WO1992017613A1 - Enzymatisch unterstützte äscher- und beizverfahren - Google Patents
Enzymatisch unterstützte äscher- und beizverfahren Download PDFInfo
- Publication number
- WO1992017613A1 WO1992017613A1 PCT/DE1992/000233 DE9200233W WO9217613A1 WO 1992017613 A1 WO1992017613 A1 WO 1992017613A1 DE 9200233 W DE9200233 W DE 9200233W WO 9217613 A1 WO9217613 A1 WO 9217613A1
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- WO
- WIPO (PCT)
- Prior art keywords
- range
- liming
- weight
- water
- alkaline
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 36
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 33
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 33
- 108090001060 Lipase Proteins 0.000 claims abstract description 43
- 239000004367 Lipase Substances 0.000 claims abstract description 43
- 102000004882 Lipase Human genes 0.000 claims abstract description 43
- 235000019421 lipase Nutrition 0.000 claims abstract description 43
- 238000004519 manufacturing process Methods 0.000 claims abstract description 8
- 230000002797 proteolythic effect Effects 0.000 claims abstract description 6
- 230000002366 lipolytic effect Effects 0.000 claims abstract 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 38
- 108091005804 Peptidases Proteins 0.000 claims description 32
- 102000035195 Peptidases Human genes 0.000 claims description 29
- 239000004365 Protease Substances 0.000 claims description 27
- 230000000694 effects Effects 0.000 claims description 20
- 238000005554 pickling Methods 0.000 claims description 9
- 108091005658 Basic proteases Proteins 0.000 claims description 6
- 239000003352 sequestering agent Substances 0.000 claims description 5
- 108091005507 Neutral proteases Proteins 0.000 claims description 4
- 102000035092 Neutral proteases Human genes 0.000 claims description 2
- 239000004094 surface-active agent Substances 0.000 claims description 2
- 229940088598 enzyme Drugs 0.000 description 28
- 210000003491 skin Anatomy 0.000 description 27
- 239000000047 product Substances 0.000 description 22
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 15
- 239000003995 emulsifying agent Substances 0.000 description 12
- AXCZMVOFGPJBDE-UHFFFAOYSA-L calcium dihydroxide Chemical compound [OH-].[OH-].[Ca+2] AXCZMVOFGPJBDE-UHFFFAOYSA-L 0.000 description 9
- -1 alkaline earth metal sulfides Chemical class 0.000 description 8
- 239000000920 calcium hydroxide Substances 0.000 description 8
- 235000011116 calcium hydroxide Nutrition 0.000 description 8
- 229910001861 calcium hydroxide Inorganic materials 0.000 description 8
- 235000014113 dietary fatty acids Nutrition 0.000 description 8
- 229930195729 fatty acid Natural products 0.000 description 8
- 239000000194 fatty acid Substances 0.000 description 8
- 239000010985 leather Substances 0.000 description 8
- 239000011734 sodium Substances 0.000 description 8
- 230000007935 neutral effect Effects 0.000 description 7
- UYXTWWCETRIEDR-UHFFFAOYSA-N Tributyrin Chemical compound CCCC(=O)OCC(OC(=O)CCC)COC(=O)CCC UYXTWWCETRIEDR-UHFFFAOYSA-N 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 6
- 230000002255 enzymatic effect Effects 0.000 description 6
- 150000004665 fatty acids Chemical class 0.000 description 6
- 230000002538 fungal effect Effects 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 240000006439 Aspergillus oryzae Species 0.000 description 5
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 5
- 206010000496 acne Diseases 0.000 description 5
- 235000019197 fats Nutrition 0.000 description 5
- 150000002191 fatty alcohols Chemical class 0.000 description 5
- 229920000151 polyglycol Polymers 0.000 description 5
- 239000010695 polyglycol Substances 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 4
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 4
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 4
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 4
- 235000011130 ammonium sulphate Nutrition 0.000 description 4
- 230000035617 depilation Effects 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000228212 Aspergillus Species 0.000 description 3
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 3
- 244000063299 Bacillus subtilis Species 0.000 description 3
- 235000014469 Bacillus subtilis Nutrition 0.000 description 3
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 3
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 3
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 3
- UCKMPCXJQFINFW-UHFFFAOYSA-N Sulphide Chemical compound [S-2] UCKMPCXJQFINFW-UHFFFAOYSA-N 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 238000005238 degreasing Methods 0.000 description 3
- 150000001991 dicarboxylic acids Chemical class 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000002736 nonionic surfactant Substances 0.000 description 3
- 239000003921 oil Substances 0.000 description 3
- 235000019198 oils Nutrition 0.000 description 3
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 235000019832 sodium triphosphate Nutrition 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- UNXRWKVEANCORM-UHFFFAOYSA-I triphosphate(5-) Chemical compound [O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O UNXRWKVEANCORM-UHFFFAOYSA-I 0.000 description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- 241000228230 Aspergillus parasiticus Species 0.000 description 2
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 2
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 2
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Natural products CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 235000011941 Tilia x europaea Nutrition 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 150000003863 ammonium salts Chemical class 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- RWGFKTVRMDUZSP-UHFFFAOYSA-N cumene Chemical compound CC(C)C1=CC=CC=C1 RWGFKTVRMDUZSP-UHFFFAOYSA-N 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 229940079919 digestives enzyme preparation Drugs 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 230000001804 emulsifying effect Effects 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 210000002615 epidermis Anatomy 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 150000002314 glycerols Chemical class 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 239000004571 lime Substances 0.000 description 2
- 235000019626 lipase activity Nutrition 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 239000004006 olive oil Substances 0.000 description 2
- 235000008390 olive oil Nutrition 0.000 description 2
- 239000012188 paraffin wax Substances 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 239000000344 soap Substances 0.000 description 2
- 229910052938 sodium sulfate Inorganic materials 0.000 description 2
- 235000011152 sodium sulphate Nutrition 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 150000003871 sulfonates Chemical class 0.000 description 2
- URAYPUMNDPQOKB-UHFFFAOYSA-N triacetin Chemical compound CC(=O)OCC(OC(C)=O)COC(C)=O URAYPUMNDPQOKB-UHFFFAOYSA-N 0.000 description 2
- 239000002699 waste material Substances 0.000 description 2
- KWVPFECTOKLOBL-KTKRTIGZSA-N 2-[(z)-octadec-9-enoxy]ethanol Chemical compound CCCCCCCC\C=C/CCCCCCCCOCCO KWVPFECTOKLOBL-KTKRTIGZSA-N 0.000 description 1
- SCVJRXQHFJXZFZ-KVQBGUIXSA-N 2-amino-9-[(2r,4s,5r)-4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]-3h-purine-6-thione Chemical class C1=2NC(N)=NC(=S)C=2N=CN1[C@H]1C[C@H](O)[C@@H](CO)O1 SCVJRXQHFJXZFZ-KVQBGUIXSA-N 0.000 description 1
- SDGNNLQZAPXALR-UHFFFAOYSA-N 3-sulfophthalic acid Chemical compound OC(=O)C1=CC=CC(S(O)(=O)=O)=C1C(O)=O SDGNNLQZAPXALR-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 241000590020 Achromobacter Species 0.000 description 1
- 241000932047 Achromobacter sp. Species 0.000 description 1
- 208000002874 Acne Vulgaris Diseases 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 241000228245 Aspergillus niger Species 0.000 description 1
- 241000228257 Aspergillus sp. Species 0.000 description 1
- 241000193375 Bacillus alcalophilus Species 0.000 description 1
- 241000193747 Bacillus firmus Species 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000941525 Chromobacterium sp. Species 0.000 description 1
- 241000146387 Chromobacterium viscosum Species 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 241000186249 Corynebacterium sp. Species 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000235395 Mucor Species 0.000 description 1
- 241001558145 Mucor sp. Species 0.000 description 1
- 241001236817 Paecilomyces <Clavicipitaceae> Species 0.000 description 1
- 102000019280 Pancreatic lipases Human genes 0.000 description 1
- 108050006759 Pancreatic lipases Proteins 0.000 description 1
- 108010019160 Pancreatin Proteins 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 241001507683 Penicillium aurantiogriseum Species 0.000 description 1
- 241001123663 Penicillium expansum Species 0.000 description 1
- 241000228168 Penicillium sp. Species 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical class OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- 229920000388 Polyphosphate Polymers 0.000 description 1
- 241000186334 Propionibacterium freudenreichii subsp. shermanii Species 0.000 description 1
- 241001521757 Propionibacterium sp. Species 0.000 description 1
- JUJWROOIHBZHMG-UHFFFAOYSA-N Pyridine Chemical class C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 1
- 241000235525 Rhizomucor pusillus Species 0.000 description 1
- 240000005384 Rhizopus oryzae Species 0.000 description 1
- 235000013752 Rhizopus oryzae Nutrition 0.000 description 1
- 241000952054 Rhizopus sp. Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 238000006887 Ullmann reaction Methods 0.000 description 1
- BNOODXBBXFZASF-UHFFFAOYSA-N [Na].[S] Chemical compound [Na].[S] BNOODXBBXFZASF-UHFFFAOYSA-N 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 229910001854 alkali hydroxide Inorganic materials 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 150000008044 alkali metal hydroxides Chemical class 0.000 description 1
- 150000001340 alkali metals Chemical class 0.000 description 1
- 229910052784 alkaline earth metal Inorganic materials 0.000 description 1
- 150000008052 alkyl sulfonates Chemical class 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 235000015278 beef Nutrition 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- KXGVEGMKQFWNSR-UHFFFAOYSA-N deoxycholic acid Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 KXGVEGMKQFWNSR-UHFFFAOYSA-N 0.000 description 1
- 230000002951 depilatory effect Effects 0.000 description 1
- HFCSXCKLARAMIQ-UHFFFAOYSA-L disodium;sulfate;hydrate Chemical compound O.[Na+].[Na+].[O-]S([O-])(=O)=O HFCSXCKLARAMIQ-UHFFFAOYSA-L 0.000 description 1
- 238000004945 emulsification Methods 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 150000002170 ethers Chemical class 0.000 description 1
- 238000007046 ethoxylation reaction Methods 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 239000001087 glyceryl triacetate Substances 0.000 description 1
- 235000013773 glyceryl triacetate Nutrition 0.000 description 1
- 239000004519 grease Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 150000004679 hydroxides Chemical class 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 150000002484 inorganic compounds Chemical class 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 239000012875 nonionic emulsifier Substances 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 229940055695 pancreatin Drugs 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 239000003208 petroleum Substances 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 229920005646 polycarboxylate Polymers 0.000 description 1
- 229920000223 polyglycerol Polymers 0.000 description 1
- 239000001205 polyphosphate Substances 0.000 description 1
- 235000011176 polyphosphates Nutrition 0.000 description 1
- 235000015277 pork Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 150000003242 quaternary ammonium salts Chemical class 0.000 description 1
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 235000021003 saturated fats Nutrition 0.000 description 1
- 231100000241 scar Toxicity 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
- HYHCSLBZRBJJCH-UHFFFAOYSA-M sodium hydrosulfide Chemical compound [Na+].[SH-] HYHCSLBZRBJJCH-UHFFFAOYSA-M 0.000 description 1
- 229910052979 sodium sulfide Inorganic materials 0.000 description 1
- GRVFOGOEDUUMBP-UHFFFAOYSA-N sodium sulfide (anhydrous) Chemical compound [Na+].[Na+].[S-2] GRVFOGOEDUUMBP-UHFFFAOYSA-N 0.000 description 1
- PANBYUAFMMOFOV-UHFFFAOYSA-N sodium;sulfuric acid Chemical compound [Na].OS(O)(=O)=O PANBYUAFMMOFOV-UHFFFAOYSA-N 0.000 description 1
- 108010079522 solysime Proteins 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 125000000446 sulfanediyl group Chemical group *S* 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 239000003760 tallow Substances 0.000 description 1
- 229960002622 triacetin Drugs 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- ICUTUKXCWQYESQ-UHFFFAOYSA-N triclocarban Chemical compound C1=CC(Cl)=CC=C1NC(=O)NC1=CC=C(Cl)C(Cl)=C1 ICUTUKXCWQYESQ-UHFFFAOYSA-N 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 150000003739 xylenols Chemical class 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C14—SKINS; HIDES; PELTS; LEATHER
- C14C—CHEMICAL TREATMENT OF HIDES, SKINS OR LEATHER, e.g. TANNING, IMPREGNATING, FINISHING; APPARATUS THEREFOR; COMPOSITIONS FOR TANNING
- C14C1/00—Chemical treatment prior to tanning
- C14C1/08—Deliming; Bating; Pickling; Degreasing
Definitions
- the invention relates to enzymatically assisted liming and pickling processes using alkaline lipases, preferably in combination with proteolytic enzymes.
- lipase and amylase in the form of pancreatin
- Hungarian patent 3325 Chem. Abstr. 77, 7341 k
- lipases offers itself for degreasing hides and skins, especially the high-fat pigskins and sheepskins and waste.
- there are recommendations for use in degreasing e.g. LH Posorske J. Am. Oil Chem.Soc. 61 (11) 1758 - 1760 (1984); K. Yeshodha et al. Leather sei (Madras) 25 (2) 77 - 86 (1978 ), Chem. Abstr. 89, 199097; T. Nielsen Fette, Seifen, Anstrichm. 82 (1) 15 - 19 (1985) also have negative experiences, eg with pickled and
- Literature reference is made to enzymatic fat degradation by means of lipases or lipase-containing enzyme preparations in a pH range below 8, preferably in the moderately acidic pH range.
- the stain also prepares fat-rich nakedness
- alkaline lipases AL have a pH optimum at about 9-11.
- the effect is particularly pronounced when the lipases mentioned are used in an enzyme combination EK together with neutral or alkaline proteases P, which are selected according to the substep in question. These are preferably the proteases used in technology.
- the liming is in the generally carried out in the pH range 12-13, either in the form of the so-called "hydroxyl ash", where calcium hydroxide in particular is used in addition to alkali hydroxide, ammonia and other alkaline earth hydroxides, or in the form of the so-called sulfide ash, the active components of which are alkali metal or alkaline earth metal sulfides, optionally in a mixture with others are basic alkalis or alkaline earths.
- the liming process according to the invention very largely follows the processes of the prior art (Ullmann's Encyclopedia of Industrial Chemistry 5th Ed. Vol.
- the liming operation can be carried out with a liquor length of 50-250%, preferably 80-150%.
- Water based on the weight of the skins can be carried out.
- the liming process generally takes 12 to 36 hours, in particular 16 to 20 hours.
- the hides and skins are neutralized and enzymatically ashed.
- the hides or skins are first washed and preferably using weak acids, for example organic acids such as lactic acid, formic acid,
- weakly acidic inorganic compounds such as sodium bisulfite, sulfophthalic acid, ammonium sulfate or carbonic acid.
- the enzymatic pickling component in particular enzymes of the pancreatic complex, is added after a certain time.
- Enzymes of the pancreatic complex can also include lipases (DE-A 37 04 465). The range between 32 and 37 degrees C has proven to be expedient for the pickling temperature.
- the pickling time is generally in the
- the enzymatic batches in particular the sequestering agents SM known per se with the enzyme combination EK, contain in advance for the purpose
- the liquor length corresponds to that when the liming is carried out.
- the lipases to be used according to the invention are those having the same definitions.
- Esterases which hydrolyze glycerol esters of fatty acid in aqueous emulsion (E.C. 3.1.1.3.).
- the triglycerides are preferably cleaved in the 1,3 position. In contrast to the lipases of the
- the lipases used according to the invention have a state of the art with a range of use of pH 6-9 pronounced optimum effect (eg against olive oil or tributyrin) between pH 9 and 11.
- Such alkaline lipases have been specially developed for the detergent industry. They are of microbiological origin.
- Lipases come e.g. in Pseudomonas strains. Rhizopus sp., Candida sp., Chromobacterium sp. as a lipase supplier. Other important lipase producers are Geotrichium sp., Aspergillus sp., Mucor sp., Penicillium sp., Corynebacterium sp.,
- Lipolase TM 30 T commercially available lipase (NOVO INDUSTRI A / S, DK 2880 Bagsvaerd, Denmark).
- the activity determination of lipases is carried out in a conventional manner with olive oil as a substrate, furthermore with triacetin and tributyrin. [See. M. Semeriva et al.
- Lipase activity is given in LCA units, but is measured at pH 9.5. According to the
- Lipases used in such a way that a lipase activity of 100-10,000 LCA, preferably 2,000 to 4,000 LCA per kg skin is present in the liquor at pH 9.5.
- proteases in the liming, which is in the pH range between 9 and 13 a sufficient proteolytic enzyme
- Alkaline proteases that develop their optimum activity in the pH range 8.5 - 13. This includes
- alkaline bacterial proteases which mostly belong to the serine type and alkaline fungal proteases.
- the proteases from Bacillus strains such as B.subtilis, B.licheniformis, B.firmus,
- B.alcalophilus B.polymixa, B.mesentericus, further Streptomyces strains such as S.alcalophilus.
- Bacterial proteases are generally at 40-60 degrees C, with fungal proteases more at 20-40 degrees C.
- Alkaline fungal proteases include those from Aspergillus strains such as A. oryzae
- Paecilomyces persicinus and others The activity of the alkaline fungal proteases is predominantly in the pH range 8.0 - 11.0. As a rule of thumb, enzyme activity can be assumed to be between 8,000 and 10,000 Löhlein-Volhard units [LVE] per gram of enzyme.
- Neutral proteases with optimal activity in the range of pH 6.0 - 9.0 include in particular neutral bacterial proteases, which are usually among the
- Neutral bacterial proteases develop their activity optimally at working temperatures of 20 - 50 degrees C, whereas the most favorable working temperature for neutral fungal proteases is 35 - 40 degrees C.
- LVE Löhlein-Volhard unit
- protease activity is in the
- the process according to the invention usually requires amounts of proteases between 0.05 and 0.8% by weight, as a rule of thumb about 0.1-0.25% by weight, based on the weight of the hides and skins used.
- Emulsifiers for example of the following types:
- anionic emulsifiers for example of the following types:
- Cationic emulsifiers are less advantageous e.g. of types:
- radical R above is a long-chain alkyl radical with 8-24 carbon atoms
- radicals R 1 , R 2 or R 3 are generally short-chain alkyl radicals with up to 6 carbon atoms.
- the emulsifiers which can be used according to the invention have an HLB value (O / W emulsion) of 8-18, preferably 9-15, especially 12-15 (cf. Ullmanns Encyklopadie der Techn. Chemie, 4th edition, vol. 19). Combinations of emulsifiers, in particular nonionic and anionic ones, can advantageously also be used
- the amount of emulsifiers in the liquors is - in
- the precipitations to be expected according to the above composition occur when using the
- the sequestering agents are selected from the group consisting of the polyphosphates, phosphonates,
- EDTA ethylenediaminetetraacetic acid
- Nitrilotriacetic acid diethylenetriamineopentaacetic acid.
- the content of the sequestering agents in the soft liquor can be 0 to 0.5% by weight, preferably 0.05 to 0.15% by weight.
- the lipases used correspond to the label given above, as do the proteases. Ashtray process
- the dosage of the product is usually in the range of 0.05-1% in terms of salt weight or fresh weight of the skins.
- the temperature is preferably
- the skins or skins are soft as usual. It was
- the switch is followed by a hair immunization step in which - based on DE-A 38 02 640 - lime hydrate and organic thio compounds together with amines in approximately 80% water at approximately pH 12 can be used. This is usually followed by a level of hair loosening.
- a greatly reduced amount of sulfide is used, for example 0.4% by weight sodium sulfhydrate (72%) based on the skins.
- the skins are hair-free for about 2 hours. It is advisable to add about 70% by weight of water together with about 2% by weight of lime hydrate and approx. 0.3% by weight of sodium hydroxide solution (50%) and leaves for a certain period of time, expediently approx. 14 hours at 28 degrees C with intervals,
- the skin material prepared in the usual way e.g.
- Fleshed and split pelts are usually first washed and descaled in the usual way (see above).
- about the same amount of water is again added, preferably at 35 ° C., and the enzymes are preferably added as an enzyme combination EK.
- Enzyme combinations EK of the following typical composition are generally used: 50 - 1 00 KLVE pancreatic enzyme complex
- the product according to the invention is at 30-35 degrees C for 20-120 minutes at 0.5-2% based on the
- the manufacturer's specifications are in the pH range 10 - 11, both under the conditions of the liming at a pH of approx. 13 and in the stain in the pH range 7 - 9
- alkaline lipase ® Lipolase 100 T NOVO
- Emulsifier combination ES
- Fat content in the nakedness 0.25% in terms of dry weight
- Tanning drum (details refer to weight)
- nonionic emulsifier based on C 13 fatty alcohol with 8 moles of ethylene oxide
Landscapes
- Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Treatment And Processing Of Natural Fur Or Leather (AREA)
- Cosmetics (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Materials For Medical Uses (AREA)
- Cleaning And De-Greasing Of Metallic Materials By Chemical Methods (AREA)
Priority Applications (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CS923435A CZ285164B6 (cs) | 1991-03-26 | 1991-03-26 | Způsob výroby holin, připravených k vyčinění |
| SK3435-92A SK277863B6 (en) | 1991-03-26 | 1992-03-19 | Method of manufacture of pelts prepared for cleaning |
| BR9204797A BR9204797A (pt) | 1991-03-26 | 1992-03-19 | Processo de caleira e mordentagem enzimaticamente apoiados |
| RU9292016365A RU2052506C1 (ru) | 1991-03-26 | 1992-03-19 | Способ обработки шкур и голья |
| JP92506477A JPH05507522A (ja) | 1991-03-26 | 1992-03-19 | 酵素的に促進される石灰浸け―及び酵解法 |
| PL92297166A PL168197B1 (pl) | 1991-03-26 | 1992-03-19 | Sposób wytwarzania gotowych do garbowania golizn ze skór przy uzyciu enzymów proteolitycznych i lipolitycznych w warsztacie mokrym PL PL PL PL PL PL |
| KR1019920702971A KR100201731B1 (en) | 1991-03-26 | 1992-11-25 | Hide liming and drenching process using enzymes |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DEP4109826.9 | 1991-03-26 | ||
| DE4109826A DE4109826A1 (de) | 1991-03-26 | 1991-03-26 | Enzymatisch unterstuetze aescher- und beizverfahren |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO1992017613A1 true WO1992017613A1 (de) | 1992-10-15 |
Family
ID=6428184
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/DE1992/000233 WO1992017613A1 (de) | 1991-03-26 | 1992-03-19 | Enzymatisch unterstützte äscher- und beizverfahren |
Country Status (16)
| Country | Link |
|---|---|
| EP (1) | EP0505920B1 (cs) |
| JP (1) | JPH05507522A (cs) |
| KR (1) | KR100201731B1 (cs) |
| AT (1) | ATE154396T1 (cs) |
| AU (1) | AU645412B2 (cs) |
| BR (1) | BR9204797A (cs) |
| CZ (1) | CZ285164B6 (cs) |
| DE (2) | DE4109826A1 (cs) |
| ES (1) | ES2103845T3 (cs) |
| HU (1) | HU217020B (cs) |
| PL (1) | PL168197B1 (cs) |
| RU (1) | RU2052506C1 (cs) |
| SK (1) | SK277863B6 (cs) |
| TW (1) | TW203102B (cs) |
| WO (1) | WO1992017613A1 (cs) |
| ZA (1) | ZA922207B (cs) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2140457C1 (ru) * | 1995-02-24 | 1999-10-27 | Рем Гмбх | Водное средство для обработки шкур и голья |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2149900C1 (ru) * | 1999-06-10 | 2000-05-27 | Центральный научно-исследовательский институт кожевенно-обувной промышленности | Способ выработки кож |
| RU2156304C1 (ru) * | 1999-12-09 | 2000-09-20 | Центральный научно-исследовательский институт кожевенно-обувной промышленности | Способ обработки голья |
| EP1555322B1 (en) | 2000-04-28 | 2010-06-16 | Novozymes A/S | Lipolytic enzyme variant |
| WO2002055679A2 (en) | 2001-01-10 | 2002-07-18 | Novozymes A/S | Thermostable lipolytic enzyme variant |
| DE10221152B4 (de) * | 2002-05-13 | 2008-10-30 | Schill + Seilacher Ag | Verfahren zur Herstellung sauberer Blößen in der Wasserwerkstatt |
| WO2005052161A2 (en) | 2003-11-19 | 2005-06-09 | Genencor International, Inc. | Serine proteases, nucleic acids encoding serine enzymes and vectors and host cells incorporating same |
| US7985569B2 (en) | 2003-11-19 | 2011-07-26 | Danisco Us Inc. | Cellulomonas 69B4 serine protease variants |
| ES2526646T3 (es) | 2007-04-09 | 2015-01-14 | Novozymes A/S | Tratamiento enzimático para el desengrasado de pieles y pellejos |
| US7618801B2 (en) | 2007-10-30 | 2009-11-17 | Danison US Inc. | Streptomyces protease |
| CN101235421B (zh) * | 2008-02-02 | 2010-06-09 | 四川大学 | 制革加工动物皮清洁化脱毛和皮纤维松散方法及其应用 |
| TW201540646A (zh) * | 2014-04-30 | 2015-11-01 | Lien Shun Yang Leather Co Ltd | 防水透濕豬皮製成方法 |
| RU2733428C1 (ru) * | 2019-04-29 | 2020-10-01 | Федеральное государственное бюджетное научное учреждение "Федеральный Алтайский научный центр агробиотехнологий" (ФГБНУ ФАНЦА) | Способ обезволашивания пантов |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR469758A (fr) * | 1914-03-18 | 1914-08-10 | Leon Krall | Procédé de mise en confit des peaux |
| DE2856320A1 (de) * | 1978-12-27 | 1980-07-17 | Roehm Gmbh | Enzymatisches beizverfahren |
| GB2233665A (en) * | 1989-07-11 | 1991-01-16 | Roehm Gmbh | Enzymatically aided soaking process for skins and hides |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3704465C2 (de) * | 1987-02-13 | 1995-11-02 | Roehm Gmbh | Flüssig-Formulierungen von Enzymen |
-
1991
- 1991-03-26 CZ CS923435A patent/CZ285164B6/cs not_active IP Right Cessation
- 1991-03-26 DE DE4109826A patent/DE4109826A1/de not_active Withdrawn
-
1992
- 1992-03-19 JP JP92506477A patent/JPH05507522A/ja active Pending
- 1992-03-19 AT AT92104751T patent/ATE154396T1/de not_active IP Right Cessation
- 1992-03-19 BR BR9204797A patent/BR9204797A/pt not_active IP Right Cessation
- 1992-03-19 PL PL92297166A patent/PL168197B1/pl unknown
- 1992-03-19 AU AU14247/92A patent/AU645412B2/en not_active Ceased
- 1992-03-19 RU RU9292016365A patent/RU2052506C1/ru active
- 1992-03-19 WO PCT/DE1992/000233 patent/WO1992017613A1/de active IP Right Grant
- 1992-03-19 ES ES92104751T patent/ES2103845T3/es not_active Expired - Lifetime
- 1992-03-19 HU HU9203708A patent/HU217020B/hu not_active IP Right Cessation
- 1992-03-19 SK SK3435-92A patent/SK277863B6/sk unknown
- 1992-03-19 EP EP92104751A patent/EP0505920B1/de not_active Expired - Lifetime
- 1992-03-19 DE DE59208598T patent/DE59208598D1/de not_active Expired - Lifetime
- 1992-03-26 TW TW081102326A patent/TW203102B/zh active
- 1992-03-26 ZA ZA922207A patent/ZA922207B/xx unknown
- 1992-11-25 KR KR1019920702971A patent/KR100201731B1/ko not_active Expired - Fee Related
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR469758A (fr) * | 1914-03-18 | 1914-08-10 | Leon Krall | Procédé de mise en confit des peaux |
| DE2856320A1 (de) * | 1978-12-27 | 1980-07-17 | Roehm Gmbh | Enzymatisches beizverfahren |
| GB2233665A (en) * | 1989-07-11 | 1991-01-16 | Roehm Gmbh | Enzymatically aided soaking process for skins and hides |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2140457C1 (ru) * | 1995-02-24 | 1999-10-27 | Рем Гмбх | Водное средство для обработки шкур и голья |
Also Published As
| Publication number | Publication date |
|---|---|
| TW203102B (cs) | 1993-04-01 |
| EP0505920B1 (de) | 1997-06-11 |
| DE59208598D1 (de) | 1997-07-17 |
| CZ343592A3 (en) | 1993-08-11 |
| CZ285164B6 (cs) | 1999-05-12 |
| AU1424792A (en) | 1992-11-02 |
| DE4109826A1 (de) | 1992-11-05 |
| ES2103845T3 (es) | 1997-10-01 |
| HUT66530A (en) | 1994-12-28 |
| JPH05507522A (ja) | 1993-10-28 |
| EP0505920A1 (de) | 1992-09-30 |
| ZA922207B (en) | 1992-12-30 |
| HU9203708D0 (en) | 1993-09-28 |
| ATE154396T1 (de) | 1997-06-15 |
| HU217020B (hu) | 1999-11-29 |
| KR100201731B1 (en) | 1999-06-15 |
| SK277863B6 (en) | 1995-05-10 |
| RU2052506C1 (ru) | 1996-01-20 |
| SK343592A3 (en) | 1994-04-06 |
| AU645412B2 (en) | 1994-01-13 |
| PL168197B1 (pl) | 1996-01-31 |
| BR9204797A (pt) | 1993-08-03 |
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