. Thus, if a much diluted solution of antigens is incubated for a time in plastic trays it is possible to wash the cavities in a buffer solution and still retain the film of antigens on the surface of the plastic. If it is required to determine the amount of antibodies in, for instance, serum then the trays with their deposits of antigens are incubated with the serum. The antibodies attach themselves to the antigens and, after thorough washing the trays are again incubated this time with a marker, for example anti-immune globulin serum to which there is attached a suitable enzyme by covalent bonding. In this particular case peroxidase is used.
- The peroxidase-marker complex will attach itself to those locations where there is already a deposit of antibodies. After thorough washing to remove all un-combined material the enzyme activity is measured, normally by the use of a suitable colour indicator. Enzyme activity may be determined by the addition of a cromogenetic substrate (i.e. colour producing compound) and hydrogen peroxide. The enzyme catalyses the reduction of the substrate to a coloured compound and the resultant degree of absorbency provides a measure of the enzyme activity. If the serum contains no antibodies there will be no enzyme activity, on the other hand if there is much antibody present there will be very considerable enzyme activity. A standard curve can be drawn showing enzyme activity as a function of the concentration of antibodies. This may be used to estimate the content of antibodies in unknown serum samples by interpolation.
- Many of the peroxidase substrates are aromatic amines and include diaminobenziden (DAB), 3,3′-diamino benzid tetra hydrochloride, 3,3′,5,5′-tetra methyl benzidin (TMD). Another peroxidase substrate, which does not belong to the group of aromatic amines, is 2,2-azino-di (3-ethyl-benzo thiazolin-6-sulphonic acid) (ABTS), this has been used as a standard for the establishment of the activity of peroxidase preparations. According to Voogd, Van der Stel and Jacobs (1980) this material is also a mutagent.
- o-phenylendiamine (OPD) is another peroxidase substrate which is widely used in hospital and development laboratories. OPD is known to be both mutagenic and carcinogenic.
- The staff of laboratories in which analyses involving the use of toxic, mutagenic or carcinogenic materials are carried out are exposed to a significant degree of risk of coming into direct contact with these materials. In order to provide a safe working environment considerable efforts are now made to substitute these dangerous materials with less dangerous ones.
- Hair Dyeing Composition
- In addition to being used as a substrate in immuno-chemical assays OPD is used to dye hair. In this connection too it is desirable to substitute a dangerous material with one less dangerous so that the user is not exposed to danger by coming into contact with it. To protect the hands against the dangerous material it is normal for gloves to be used while the hair dye is being applied. Gloves cannot, of course, protect the scalp of the person to whom the dye is applied.
- In general hair dyeing compositions on the market today can be divided into three main groups:
- temporary hair dyes,
- semi-permanent hair dyes, and
- permanent oxidative hair dyes.
- The temporary hair dyes are only intended to change the natural hair colour for a short period of time and usually functions by depositing dyes on the surface of the hair. Such hair dyes are easy to remove with normal shampooing.
- When using semi-permanent hair dyes the colour of the dyed hair can survive for five or more shampooings. This is achieved by using dyes having a high affinity for hair keratin and which is able penetrate into the interior of the hair shaft.
- Permanent hair dyes are very durable to sunlight, shampooing and other hair treatments and need only to be refreshed once a month as new hair grows out. With these dyeing systems the dyes are created directly in and on the hair. Small aromatic colourless dye precursors (e.g. p-phenylene-diamine, o-aminophenol, o-phenylendiamine (OPD)) penetrate deep into the hair where said dye precursors are oxidised by an oxidising agent into coloured polymeric compounds. These coloured compounds are larger than the dye precursors and can not be washed out of the hair.
- By including compounds referred to as modifiers (or couplers) in the hair dyeing composition a number of hair colour tints can be obtained. Cathecol and Resorcinol are examples of such modifiers.
- Some of the today most widely used dye precursors such as OPD are known to be both mutagenic and carcinogenic.
- Further, traditionally H2O2 is used as the oxidizing agent (colour builder), but also as a bleaching agent. Dyeing compositions comprising H2O2 are often referred to as “lightening dyes” due to this lightening effect of H2O2.
- The use of H2O2 in dyeing compositions have some disadvantages as H2O2 damages the hair. Further, oxidative dyeing often demands high pH (normally around pH 9-10), which also inflicts damage on the hair and on the skin. Consequently, if using dye compositions comprising H2O2 it is not recommendable to dye the hair often.
- To overcome the disadvantages of using H2O2 it has been suggested to use oxidation enzymes to replace H2O2.
- U.S. Pat. No. 3,251,742 (Revlon) describes a method for dyeing human hair by dye formation in situ (i.e. on the hair). An oxidation enzyme is used for the colour formation reactions at a substantially neutral pH (7-8.5). Laccases, tyrosinases, polyphenolases and catacolases are mentioned as suitable oxidation enzymes. The hair colour pigment is formed by controlled oxidation of various quinone-forming compounds and mono or poly aromatic amines having the amino groups on the aromatic rings to form natural appearing pigments. Specifically mentioned dye precursors are 2-amino-4-nitrophenol, p-phenylene diamine, m-phenylene diamine, o-phenylene diamine, 2-amino-1,4-naphthoquenone, m-aminophenol, p-aminophenol, o-aminophenol, 2-amino resorcinol, 1,2,4-benzene triamine, nitro-p-phenylene diamine, 2-amino-5-diethyl amino toluene.
- EP patent no. 504.005 (Perma S.A.) concerns dyeing compositions for keratinous fibres, in particular hair, which do not require the presence of H2O2 (hydrogen peroxide). The composition comprises an enzyme capable of catalysing the formation of the polymeric dyes and also dye precursors, such as bases and couplers, in a buffer solution wherein the pH of said composition is between 6.5 and 8 and said enzyme has an optimal activity in the pH range between 6.5 and 8. Rhizoctonia praticola laccase and Rhus vernicifera laccase are exemplified as the oxidation enzyme to oxidize the dye precursor(s). The following dye precursors are specifically mentioned: p-phenylene diamine, o-aminophenol, p-methylaminophenol, p-aminophenol, p-toluylenediamine and N-phenyl-p-phenylene diamine.
- The aim of the present invention is to use the present findings to make available a substrate which to all intents and purposes is non-toxic, non-mutagenic and/or non-carcinogenic and which may be used in immuno-chemical assays, for the dying of keratinous fibres, in particular hair and for dying both natural and synthetic fibres, e.g. textiles. This aim is achieved by utilising the discovery of a substrate which includes the group with the general formulae shown in 1.
- wherein
- R is an amino, mono- or a distributed amino or OR′, where R is H, alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl or substituted phenyl. X, Y and Z may each be any one of the following: alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl, substituted phenyl, amino, hydroxy or mercapto with the proviso that at least one of the groups X, Y and Z is an amino group or an amino salt.
- In a special embodiment of the invention a substrate is made available which includes a connection with formula 1 where R′ is a methyl, ethyl or isopropyl group.
- In an preferred embodiment the substrate is a benzoic acid ester, in particular 3,4-diaminobenzoic acid methyl ester (DABA-Me), 3,4-diaminibenzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester.
- Comparison of the very toxic aniline with the carboxyl acid derivative of aniline, p-amino benzoic acid (PABA) shows that the toxicity of the molecule is radically altered by the addition of the carboxyl group. PABA is generally considered to be non-toxic and, among other applications, is used as an ultra violet filter in sun lotions. If the substrate OPD is thought of along the same lines it can be seen that a possible analogue is 3,4-diamino benzoic acid (3,4-DABA). This material is comparatively cheap and readily obtainable.
- Investigation using enzymes showed that 3,4-DABA is a considerably poorer substrate for peroxidase than is OPD. In other words 3,4-DABA has a higher Km-value at the same Vmax when compared with OPD. This is apparently due to the carboxyl group's inductive (deactivating) effect upon the aromatic ring. This effect can be countered by modifying the carboxyl group, for example by esterification with an alcohol. The preferred alcohols are methanol, ethanol and isopropanol. Methyl, ethyl and isopropyl esters were examined in connection with enzymes and the materials were shown to have significantly improved properties than 3,4-DABA. Especially the ethyl ester was found to have a very high Vmax, i.e. at the same concentration it gives a very much higher reaction speed than OPD.
-
- It may be seen from this that the product of oxidation is 2,3-diamino phenazin.
-
- The substrate should have two amino groups at the 3,4-location for the reaction to take place. However, substrates which have the amino groups at either the 2,3-location or the 2,3,4-location may be used but only if the carboxyl group does not hinder the reaction.
- Substrates which have the amino group at the para location may also be used to produce a coloured product. An example of this is 3,6-DABA.
- In order to counteract the carboxyl groups inductive effect (i.e. deactivation of the aromatic ring caused by the groups attractive effect upon electrons) esterification of the carboxyl group was investigated using electron donating groups to see if deactivation could be counteracted while at the same time retaining non-mutagenic attributes. To investigate the effect of different alkyl groups on the material's enzymatic properties as well as possible mutagenic properties the methyl, ethyl and isopropyl esters of 3,4-DABA were synthesised.
- Compounds with the general formulae 1 are preferably dissolved in DMF (Dimethyl formamide) but other organic solvents may be used for this purpose. If a compound with the general formulae 1 is in the form of a salt it can be dissolved in water and this is preferred when using organic solvents.
- In another aspect the invention relates to a method for quantitative and/or qualitative analysis of a material of biological interest. In this case a peroxidase enzyme together with a marker is bound to the compound in question. Hydrogen peroxide is then converted with a cromogenetic substrate (i.e. colour forming compound) in the presence of the peroxidase, the substrate includes a bond with the general formulae 1.
- In a preferred embodiment of the method of the invention one of the following substrates are used: the methyl, propyl or isopropyl ester of amino benzoic acid.
- In those cases where the material of biological interest is an antigen the associated antibody is used. In this connection other combinations will suggest themselves to the skilled person.
- The coloured product produced by the method of the invention is especially suited to the dying of textiles, thread, yarn, wool, hides and skins and human hair. Other natural fibres such as cotton and silk may also be dyed with the product as may synthetic fibres such as polyamides, polyurethane and polyester.
- The coloured product may either be made immediately before it is to be used for dying or it may be synthesised in the immediate vicinity of the substance to be dyed. For example this may be done by mixing the substrate and the oxidation system in a person's hair.
- The dying process may be carried out rinsing the person's hair with a mixture of the substrate of the invention and hydrogen peroxide or an oxidation enzyme. A peroxidase is then added and distributed in the hair. When the desired degree of colouring has been obtained the hair is rinsed with water.
- The substrate may be mixed with the oxidation system before it is applied to the hair. As stated above the substrate may be oxidised with hydrogen peroxide or an oxidation enzyme generating hydrogen peroxidase in the presence of a peroxidase.
- Peroxidases belongs to the group of enzymes which is known as the oxidoreductases. The group also includes the classes of enzymes dehydrogenase, oxygenase, oxidase, laccase and related enzymes. These enzymes may also be used for as an oxidation system/agent for e.g. dyeing keratinous fibres, such as hair, wool, fur and hides and the like. Dyeing composition and preferred oxidation enzymes will be described further below.
- In oxidation reactions which are catalysed by the enzyme peroxidase the oxygen donor is hydrogen peroxide which is used as an electron acceptor. Oxidases employ oxygen as an electron acceptor.
- Examples of suitable oxidases include catecholoxidase, laccase and o-amino phenoloxidase.
- Oxidation systems which may be used for the oxidation of the substrate in this connection therefore include peroxidase and hydrogen peroxide as well as oxidases, laccases and related enzymes and oxygen. When the system consists of only an oxidase and oxygen it is only necessary to add the oxidase to the substrate as the oxygen in the air is used as an oxidant.
- Dyeing Composition
- In an aspect the invention relates to a composition in particular adapted for dyeing keratinous fibres comprises, e.g. hair, fur, hide or wool. Comprising 1) at least one oxidation enzyme 2) at least one substrate as defined by the formulae 1 and optionally 3) at least one modifier.
- A preferred use of the composition is as a permanent dye for the dyeing of human hair.
- The oxidation enzyme is as also indicated above an oxidoreductase, i.e. an enzyme classified under the Enzyme Classification number E.C. 1 (Oxidoreductases) in accordance with the Recommendations (1992) of the International Union of Biochemistry and Molecular Biology (IUBMB)) which catalyses oxidoreduction reactions.
- Within the class of oxidoreductase enzymes are preferred enzymes which catalyse the oxidation of a substrate (an electron or hydrogen donor) by acting on oxygen (O2) and/or a peroxide as the acceptor. Such enzymes include enzymes classified within the enzyme classes comprising oxidases, including E.C. 1.1.3. E.C. 1.2.3, E.C. 1.3.3, E.C. 1.4.3, E.C. 1.5.3, E.C. 1.7.3, E.C. 1.8.3 and E.C. 1.9.3, laccases and related enzymes in E.C. 1.10.3, and peroxidases in E.C. 1.11.
- According to the invention three types of oxidoreductases are specifically contemplated:
- a) Laccases or related enzymes, which act on molecular oxygen and yield water (H2O) without any need for peroxide (e.g. H2O2),
- b) Oxidases, which act on molecular oxygen (O2) and yield peroxide (H2O2), and
- c) Peroxidases, which act on peroxide (e.g. H2O2) and yield water (H2O).
- Also, enzyme systems which comprise a combination of more than one enzyme from a single class or from different classes among the three types of enzymes are contemplated. In the present specification, although reference will often be made to a single enzyme for the sake of simplicity, it is to be understood that the description is generally applicable to such combinations of more than one enzyme. Further, although the invention is generally described in terms of the preferred aspect relating to the dyeing of hair, it is to be understood that the description is generally applicable to compositions according to the invention adapted for dyeing of other types of keratinous fibres.
- Particularly preferred enzymes are laccases and related enzymes, the term “laccases and related enzymes” including enzymes comprised by the enzyme classification E.C. 1.10.3.2 (laccases) and catechol oxidase enzymes comprised by E.C. 1.10.3.1, bilirubin oxidase enzymes comprised by the enzyme classification E.C. 1.3.3.5 and mono-phenol mono-oxygenase enzymes comprised by the enzyme classification E.C. 1.14.99.1. Laccases are multi-copper containing enzymes that catalyze the oxidation of phenols and aromatic amines. Laccase-mediated oxidation results in the production of aryloxy-radical intermediates from suitable phenolic substrates; the ultimate coupling of the intermediates so produced provides a combination of dimeric, oligomeric, and polymeric reaction products. Certain reaction products can be used to form dyes suitable for dyeing hair.
- Preferably, the laccase employed may be derived from a strain of Polyporus sp., in particular a strain ofP. pinsitus or P. versicolor, a strain of Myceliophthora sp., e.g. M. thermophila, a strain of Rhizoctonia sp., in particular a strain of Rh. praticola or Rh. solani, a strain of a Rhus sp., in particular Rhus vernicifera, a strain of Pyricularia sp, in particular P. oryzae, or a strain of Scytalidium, such as S. thermophilium.
- In specific embodiments of the invention the oxidoreductase is a laccase such as a Polyporus sp. laccase, especially thePolyporus pinisitus laccase (also called Trametes villosa laccase) described in WO 96/00290 (from Novo Nordisk Biotec Inc.) or a Myceliophthora sp. laccase, especially the Myceliophthora thermophila laccase described in WO 95/33836 (from Novo Nordisk Biotech Inc.).
- Further, the laccase may be a Scytalidium sp. laccase such as theS. thermophilium laccase described in WO 95/33837 and WO 97/19998 (from Novo Nordisk Biotech Inc.), the contents of which is incorporated herein by reference, or a Pyricularia sp. laccase, such as the Pyricularia oryzae laccase which can be purchased from SIGMA under the trade name SIGMA No. L5510, or a Coprinus sp. laccase, such as a C. cinereus laccase, especially a C. cinereus IFO 30116 laccase, or a Rhizoctonia sp. laccase, such as a Rh. solani laccase, especially the neutral Rh. solani laccase described WO 95/07988 (from Novo Nordisk A/S) having a pH optimum in the range from 6.0 to 8.5.
- The laccase may also be derived from a fungus such as Collybia, Fomes, Lentinus, Pleurotus, Aspergillus, Neurospora, Podospora, Phlebia, e.g.P. radiata (WO 92/01046), Coriolus sp., e.g. C. hirsitus (JP 2-238885), or Botrytis.
- Bilirubin oxidase may preferably be derived from a strain of Myrothecium sp., such asM. verrucaria.
- The substrates (i.e. dye precursors) may according to the dyeing composition of the invention be any of the above within the definition of the general formulae 1.
- Preferred dye precursors (i.e. substrates) are benzoic acid esters, especially diamino benzoic acid esters, in particular 3,4-diamino benzoic acid methyl ester (DABA-Me), 3,4-diamino benzoic acid ethyl ester and 3,4-diamino benzoic acid isopropyl ester.
- Other Oxidation Agents
- The substrate may also be oxidised by a number of inorganic compounds, among these are compounds which include hypochlorite (ClO−), hypobromite (BrO−), permanganate (MnO4 −) dicromate (Cr2O7 2−) and the iron ion (Fe3+).
- Oxidation systems are taken to be either an oxidant per se or a combination of an enzyme and an oxidant.
- Modifiers
- Modifiers typically incorporation in a dye compositions include m-aromatic diamines, m-aminophenols, polyphenols, amino naphthalines or naphthols. The modifier (coupler) reacts with the dye precursor in the presence of the oxidative enzyme or the like, converting it into a coloured compound. Examples of specific modifiers (couplers) include m-phenylene-diamine, 2,4-diaminoanisole, 1-hydroxynaphthalene (α-naphthol), 1,4-dihydroxybenzene(hydroquinone), 1,5-dihydroxynapthalene, 1,2-dihydroxybenzene(pyrocatechol), 1,3-dihydroxybenzene (resorcinol), 1,3-dihydroxy-2-methylbenzene, 1,3-dihydroxy-4-chlorobenzene(4-chlororesorcinol), 1,2,3,trihydroxybenzene, 1,2,4-trihydroxybenzene, 1,2,4-trihydroxy-5-methylbenzene, and 1,2,4-trihydroxytoluene.
- Method of Dyeing Keratinous Fibres
- In a further aspect the invention relates to a method for dyeing keratinous fibres, in particular hair, fur, hide and wool, using a composition as described above. The dyeing method can be conducted with one or more dye precursors (i.e. substrates of the invention) and optionally in combination with one or more modifiers. The amount of dye precursor(s) and other ingredients used in the composition of the invention for this purpose are in accordance with usual commercial amounts and therefore known for the skilled person. Hair dyeing is typically carried out at or near room temperature, preferably around the optimum temperature of the enzyme being used, and at a pH in the range of from 3.0 to 9.0, preferably 4.0 to 8.5, especially 6.0 to 8.0. Dye precursors (i.e. substrates of the invention) and optional modifiers are described above.
- The invention is further illustrated in the following non-limiting example.
- Synthesis of 3,4-diamino Benzoic Acid Esters
-
- The amino group in 4-amino-3-nitrotoluene is protected by boiling in anhydrous acetic acid in acetic acid. The methyl group is oxidized with permanganate in an aqueous solution containing magnesium sulphate. The acetyl group is removed by boiling with 0.1 hydrochloric acid. After isolation and drying 4-amino-3-nitrobenzoicacid is dissolved in absolute alcohol and concentrated sulphuric acid is added. On boiling for two to five hours the acid groups are esterified. The exact boiling time depends on the type of alcohol. The last stage is the reduction of the isolated product with activated iron and water in boiling benzine for about five hours.
- When the reaction was complete the iron particles were filtered out and the residue dried for between 24 to 48 hours over anhydrous sodium sulphate. After filtration and evaporation the ester was recrystallised in a mixture of n-butanol and benzine in the ratio of 1 to 10.
- The above procedure was used to produce 3,4-DABA esters for measurement of enzymes and for mutagenetic testing. If larger amounts were to be required at a reasonable price then direct esterification of 3,4-DABA would be preferred. Thus the methyl ester may be prepared by bubbling hydrochloric acid gas through a solution of 3,4-DABA containing methanol. This last method finds only limited use in the production of the ethyl ester and cannot be used to produce the isopropyl ester.
- Characterization of 3,4-DABA Esters
- Thin Layer Chromatography
- The DABA esters that were prepared were analysed and compared with the help of thin layer chromatography (TLC) using silica gel plates of the type MERC 60 F254 the stock number of the zone of concentration was 5583. A mixture of chloroform, methanol and acetic acid in the ratio of 90:5:5 on a volumetric basis was used as a solvent For the purpose of comparison OPD and 3,4-DABA were analyzed on the same plate. The Rf values obtained are shown in Table 1.
TABLE 1 Chemical bond Rf-value 3,4-DABA 0.15 OPD 0.19 Methyl ester 0.29 Ethyl ester 0.31 Isopropyl ester 0.33 - It can be seen from table 1 that the bigger alkyl groups give a measurably greater displacement in the solvent which contains chloroform. The least displacement is seen, as might be expected, with 3,4-DABA which contains a free carboxyl group. All the combinations tested moved in the form of patches which is an indication of their purity.
- The fact that the 3,4-DABA esters are lipeds gives no problems with regard to solubility in water when making up solutions of substrates. A standard solution of dimethyl formamide diluted in an aqueous buffer with a pH of 5.0. At high concentrations of substrate oxidation products formed by the action of enzymes may cause slight turbidity in the solution. By reducing the pH to about 1 with 1M sulphuric acid a completely clear solution is produced. This is due to the addition of protons to the amino groups.
- Determination of Melting Points
- To verify that the materials synthesised were identical with those described in the literature their melting points were determined and compared with values given in a table on page 1532 of Chapman and Hall's Dictionary of Organic Compounds, Fifth Edition, Volume 2. Melting points were determined by the use of the capillary tube method using a silicone oil bath.
- Melting points are given in Table 2.
TABLE 2 Material Measured melting point Value from literature methyl ester 108-109° C. 108-109° C. ethyl ester 112-113° C. 112-113° C. isopropyl ester 73-74° C. — - It can be seen from the above table that there is close agreement between the melting points determined by experiment and the melting points as given in the literature. It may, therefore, reasonably be assumed that the synthesised material are identical with those described in the literature. It was not possible to find a value for the isopropyl ester in the literature.
- Ultraviolet Spectroscopy
- UV spectra were taken of OPD as well as the methyl, ethyl and isopropyl esters.
- Scanning was done from 360 nm to 210 nm using a solution of the compounds in methanol. The concentration was 0.1 /1. Table 3 shows the absorption maxima and the extinction coefficients for the compounds investigated.
TABLE 3 Material Absorption max. Extinction coefficient OPD 290.0 nm 2000 M−1 231.3 nm 3400 M−1 methyl ester 310.0 nm 6000 M−1 277.5 nm 6000 M−1 232.5 nm 8400 M−1 ethyl ester 310.0 nm 6200 M−1 277.5 nm 6000 M−1 232.5 nm 8600 M−1 isopropyl 310.0 nm 6500 M−1 ester 277.5 nm 6200 M−1 232.5 nm 8700 M−1 - As can be seen from the above table all three esters absorb at the same wavelength. At 237.5 nm there is a slight increase in extinction with increasing molecular weight of the alkyl group. 3,4-DABA-esters show a typical maximum at 277.5 nm. This maximum is not found in OPD because of the ester carbonyl group.
- In order to investigate the properties of 3,4-DABA and the three esters with respect to oxidation catalyzed by peroxidase a series of measurements were carried out on the enzymatic reactions initial velocity with increasing concentration of the substrate. Measurements were carried out on OPD,3,4-DABA, 3,4-DABA-methyl ester, 3,4-DABA-ethyl ester, and 3,4-DABA isopropyl ester.
- Absorbancy at 492 nm was used as a measure of the course of the reaction. The initial velocity was taken to be the absorbancy at 492 nm two minutes after the addition of the peroxidase to a mixture of the substrate and hydrogen peroxide in a buffer with a pH of 5.0. The wavelength of 492 nm was chosen because it is employed in the standard assay procedures for OPD. None of the substrates has a specially high absorption at this wavelength.
- By varying the concentration of the substrate and at the same time measuring the initial velocity of the reaction it is posible to apply the Michaelis/Menten equation to the system.
-
- where [S] is the concentration of the substrate, Vmax is the maximum initial concentration which is reached in the particular assay. Km is defined as the concentration of the substrate at Vmax/2. A small Km value will therefore be characteristic for an enzyme system where a low concentration of the substrates produces saturation of the enzyme.
- The expression implies that the initial velocity will increase with increasing concentration of the substrate, but the curve for the velocity will flatten out and approach Vmax for very high concentrations of the substrate. In actual fact the parameter Kkat be calculated as Vmax/[E] where [E] is the molar concentration of the enzyme in the reaction. Kkat is the same as min−1 and reflects the activity of the enzyme in a saturated solution upon the substrate.
- The peroxidase system has an extremely complicated energy balance (Arnoa et al. (1990)) for short periods of less than a minute the system may nevertheless be described in terms of the above given formulae.
- Enzymatic Determination
- The following solutions were prepared for use in the enzyme assay:
- a) Assay buffer
- A 50 mM phosphate/citrate buffer with a pH of 5.0 was made by mixing a 50 mm Na2HPO4 solution and a 50 mm solution of citric acid. The pH was measured while mixing was in progress.
- b) DMF diluted 1:10
- By means of pipette 10 ml were placed in a graduated flask which was then topped up to 100 ml with assay buffer.
- c) Solution of hydrogen peroxide 0.018%
- 15 μl of a 30% solution of hydrogen peroxide (PERHYDROL, Merck) was thinned down with 25 ml of the assay buffer.
- d) Stabilizing buffer for peroxidase
- The stabilizing buffer for peroxidase, i.e. a buffer which stabilizes the enzyme, was prepared according to the method of Olsen and Little (1983). A 0.1M Na-acetate buffer, which was 0.5M in terms of CaCl2 was adjusted to pH 5.6.
- 37.5 mg N-acetyl-trimethyl-ammonium-bromide was dissolved in 75 ml of the buffer. To this solution 25 ml of glycerol was added. The enzyme activity is maintained in this buffer because the molecules of the enzyme are prevented from aggregating.
- e) Standard solution of peroxidase
- 10 mg of horseradish peroxidase type VI-A (Sigma no. 6782) were dissolved in 10 ml of the stabilizing buffer. This was stored at −15° C. This will keep for several months (Olsen and Little (1983).
- f) Bench solution of peroxidase
- The standard peroxidase solution was diluted to 1:1000 with the 10 ml assay-buffer solution in 10 μl standard solution.
- g) Standard solutions of the substrates
- 0.5 mmol of each substrate in 5 ml DMF. These solutions will keep for several weeks at −15° C.
- h) Bench solutions of the substrates
- The standard solutions were diluted by 1:10 with the assay buffer. Before being used the substrate solutions were diluted by 1:10. 0.5 ml of the standard solution was thinned down with 4.5 ml of the assay buffer.
- Measurement of the Velocity of Reaction as a Function of the Concentration of the Substrates
- For each of the compounds OPD, 3,4-DABA-, and the methyl, ethyl, and isopropyl esters of 3,4-DABA 15 measurements were carried out and absorbency was measured twice in each case at 492 nm one minute after the addition of 100 μl dilute peroxidase solution (bench solution). The concentration of the peroxidase was held constant at 50 ng/ml during the whole investigation. By using the volume of substrate and the volumes of 10 vol-% DMF solution as given in table 4 it was possible to employ a constant reaction volume and a constant concentration of DMF. For all measurements there was used 1550 μl buffer and 50 μl bench solution of peroxidase. The total volume is then as follows: 300 μI DMF and substrate solution, 1550 μl buffer, 100 μl bench solution of peroxidase and 50 μl hydrogen peroxide solution. That is 2000 μl in total.
TABLE 4 Substrate μl substrate μl 10% DMF- concentration solution solution (μmol/l) 0 300 0 5 295 25 10 290 50 15 285 75 20 280 100 25 275 125 30 270 150 35 265 175 40 260 200 50 250 250 60 240 300 80 220 400 100 200 500 150 150 750 200 100 1000 300 0 1500 - Table 5 contains information about the values measured for Km, Vmax and Kkat for the five compounds.
TABLE 5 Km Vmax Kkat Substrate (μmol/μl) (min−1) (1*mol−1*min−1) OPD 47.35 0.16 1.6 * 108 3,4-DABA 251.22 0.20 2.0 * 108 methyl 125.97 0.22 2.2 * 108 ester ethyl 212.39 0.27 2.7 * 108 ester isopropyl 118.46 0.22 2.2 * 108 ester - The results of the measurements of initial velocities are stated in units of absorbency and not in molar units. In order to be able to measure the “true” velocity of reaction it is necessary to isolate the oxidation product for each substrate and determine the molar extinction coefficient. The value of Kkat is worked out from 1 mole of peroxidase of 50,000 g/mol.
- FIG.1 +L-5 is a graphic representation of the result of the measurement of initial velocity on OPD, 3,4-DABA, 3,4-DABA-methyl ester, 3,4-DABA-ethyl ester, 3,4-DABA-isopropyl ester.
- As is shown by Table 5 and FIGS. 1 to 6 the carboxyl esters of 3,4-DABA are effective substrates in a peroxidase/hydrogen peroxide system. It is possible to obtain much higher initial velocities with these compounds than with OPD. Km per se is a poor indicator of the effectiveness in enzyme assays of the substrates in question as it actually only shows the sensitivity of the system at low concentrations of substrate. In practice substrate concentrations would be chosen to allow maximum and linear colour development with different concentrations of enzymes. In other words Vmax and Kkat are more relevant parameters for the comparison of different substrates. It was found that, for all the esters investigated, the values of Vmax and Kkat were considerably larger than the comparable values for OPD.
- All reaction velocities are expressed as absorption units, this is partly because most practical enzyme essays are based on the measurement of absorption and partly because the products of reaction are not isolated from the reaction mixture.
- Determination of the Mutagenicity of the Compounds
- The Ames test (Maron and Ames (1983)) was used to determine the mutagenic properties of the compounds. Nutrient media were prepared in the manner described by Venitt and Parry (1984). To 3×2 ml melted agar at 45° C. were added 100 μl of 50, 100 and 200 mM of solutions of the compounds dissolved in DMSO. By means of a pipette 100 μl of a well-grown culture ofSalmonella tphimurium TA 98 (BIO-TEST gl. skolevej 47, 6731 Tiaereborg) were added to the same test-tube. The bacteria contain a frameshift mutation on the histinol-dehydrogenase gene and require histidin in order to grow. Mutagenic aromatic amines can cause the bacteria to mutate to His+ and they can then grow on the nutrient medium. The number of colonies after incubation therefore give a quantitative measure of the ability of the added compound to cause mutation. In all trials spontaneous mutations take place in the absence of a mutagen. These provide a measure of “background” mutation.
- OPD is not a direct mutagen, it must first be activated by the liver enzyme system P450. All trials were therefore carried out both with and without the addition of “S9-mix” from the livers of rats, this contains the P450 system. 0.5 ml of “59-mix” was added to each test-tube. The criteria for mutation are that increasing concentrations of the compound under investigation give a marked increase in the number of His+ mutants. The results of these trial are given in FIG.7 +L-11. It may be seen from this figure that only OPD has mutagenic properties.
- Dyeing Effect of Dye Precursors of the Invention
- The permanent oxidative dyeing effect of different dye precursors using 0.05 mg active enzyme proteinMyceliophthora thermophila laccase (available from Novo Nordisk and described in WO 95/33836) per ml reaction mixture were tested.
- The dye precursors tested were
- 0.1% w/w 3,4 diamino benzoic acid (DABA) in 0.1M K-phosphatebuffer, pH 7.0.
-
- Modifier used
- 0.1% w/w m-phenylenediamine (MPD) in 0.1M K-phosphatebuffer, pH 7.0.
- Dye precursor solutions were prepared by mixing the indicated modifier so that the final concentration in the dyeing solution was 0.1% w/w with respect to dye precursor (i.e. substrate of the invention) and 0.1% w/w with respect to modifier.
- Hair Dyeing
- 1 gram 6″ De Meo Virgin natural white hair tresses (De Meo Brothers Inc. USA) were used.
- 4 ml dye precursor solution (including modifier) was mixed with 1 ml laccase on a Whirley mixer, applied to the hair tresses and incubated at 30° C. for 30 minutes.
- The hair tresses were then rinsed with running water, washed with shampoo, rinsed with water, combed, and air dried.
- a*, b* and L* were determined on the Chroma Meter and ΔE* was then calculated as described below.
- Hair tress samples treated without enzyme were used as a blind.
- The result of the test is shown in Table 6.
TABLE 6 DABA and DABA-Me 0.1% w/w dye with/without MPD precursor/modifier ΔL Δa Δb ΔE Assessment DABA −4.27 −0.63 −2.55 5.01 no colour DABA + MPD −23 −2.21 −18.29 29.47 grayish DABA-Me −7.58 6.53 −2.14 10.23 light orange DABA-Me + MPD −32.31 2.35 −25.07 40.96 grayish violet - Assessment of the Hair Colour
- The quantitative colour of the hair tresses was determined on a Minolta CR200 Chroma Meter by the use the parameters L* (“0”=black and “100”=white), a* (“−”=green and “+”=red) and b* (“−” blue and “+” yellow).
- ΔL*, Δa* and Δb* are the delta values of L*, a* and b* respectively compared to L*, a* and b* of untreated hair (e.g. ΔL*=L*sample−L*untreated hair).
- ΔE* was calculated as ΔE*=square root(ΔL*2+Δa*2+Δb*2) and is an expression for the total quantitative colour change.
- Dyeing Effect of DAB-Me and Various Modifiers
- Using the procedure described in Example 4 the permanent dyeing effect of the dye precursor (i.e. substrates) DABA-Me with various modifiers were tested, except that 0.2% w/w dye precursor and 0.2% modifier were used.
TABLE 2 0.2% DABA-Me and 0.2% w/w modifier ΔL* Δa* Δb* ΔE* Assessment 4-chlor-resorcinol −22.36 1.19 −6.28 23.26 Gray-green 5-amino-o-cresol −14.1 5.69 −2.1 15.35 light orange m-phenylene-diamine −33.25 2.17 −23.71 40.9 Grey (Bluish) pyrogallol −29.47 5.74 −7.69 30.99 Brown 4-methoxy-1,3-phenyl- −39.24 2.33 −19.73 43.98 Brown-gray/ enediamine black - As can be seen the keratinous fibers can be dyed using DABA-Me and a modifier.
Claims (20)
1. A substrate, which develops colour on oxidation characterized by the inclusion of an amino benzoic acid compound with the general formula 1
wherein
R is an amino, mono- or a distributed amino or OR′, where R is H, alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl or substituted phenyl, X, Y and Z may each independently be hydrogen alkyl, alkenyl, alkynyl, halogenalkyl, nitro, benzyl, phenyl, substituted phenyl, amino, hydroxy or mercapto with the proviso that at least one of the groups X, Y and Z is an amino group or an salt thereof.
2. The substrate according to claim 1 , wherein R′ is a methyl, ethyl or isopropyl ester.
3. The use of amino benzoic acid compounds with the general formula 1 as well as the salt thereof as a colour producing substrate in analysis based on the use of peroxidase.
4. The use of amino benzoic acid compounds with the general formula 1 as well as the salt thereof as a colour producing substrate in hair dyeing compositions as well as for compositions for dying of natural and synthetic fibres including textiles, thread and yarns.
5. Use according to claims 3 or 4 wherein the compound is selected from the group of methyl, ethyl or isopropyl esters of amino benzoic acid.
6. Method for quantitative and/or qualitative analysis of a material of biological interest, wherein a peroxidase enzyme together with a marker is bound to the compound of interest, hydrogen peroxide is then converted with a colour producing substrate in the presence of the peroxidase, characterized by the use of a substrate selected from the group made up of amino benzoic acid compounds with the general formula 1 as well as its salts.
7. The method according to claim 8 wherein the compound is selected from the group of methyl, ethyl or isopropyl esters of amino benzoic acid as well as its salts.
8. The method according to claim 6 wherein the peroxidase marker is capable of forming an immunological link to the materiel of biological interest.
9. The method according to claim 6 wherein the materiel of biological interest is an antigen and the marker is an antibody to the antigen.
10. Method for producing a colored product wherein the substrate according to claim 1 or 2 is converted by means of an oxidation system.
11. The method according to claim 10 , wherein the oxidation system comprises an inorganic compound, preferably one of the compound hypochlorite, hypobromite, permanganate, dichromate, or iron as Fe3+).
12. The method according to claim 10 , wherein the oxidation system includes an enzyme and an electron acceptor.
13. The method according to claim 12 , wherein the enzyme is a peroxidase and the electron acceptor is hydrogen peroxide or that the enzyme is oxidase and the electron acceptor is oxygen.
14. The method according to claim 13 , wherein the oxidase is chosen from the group catechol oxidase, laccase and related enzymes o-amino phenoloxidase.
15. A composition adapted for dyeing of keratinous fibres, comprising 1) at least one oxidation enzyme, 2) at least one substrate according to any of claims 1 or 2, and optionally 3) at least one modifier.
16. The composition according to claim 15 , wherein the oxidation enzyme is an oxidoreductase selected from laccases and related enzymes, oxidases or peroxidases.
17. The composition of claim 16 , wherein the oxidation enzyme is a laccase, in particular a laccase derived from a strain of Polyporus sp., in particular a strain of P. pinsitus or P. versicolor, a strain of Myceliophthora sp., in particular M. thermophila, a strain of Rhizoctonia sp., in particular Rh. praticola or Rh. solani, a strain of a Rhus sp., in particular Rhus vernicifera, or a strain of Scytalidium, in particular S. thermophilium, a strain of Pyricularia sp., in particular P. oryzae.
18. A method for dyeing keratinous fibres, comprising contacting the fibers with a composition comprising 1) at least one oxidation enzyme, 2) at least one substrate according to claims 1 or 2, and optionally 3) at least one modifier, for a period of time and under conditions sufficient to permit oxidation of the substrate to a colored compound.
19. The method of claim 18 , wherein the dyeing is carried out at a pH in the range from 3.0 to 9.0, preferably 4.0 to 8.5, especially 6.0 to 8.0.
20. The method of claims 18 or 19, wherein the composition is as defined in any of claims 15 to 17 .
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US09/271,540 US6231621B1 (en) | 1996-10-08 | 1999-03-18 | Diaminobenzoic acid derivatives as dye precursors |
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DD291094A5 (en) * | 1989-12-28 | 1991-06-20 | Veb Filmfabrik Wolfen,De | ANALYTICAL ELEMENT FOR DETERMINING INVERTASE |
FR2673534B1 (en) * | 1991-03-08 | 1995-03-03 | Perma | COMPOSITION FOR THE ENZYMATIC COLORING OF KERATINIC FIBERS, ESPECIALLY HAIR, AND ITS APPLICATION IN A COLORING PROCESS. |
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EP0891182B1 (en) * | 1996-04-03 | 2001-11-14 | Novozymes A/S | Enzyme assisted dyeing of keratinous fibres |
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JP2001502369A (en) | 2001-02-20 |
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CN1232384A (en) | 1999-10-20 |
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AU730286B2 (en) | 2001-03-01 |
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AU4452397A (en) | 1998-05-05 |
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