IL85954A - Thermostable fungal serine proteases - Google Patents
Thermostable fungal serine proteasesInfo
- Publication number
- IL85954A IL85954A IL8595488A IL8595488A IL85954A IL 85954 A IL85954 A IL 85954A IL 8595488 A IL8595488 A IL 8595488A IL 8595488 A IL8595488 A IL 8595488A IL 85954 A IL85954 A IL 85954A
- Authority
- IL
- Israel
- Prior art keywords
- protease
- serine protease
- dna sequence
- sequence
- activity
- Prior art date
Links
- 102000012479 Serine Proteases Human genes 0.000 title claims abstract description 58
- 108010022999 Serine Proteases Proteins 0.000 title claims abstract description 58
- 230000002538 fungal effect Effects 0.000 title description 7
- 239000003599 detergent Substances 0.000 claims abstract description 56
- 239000000203 mixture Substances 0.000 claims abstract description 47
- 238000000034 method Methods 0.000 claims abstract description 28
- 230000008569 process Effects 0.000 claims abstract description 5
- 239000002299 complementary DNA Substances 0.000 claims description 38
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 27
- 108020004414 DNA Proteins 0.000 claims description 19
- 238000004519 manufacturing process Methods 0.000 claims description 16
- 150000001413 amino acids Chemical group 0.000 claims description 10
- 239000013604 expression vector Substances 0.000 claims description 7
- 239000013598 vector Substances 0.000 claims description 7
- 108091029865 Exogenous DNA Proteins 0.000 claims description 6
- 125000000729 N-terminal amino-acid group Chemical group 0.000 claims description 2
- 230000001131 transforming effect Effects 0.000 claims description 2
- 238000009472 formulation Methods 0.000 abstract description 28
- 241001523956 Parengyodontium album Species 0.000 abstract description 19
- 239000001963 growth medium Substances 0.000 abstract description 4
- 238000010188 recombinant method Methods 0.000 abstract 1
- 150000003355 serines Chemical class 0.000 abstract 1
- 108091005804 Peptidases Proteins 0.000 description 196
- 102000035195 Peptidases Human genes 0.000 description 195
- 239000004365 Protease Substances 0.000 description 171
- 235000019419 proteases Nutrition 0.000 description 147
- 108090000623 proteins and genes Proteins 0.000 description 85
- 102000004190 Enzymes Human genes 0.000 description 65
- 108090000790 Enzymes Proteins 0.000 description 65
- 229940088598 enzyme Drugs 0.000 description 65
- 230000000694 effects Effects 0.000 description 47
- 108010067770 Endopeptidase K Proteins 0.000 description 36
- 235000018102 proteins Nutrition 0.000 description 29
- 102000004169 proteins and genes Human genes 0.000 description 29
- NRTLIYOWLVMQBO-UHFFFAOYSA-N 5-chloro-1,3-dimethyl-N-(1,1,3-trimethyl-1,3-dihydro-2-benzofuran-4-yl)pyrazole-4-carboxamide Chemical compound C=12C(C)OC(C)(C)C2=CC=CC=1NC(=O)C=1C(C)=NN(C)C=1Cl NRTLIYOWLVMQBO-UHFFFAOYSA-N 0.000 description 26
- 239000000243 solution Substances 0.000 description 26
- 108090000787 Subtilisin Proteins 0.000 description 24
- 108010056079 Subtilisins Proteins 0.000 description 23
- 102000005158 Subtilisins Human genes 0.000 description 23
- 108020004999 messenger RNA Proteins 0.000 description 21
- 239000002773 nucleotide Substances 0.000 description 21
- 125000003729 nucleotide group Chemical group 0.000 description 21
- 125000003275 alpha amino acid group Chemical group 0.000 description 19
- 239000000872 buffer Substances 0.000 description 18
- 235000019833 protease Nutrition 0.000 description 18
- 230000002797 proteolythic effect Effects 0.000 description 17
- 238000002955 isolation Methods 0.000 description 16
- 238000011534 incubation Methods 0.000 description 15
- 239000013612 plasmid Substances 0.000 description 15
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 15
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 14
- 238000005119 centrifugation Methods 0.000 description 13
- 239000012634 fragment Substances 0.000 description 13
- 239000001488 sodium phosphate Substances 0.000 description 13
- 229910000162 sodium phosphate Inorganic materials 0.000 description 13
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 13
- 238000005406 washing Methods 0.000 description 13
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 12
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 11
- 230000000717 retained effect Effects 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 239000000758 substrate Substances 0.000 description 10
- 241000233866 Fungi Species 0.000 description 9
- 238000010276 construction Methods 0.000 description 9
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 9
- 239000002244 precipitate Substances 0.000 description 9
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 8
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 8
- 108010041102 azocasein Proteins 0.000 description 8
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 8
- 238000009396 hybridization Methods 0.000 description 8
- PHTQWCKDNZKARW-UHFFFAOYSA-N isoamylol Chemical compound CC(C)CCO PHTQWCKDNZKARW-UHFFFAOYSA-N 0.000 description 8
- 239000007788 liquid Substances 0.000 description 8
- 239000002751 oligonucleotide probe Substances 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 238000001712 DNA sequencing Methods 0.000 description 7
- 108091092195 Intron Proteins 0.000 description 7
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 7
- 235000001014 amino acid Nutrition 0.000 description 7
- 108010085889 azoalbumin Proteins 0.000 description 7
- 230000002255 enzymatic effect Effects 0.000 description 7
- 108091008146 restriction endonucleases Proteins 0.000 description 7
- 238000012216 screening Methods 0.000 description 7
- 229920001817 Agar Polymers 0.000 description 6
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 6
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 6
- 239000008272 agar Substances 0.000 description 6
- 229940098773 bovine serum albumin Drugs 0.000 description 6
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- 239000000020 Nitrocellulose Substances 0.000 description 5
- 238000000636 Northern blotting Methods 0.000 description 5
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 5
- 229960000723 ampicillin Drugs 0.000 description 5
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 5
- 238000010804 cDNA synthesis Methods 0.000 description 5
- 239000004202 carbamide Substances 0.000 description 5
- 239000001913 cellulose Substances 0.000 description 5
- 229920002678 cellulose Polymers 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 239000006166 lysate Substances 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- 229920001220 nitrocellulos Polymers 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 235000020183 skimmed milk Nutrition 0.000 description 5
- 241000894007 species Species 0.000 description 5
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 4
- 239000005695 Ammonium acetate Substances 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 4
- 102000053602 DNA Human genes 0.000 description 4
- 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 4
- 101000964562 Homo sapiens Zinc finger FYVE domain-containing protein 9 Proteins 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 102100040801 Zinc finger FYVE domain-containing protein 9 Human genes 0.000 description 4
- 229940043376 ammonium acetate Drugs 0.000 description 4
- 235000019257 ammonium acetate Nutrition 0.000 description 4
- 230000015556 catabolic process Effects 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 230000003287 optical effect Effects 0.000 description 4
- 239000002002 slurry Substances 0.000 description 4
- 239000004094 surface-active agent Substances 0.000 description 4
- 239000003155 DNA primer Substances 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000011543 agarose gel Substances 0.000 description 3
- -1 alkyl aryl sulphonate Chemical compound 0.000 description 3
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 3
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 3
- 235000011130 ammonium sulphate Nutrition 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 239000008367 deionised water Substances 0.000 description 3
- 229910021641 deionized water Inorganic materials 0.000 description 3
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 239000008103 glucose Substances 0.000 description 3
- 239000012139 lysis buffer Substances 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 239000004570 mortar (masonry) Substances 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 239000013600 plasmid vector Substances 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 3
- 229960004319 trichloroacetic acid Drugs 0.000 description 3
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 108010076119 Caseins Proteins 0.000 description 2
- 108091033380 Coding strand Proteins 0.000 description 2
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N DMSO Substances CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 241001524679 Escherichia virus M13 Species 0.000 description 2
- 241000223218 Fusarium Species 0.000 description 2
- 108010024636 Glutathione Proteins 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 239000006137 Luria-Bertani broth Substances 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 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
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 238000002105 Southern blotting Methods 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 229910001424 calcium ion Inorganic materials 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- 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 2
- 235000021240 caseins Nutrition 0.000 description 2
- 229960005091 chloramphenicol Drugs 0.000 description 2
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 2
- 230000002596 correlated effect Effects 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- FFYPMLJYZAEMQB-UHFFFAOYSA-N diethyl pyrocarbonate Chemical compound CCOC(=O)OC(=O)OCC FFYPMLJYZAEMQB-UHFFFAOYSA-N 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 239000007789 gas Substances 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 229960003180 glutathione Drugs 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000004276 hyalin Anatomy 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- 239000011256 inorganic filler Substances 0.000 description 2
- 229910003475 inorganic filler Inorganic materials 0.000 description 2
- 239000002198 insoluble material Substances 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 239000002808 molecular sieve Substances 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000013615 primer Substances 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 238000004153 renaturation Methods 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 2
- 108010031354 thermitase Proteins 0.000 description 2
- LOGVYQQJAJKAJB-TZYAJKAJSA-N 4-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-1-(N-nitroanilino)-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound [N+](=O)([O-])N(C1=CC=CC=C1)C([C@@H](NC([C@H]1N(CCC1)C([C@@H](NC([C@@H](NC(CCC(=O)O)=O)C)=O)C)=O)=O)CC1=CC=CC=C1)=O LOGVYQQJAJKAJB-TZYAJKAJSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- 229910002012 Aerosil® Inorganic materials 0.000 description 1
- 229910002016 Aerosil® 200 Inorganic materials 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 238000002238 CM-cellulose chromatography Methods 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102100025566 Chymotrypsin-like protease CTRL-1 Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 1
- 108090000860 Endopeptidase Clp Proteins 0.000 description 1
- KRHYYFGTRYWZRS-UHFFFAOYSA-M Fluoride anion Chemical compound [F-] KRHYYFGTRYWZRS-UHFFFAOYSA-M 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 101000856199 Homo sapiens Chymotrypsin-like protease CTRL-1 Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- JLVVSXFLKOJNIY-UHFFFAOYSA-N Magnesium ion Chemical compound [Mg+2] JLVVSXFLKOJNIY-UHFFFAOYSA-N 0.000 description 1
- 241001154030 Malbranchea pulchella Species 0.000 description 1
- 101100407828 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) ptr-3 gene Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 102100038946 Proprotein convertase subtilisin/kexin type 6 Human genes 0.000 description 1
- 241000208465 Proteaceae Species 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 241000190542 Sarocladium kiliense Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 239000004115 Sodium Silicate Substances 0.000 description 1
- 108700037663 Subtilisin-like proteases Proteins 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 125000005037 alkyl phenyl group Chemical group 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000007844 bleaching agent Substances 0.000 description 1
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011089 carbon dioxide Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- UHZZMRAGKVHANO-UHFFFAOYSA-M chlormequat chloride Chemical compound [Cl-].C[N+](C)(C)CCCl UHZZMRAGKVHANO-UHFFFAOYSA-M 0.000 description 1
- ZYWFEOZQIUMEGL-UHFFFAOYSA-N chloroform;3-methylbutan-1-ol;phenol Chemical compound ClC(Cl)Cl.CC(C)CCO.OC1=CC=CC=C1 ZYWFEOZQIUMEGL-UHFFFAOYSA-N 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000002951 depilatory effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- WLGJTMBOEAHNNY-UHFFFAOYSA-N disodium hydrogen borate phosphoric acid Chemical compound [Na+].[Na+].OB([O-])[O-].OP(O)(O)=O WLGJTMBOEAHNNY-UHFFFAOYSA-N 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 235000013312 flour Nutrition 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 229910021485 fumed silica Inorganic materials 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 235000013905 glycine and its sodium salt Nutrition 0.000 description 1
- 239000004247 glycine and its sodium salt Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000000413 hydrolysate Substances 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 238000004900 laundering Methods 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000000464 low-speed centrifugation Methods 0.000 description 1
- 229910001425 magnesium ion Inorganic materials 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000008450 motivation Effects 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 239000012457 nonaqueous media Substances 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920000151 polyglycol Polymers 0.000 description 1
- 239000010695 polyglycol Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000007065 protein hydrolysis Effects 0.000 description 1
- 230000007420 reactivation Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 239000003352 sequestering agent Substances 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 229940029258 sodium glycinate Drugs 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- WUWHFEHKUQVYLF-UHFFFAOYSA-M sodium;2-aminoacetate Chemical compound [Na+].NCC([O-])=O WUWHFEHKUQVYLF-UHFFFAOYSA-M 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H15/00—Compounds containing hydrocarbon or substituted hydrocarbon radicals directly attached to hetero atoms of saccharide radicals
- C07H15/02—Acyclic radicals, not substituted by cyclic structures
- C07H15/12—Acyclic radicals, not substituted by cyclic structures attached to a nitrogen atom of the saccharide radical
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/58—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Mycology (AREA)
- Physics & Mathematics (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Enzymes And Modification Thereof (AREA)
- Detergent Compositions (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Compositions Of Macromolecular Compounds (AREA)
- Cosmetics (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US3581687A | 1987-04-03 | 1987-04-03 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IL85954A0 IL85954A0 (en) | 1988-09-30 |
| IL85954A true IL85954A (en) | 1994-11-28 |
Family
ID=21884943
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL8595488A IL85954A (en) | 1987-04-03 | 1988-03-31 | Thermostable fungal serine proteases |
Country Status (12)
| Country | Link |
|---|---|
| EP (1) | EP0309550B1 (de) |
| JP (1) | JP2731407B2 (de) |
| KR (1) | KR970009949B1 (de) |
| AT (1) | ATE139567T1 (de) |
| AU (1) | AU617996B2 (de) |
| CA (1) | CA1331154C (de) |
| DE (1) | DE3855375T2 (de) |
| DK (1) | DK672088A (de) |
| FI (1) | FI100602B (de) |
| IL (1) | IL85954A (de) |
| NO (1) | NO179217C (de) |
| WO (1) | WO1988007581A1 (de) |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8726999D0 (en) * | 1987-11-18 | 1987-12-23 | Unilever Plc | Enzymatic liquid detergent composition |
| US5288627A (en) * | 1988-01-07 | 1994-02-22 | Novo Nordisk A/S | Endoprotease from Fusarium oxysporumDSM 2672 for use in detergents |
| CA2069147A1 (en) * | 1991-05-22 | 1992-11-23 | Kazuaki Kitano | Dna and its use |
| EP0623672A1 (de) * | 1993-05-04 | 1994-11-09 | Research Institute For Plant Protection | Alkalische Serine-Protease von Paecilomyces lilacinus |
| DE10001140C2 (de) * | 2000-01-13 | 2003-06-12 | Gsf Forschungszentrum Umwelt | Oligonukleotide zur Amplifikation und zum Nachweis von bakteriellen Genen für extrazelluläre alkalische Metallopeptidasen (Apr), neutrale Metallopeptidasen (Npr) und Serinpeptidasen (Spr) |
| DE10105911A1 (de) | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Expression der rekombinanten Proteinase K aus Tritirachium album in Hefe |
| DE10105912A1 (de) * | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Rekombinante Proteinase K |
| DE10153792A1 (de) | 2001-10-31 | 2003-05-22 | Henkel Kgaa | Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten |
| DE10162728A1 (de) | 2001-12-20 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus gibsonii (DSM 14393) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease |
| DE10162727A1 (de) | 2001-12-20 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus gibsonii (DSM 14391) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease |
| DE10163884A1 (de) | 2001-12-22 | 2003-07-10 | Henkel Kgaa | Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease |
| EP1678296B1 (de) * | 2003-10-23 | 2011-07-13 | Novozymes A/S | Protease mit verbesserter stabilität in detergentien |
| DE10360805A1 (de) | 2003-12-23 | 2005-07-28 | Henkel Kgaa | Neue Alkalische Protease und Wasch- und Reinigungsmittel, enthaltend diese neue Alkalische Protease |
| DE102004019751A1 (de) | 2004-04-23 | 2005-11-17 | Henkel Kgaa | Neue Alkalische Proteasen und Wasch- und Reinigungsmittel, enthaltend diese neuen Alkalischen Proteasen |
| FI121712B (fi) | 2009-04-30 | 2011-03-15 | Ab Enzymes Oy | Uusi sieniperäinen proteaasi ja sen käyttö |
| FI121711B (fi) | 2009-04-30 | 2011-03-15 | Ab Enzymes Oy | Sieniperäinen seriiniproteaasi ja sen käyttö |
| FI121851B (fi) | 2009-07-08 | 2011-05-13 | Ab Enzymes Oy | Sieniperäinen proteaasi ja sen käyttö |
| FI123942B (fi) | 2010-10-29 | 2013-12-31 | Ab Enzymes Oy | Sieniperäisen seriiniproteaasin variantteja |
| FI123425B (fi) | 2011-03-31 | 2013-04-30 | Ab Enzymes Oy | Proteaasientsyymi ja sen käytöt |
| CN108603187A (zh) * | 2015-11-24 | 2018-09-28 | 诺维信公司 | 具有蛋白酶活性的多肽以及编码它们的多核苷酸 |
| EP3636735B1 (de) | 2018-10-12 | 2024-03-27 | AB Enzymes Oy | Variante einer protease und die verwendung davon |
| WO2023225459A2 (en) | 2022-05-14 | 2023-11-23 | Novozymes A/S | Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1240058A (en) * | 1968-04-12 | 1971-07-21 | Procter & Gamble | Enzyme-containing detergent compositions |
| US3623957A (en) * | 1970-01-21 | 1971-11-30 | Baxter Laboratories Inc | Preparation of microbial alkaline protease by fermentation with bacillus subtilis, variety licheniformis |
| WO1988003448A1 (en) * | 1986-11-14 | 1988-05-19 | Erich Goergens | Process and device for transmitting or supporting deformation energy |
| PT89702B (pt) * | 1988-02-11 | 1994-04-29 | Gist Brocades Nv | Processo para a preparacao de novos enzimas proteoliticos e de detergentes que os contem |
-
1988
- 1988-03-28 AT AT88903675T patent/ATE139567T1/de not_active IP Right Cessation
- 1988-03-28 WO PCT/US1988/001040 patent/WO1988007581A1/en not_active Ceased
- 1988-03-28 AU AU15716/88A patent/AU617996B2/en not_active Expired
- 1988-03-28 DE DE3855375T patent/DE3855375T2/de not_active Expired - Lifetime
- 1988-03-28 EP EP88903675A patent/EP0309550B1/de not_active Expired - Lifetime
- 1988-03-28 JP JP63503271A patent/JP2731407B2/ja not_active Expired - Lifetime
- 1988-03-31 CA CA000563169A patent/CA1331154C/en not_active Expired - Lifetime
- 1988-03-31 IL IL8595488A patent/IL85954A/en not_active IP Right Cessation
- 1988-12-02 FI FI885635A patent/FI100602B/fi not_active IP Right Cessation
- 1988-12-02 NO NO885391A patent/NO179217C/no not_active IP Right Cessation
- 1988-12-02 DK DK672088A patent/DK672088A/da not_active Application Discontinuation
- 1988-12-03 KR KR88701597A patent/KR970009949B1/ko not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| DE3855375T2 (de) | 1996-11-14 |
| DK672088D0 (da) | 1988-12-02 |
| CA1331154C (en) | 1994-08-02 |
| EP0309550A1 (de) | 1989-04-05 |
| KR970009949B1 (en) | 1997-06-19 |
| NO885391D0 (no) | 1988-12-02 |
| NO179217C (no) | 1996-08-28 |
| JP2731407B2 (ja) | 1998-03-25 |
| FI885635L (fi) | 1988-12-02 |
| EP0309550B1 (de) | 1996-06-19 |
| JPH01502798A (ja) | 1989-09-28 |
| EP0309550A4 (de) | 1990-01-08 |
| KR890700675A (ko) | 1989-04-26 |
| AU617996B2 (en) | 1991-12-12 |
| DE3855375D1 (de) | 1996-07-25 |
| IL85954A0 (en) | 1988-09-30 |
| NO179217B (no) | 1996-05-20 |
| DK672088A (da) | 1989-02-03 |
| NO885391L (no) | 1989-02-03 |
| WO1988007581A1 (en) | 1988-10-06 |
| FI885635A0 (fi) | 1988-12-02 |
| ATE139567T1 (de) | 1996-07-15 |
| AU1571688A (en) | 1988-11-02 |
| FI100602B (fi) | 1998-01-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP0309550B1 (de) | Proteolytische enzyme | |
| JP2726799B2 (ja) | 変異ズブチリシン | |
| EP0290567B1 (de) | Bei niedriger temperatur aktive alkalische protease aus nocardiopsis dassonvillei und deren herstellung | |
| FI112500B (fi) | Mutatoitu subtilisiiniproteaasi | |
| JP2590247B2 (ja) | スブチリシンアナログ | |
| KR100601189B1 (ko) | 알카리 프로테아제 | |
| RU2566549C2 (ru) | Новая протеаза грибов и ее применение | |
| US8609390B2 (en) | Fungal serine protease and use thereof | |
| CN102994486A (zh) | 在洗涤剂中具有改善稳定性的蛋白酶 | |
| WO1994025583A1 (en) | A recombinant trypsin-like protease | |
| US5278062A (en) | Proteolytic enzymes | |
| EP2691520B1 (de) | Proteaseenzym und seine verwendungen | |
| US5646028A (en) | Alkaline serine protease streptomyces griseus var. alkaliphus having enhanced stability against urea or guanidine | |
| Singh et al. | Purification and characterization of two extracellular alkaline proteases from a newly isolated obligate alkalophilic Bacillus sphaericus | |
| EP3665298A1 (de) | Aus o. corvina gewonnene, neutrale, wärmeempfindliche serinprotease | |
| CN115260314A (zh) | 一种重组嗜热中性蛋白酶及其在降解蛋白质中的应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| RH | Patent void | ||
| NE | Application for restoration - patent lapsed through non-payment of renewal fees (section 60, patents law, 5727-1967) | ||
| KB | Patent renewed | ||
| MM9K | Patent not in force due to non-payment of renewal fees | ||
| NE | Application for restoration - patent lapsed through non-payment of renewal fees (section 60, patents law, 5727-1967) | ||
| KB | Patent renewed | ||
| EXP | Patent expired |