LT3963B - Enzymatic product containing mutant proteolytic enzyme, process for selecting proteolytic enzyme, mutant gene, expression vector, procariotic host-strain, process for preparing mutant proteolytic enzyme, detergent composition - Google Patents

Enzymatic product containing mutant proteolytic enzyme, process for selecting proteolytic enzyme, mutant gene, expression vector, procariotic host-strain, process for preparing mutant proteolytic enzyme, detergent composition Download PDF

Info

Publication number: LT3963B
Authority: LT; Lithuania
Prior art keywords: protease; amino acid; mutant; enzyme; enzymatic product
Prior art date: 1988-02-11

Application number

LTIP1650A

Other languages

English (en)

Lithuanian (lt)

Inventor

Christiaan Albertus Vaneekelen

Leonardus Johannes S Mulleners

Johannes Cornelis Vanderlaan

Onno Misset

Roelck Anneke Cuperus

Johan Herman Albert Lensink

Original Assignee

Gist Brocades Nv

Priority date (The priority date 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 date listed.)

1988-02-11

Filing date

1993-12-21

Publication date

1996-05-27

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=8199752&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=LT3963(B) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1993-12-21 Application filed by Gist Brocades Nv filed Critical Gist Brocades Nv

1995-07-25 Publication of LTIP1650A publication Critical patent/LTIP1650A/xx

1996-05-27 Publication of LT3963B publication Critical patent/LT3963B/lt

Links

108091005804 Peptidases Proteins 0.000 title claims abstract description 258
102000035195 Peptidases Human genes 0.000 title claims abstract description 242
239000003599 detergent Substances 0.000 title claims abstract description 99
108090000623 proteins and genes Proteins 0.000 title claims abstract description 46
239000000203 mixture Substances 0.000 title claims description 44
238000000034 method Methods 0.000 title claims description 40
230000002255 enzymatic effect Effects 0.000 title claims description 27
239000013604 expression vector Substances 0.000 title claims description 5
238000004519 manufacturing process Methods 0.000 title description 8
230000008569 process Effects 0.000 title description 3
102000004190 Enzymes Human genes 0.000 claims abstract description 80
108090000790 Enzymes Proteins 0.000 claims abstract description 80
229940088598 enzyme Drugs 0.000 claims abstract description 80
150000001413 amino acids Chemical group 0.000 claims abstract description 53
241000193830 Bacillus <bacterium> Species 0.000 claims abstract description 20
229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 claims abstract description 20
108010022999 Serine Proteases Proteins 0.000 claims abstract description 12
102000012479 Serine Proteases Human genes 0.000 claims abstract description 12
239000004365 Protease Substances 0.000 claims description 201
238000005406 washing Methods 0.000 claims description 97
230000035772 mutation Effects 0.000 claims description 42
238000002703 mutagenesis Methods 0.000 claims description 20
231100000350 mutagenesis Toxicity 0.000 claims description 20
239000012634 fragment Substances 0.000 claims description 12
-1 aliphatic amino acid Chemical class 0.000 claims description 11
239000007800 oxidant agent Substances 0.000 claims description 9
239000002253 acid Substances 0.000 claims description 8
235000014469 Bacillus subtilis Nutrition 0.000 claims description 7
230000002797 proteolythic effect Effects 0.000 claims description 7
230000009466 transformation Effects 0.000 claims description 6
239000000654 additive Substances 0.000 claims description 5
230000007935 neutral effect Effects 0.000 claims description 5
241000894007 species Species 0.000 claims description 5
241000194108 Bacillus licheniformis Species 0.000 claims description 4
229930182817 methionine Natural products 0.000 claims description 4
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 3
230000001580 bacterial effect Effects 0.000 claims description 3
238000000855 fermentation Methods 0.000 claims description 3
230000004151 fermentation Effects 0.000 claims description 3
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 2
230000000996 additive effect Effects 0.000 claims description 2
238000012258 culturing Methods 0.000 claims description 2
229940024606 amino acid Drugs 0.000 claims 21
238000006467 substitution reaction Methods 0.000 claims 5
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims 2
239000004471 Glycine Substances 0.000 claims 2
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 2
125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims 2
241001150538 Iria Species 0.000 claims 1
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims 1
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims 1
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims 1
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims 1
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims 1
229960000310 isoleucine Drugs 0.000 claims 1
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims 1
230000001590 oxidative effect Effects 0.000 claims 1
125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims 1
125000000446 sulfanediyl group Chemical group *S* 0.000 claims 1
239000004474 valine Substances 0.000 claims 1
108700026220 vif Genes Proteins 0.000 claims 1
230000014509 gene expression Effects 0.000 abstract description 12
230000001747 exhibiting effect Effects 0.000 abstract 1
230000000694 effects Effects 0.000 description 52
238000012360 testing method Methods 0.000 description 31
239000000843 powder Substances 0.000 description 25
239000007788 liquid Substances 0.000 description 21
210000001519 tissue Anatomy 0.000 description 20
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 18
235000018102 proteins Nutrition 0.000 description 16
102000004169 proteins and genes Human genes 0.000 description 16
239000013598 vector Substances 0.000 description 15
239000007844 bleaching agent Substances 0.000 description 14
239000000243 solution Substances 0.000 description 14
108020004414 DNA Proteins 0.000 description 13
239000000758 substrate Substances 0.000 description 13
238000003860 storage Methods 0.000 description 11
108090000787 Subtilisin Proteins 0.000 description 10
CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 9
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
238000012986 modification Methods 0.000 description 9
230000004048 modification Effects 0.000 description 9
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 8
IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
108010056079 Subtilisins Proteins 0.000 description 8
102000005158 Subtilisins Human genes 0.000 description 8
238000010276 construction Methods 0.000 description 8
239000004744 fabric Substances 0.000 description 8
239000008187 granular material Substances 0.000 description 8
108010076119 Caseins Proteins 0.000 description 7
239000005018 casein Substances 0.000 description 7
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 7
235000021240 caseins Nutrition 0.000 description 7
239000012418 sodium perborate tetrahydrate Substances 0.000 description 7
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 6
108091008146 restriction endonucleases Proteins 0.000 description 6
229920000742 Cotton Polymers 0.000 description 5
108091034117 Oligonucleotide Proteins 0.000 description 5
150000007513 acids Chemical class 0.000 description 5
238000001962 electrophoresis Methods 0.000 description 5
238000002474 experimental method Methods 0.000 description 5
239000006260 foam Substances 0.000 description 5
238000002360 preparation method Methods 0.000 description 5
239000000047 product Substances 0.000 description 5
238000012216 screening Methods 0.000 description 5
238000002741 site-directed mutagenesis Methods 0.000 description 5
IBDSNZLUHYKHQP-UHFFFAOYSA-N sodium;3-oxidodioxaborirane;tetrahydrate Chemical compound O.O.O.O.[Na+].[O-]B1OO1 IBDSNZLUHYKHQP-UHFFFAOYSA-N 0.000 description 5
102000053602 DNA Human genes 0.000 description 4
241000588724 Escherichia coli Species 0.000 description 4
229930193140 Neomycin Natural products 0.000 description 4
108091028043 Nucleic acid sequence Proteins 0.000 description 4
229910010413 TiO 2 Inorganic materials 0.000 description 4
125000000129 anionic group Chemical group 0.000 description 4
238000003556 assay Methods 0.000 description 4
210000004027 cell Anatomy 0.000 description 4
238000009472 formulation Methods 0.000 description 4
239000003112 inhibitor Substances 0.000 description 4
238000002955 isolation Methods 0.000 description 4
108010020132 microbial serine proteinases Proteins 0.000 description 4
244000005700 microbiome Species 0.000 description 4
229960004927 neomycin Drugs 0.000 description 4
239000002773 nucleotide Substances 0.000 description 4
230000003647 oxidation Effects 0.000 description 4
238000007254 oxidation reaction Methods 0.000 description 4
239000002245 particle Substances 0.000 description 4
229920000036 polyvinylpyrrolidone Polymers 0.000 description 4
235000013855 polyvinylpyrrolidone Nutrition 0.000 description 4
238000000746 purification Methods 0.000 description 4
239000011734 sodium Substances 0.000 description 4
239000011780 sodium chloride Substances 0.000 description 4
239000004094 surface-active agent Substances 0.000 description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
NLZUEZXRPGMBCV-UHFFFAOYSA-N Butylhydroxytoluene Chemical compound CC1=CC(C(C)(C)C)=C(O)C(C(C)(C)C)=C1 NLZUEZXRPGMBCV-UHFFFAOYSA-N 0.000 description 3
241000282326 Felis catus Species 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
BGRWYDHXPHLNKA-UHFFFAOYSA-N Tetraacetylethylenediamine Chemical compound CC(=O)N(C(C)=O)CCN(C(C)=O)C(C)=O BGRWYDHXPHLNKA-UHFFFAOYSA-N 0.000 description 3
125000001931 aliphatic group Chemical group 0.000 description 3
230000008901 benefit Effects 0.000 description 3
239000008280 blood Substances 0.000 description 3
210000004369 blood Anatomy 0.000 description 3
238000006243 chemical reaction Methods 0.000 description 3
238000010367 cloning Methods 0.000 description 3
150000001875 compounds Chemical class 0.000 description 3
238000010790 dilution Methods 0.000 description 3
239000012895 dilution Substances 0.000 description 3
238000005516 engineering process Methods 0.000 description 3
238000004128 high performance liquid chromatography Methods 0.000 description 3
238000011534 incubation Methods 0.000 description 3
238000005259 measurement Methods 0.000 description 3
125000003729 nucleotide group Chemical group 0.000 description 3
239000008363 phosphate buffer Substances 0.000 description 3
239000012064 sodium phosphate buffer Substances 0.000 description 3
229910001220 stainless steel Inorganic materials 0.000 description 3
239000010935 stainless steel Substances 0.000 description 3
238000004448 titration Methods 0.000 description 3
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 2
229920000936 Agarose Polymers 0.000 description 2
241000193744 Bacillus amyloliquefaciens Species 0.000 description 2
244000063299 Bacillus subtilis Species 0.000 description 2
244000025254 Cannabis sativa Species 0.000 description 2
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 2
KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
239000007993 MOPS buffer Substances 0.000 description 2
108010049190 N,N-dimethylcasein Proteins 0.000 description 2
229910019142 PO4 Inorganic materials 0.000 description 2
108010076504 Protein Sorting Signals Proteins 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
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
230000008033 biological extinction Effects 0.000 description 2
239000000872 buffer Substances 0.000 description 2
239000002775 capsule Substances 0.000 description 2
125000002091 cationic group Chemical group 0.000 description 2
235000019219 chocolate Nutrition 0.000 description 2
238000004587 chromatography analysis Methods 0.000 description 2
238000004140 cleaning Methods 0.000 description 2
238000012217 deletion Methods 0.000 description 2
230000037430 deletion Effects 0.000 description 2
238000010586 diagram Methods 0.000 description 2
XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
238000004851 dishwashing Methods 0.000 description 2
POULHZVOKOAJMA-UHFFFAOYSA-N dodecanoic acid Chemical compound CCCCCCCCCCCC(O)=O POULHZVOKOAJMA-UHFFFAOYSA-N 0.000 description 2
238000009585 enzyme analysis Methods 0.000 description 2
239000012847 fine chemical Substances 0.000 description 2
238000002523 gelfiltration Methods 0.000 description 2
230000002779 inactivation Effects 0.000 description 2
239000000463 material Substances 0.000 description 2
230000007246 mechanism Effects 0.000 description 2
239000002609 medium Substances 0.000 description 2
238000002844 melting Methods 0.000 description 2
230000008018 melting Effects 0.000 description 2
230000000813 microbial effect Effects 0.000 description 2
238000002156 mixing Methods 0.000 description 2
108020004707 nucleic acids Proteins 0.000 description 2
102000039446 nucleic acids Human genes 0.000 description 2
150000007523 nucleic acids Chemical class 0.000 description 2
230000037361 pathway Effects 0.000 description 2
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
239000010452 phosphate Substances 0.000 description 2
229920002401 polyacrylamide Polymers 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
108090000765 processed proteins & peptides Proteins 0.000 description 2
230000003362 replicative effect Effects 0.000 description 2
238000012552 review Methods 0.000 description 2
230000028327 secretion Effects 0.000 description 2
239000000344 soap Substances 0.000 description 2
229910052708 sodium Inorganic materials 0.000 description 2
229960001922 sodium perborate Drugs 0.000 description 2
235000019832 sodium triphosphate Nutrition 0.000 description 2
YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 2
239000000126 substance Substances 0.000 description 2
QQGISFDJEJMKIL-JAIQZWGSSA-N (5z)-5-[[3-(hydroxymethyl)thiophen-2-yl]methylidene]-10-methoxy-2,2,4-trimethyl-1h-chromeno[3,4-f]quinolin-9-ol Polymers C1=CC=2NC(C)(C)C=C(C)C=2C2=C1C=1C(OC)=C(O)C=CC=1O\C2=C/C=1SC=CC=1CO QQGISFDJEJMKIL-JAIQZWGSSA-N 0.000 description 1
WRIDQFICGBMAFQ-UHFFFAOYSA-N (E)-8-Octadecenoic acid Natural products CCCCCCCCCC=CCCCCCCC(O)=O WRIDQFICGBMAFQ-UHFFFAOYSA-N 0.000 description 1
DNIAPMSPPWPWGF-GSVOUGTGSA-N (R)-(-)-Propylene glycol Chemical compound C[C@@H](O)CO DNIAPMSPPWPWGF-GSVOUGTGSA-N 0.000 description 1
XVGXMXZUJNAGFZ-VOTSOKGWSA-N (e)-1-imidazol-1-yl-3-phenylprop-2-en-1-one Chemical compound C1=CN=CN1C(=O)\C=C\C1=CC=CC=C1 XVGXMXZUJNAGFZ-VOTSOKGWSA-N 0.000 description 1
OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
FCKKYKUOPXGLCY-XXAVUKJNSA-N 2-[bis(2-hydroxyethyl)amino]ethanol;dodecanoic acid;(z)-octadec-9-enoic acid Chemical compound OCCN(CCO)CCO.CCCCCCCCCCCC(O)=O.CCCCCCCC\C=C/CCCCCCCC(O)=O FCKKYKUOPXGLCY-XXAVUKJNSA-N 0.000 description 1
LQJBNNIYVWPHFW-UHFFFAOYSA-N 20:1omega9c fatty acid Natural products CCCCCCCCCCC=CCCCCCCCC(O)=O LQJBNNIYVWPHFW-UHFFFAOYSA-N 0.000 description 1
QJRVOJKLQNSNDB-UHFFFAOYSA-N 4-dodecan-3-ylbenzenesulfonic acid Chemical compound CCCCCCCCCC(CC)C1=CC=C(S(O)(=O)=O)C=C1 QJRVOJKLQNSNDB-UHFFFAOYSA-N 0.000 description 1
QSBYPNXLFMSGKH-UHFFFAOYSA-N 9-Heptadecensaeure Natural products CCCCCCCC=CCCCCCCCC(O)=O QSBYPNXLFMSGKH-UHFFFAOYSA-N 0.000 description 1
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
101710184263 Alkaline serine protease Proteins 0.000 description 1
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 1
208000035404 Autolysis Diseases 0.000 description 1
206010057248 Cell death Diseases 0.000 description 1
KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
102000010911 Enzyme Precursors Human genes 0.000 description 1
108010062466 Enzyme Precursors Proteins 0.000 description 1
108010054147 Hemoglobins Proteins 0.000 description 1
102000001554 Hemoglobins Human genes 0.000 description 1
125000002066 L-histidyl group Chemical group [H]N1C([H])=NC(C([H])([H])[C@](C(=O)[*])([H])N([H])[H])=C1[H] 0.000 description 1
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
239000005639 Lauric acid Substances 0.000 description 1
102000003960 Ligases Human genes 0.000 description 1
108090000364 Ligases Proteins 0.000 description 1
GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
ZFMITUMMTDLWHR-UHFFFAOYSA-N Minoxidil Chemical compound NC1=[N+]([O-])C(N)=CC(N2CCCCC2)=N1 ZFMITUMMTDLWHR-UHFFFAOYSA-N 0.000 description 1
238000005481 NMR spectroscopy Methods 0.000 description 1
RSPISYXLHRIGJD-UHFFFAOYSA-N OOOO Chemical compound OOOO RSPISYXLHRIGJD-UHFFFAOYSA-N 0.000 description 1
239000005642 Oleic acid Substances 0.000 description 1
ZQPPMHVWECSIRJ-UHFFFAOYSA-N Oleic acid Natural products CCCCCCCCC=CCCCCCCCC(O)=O ZQPPMHVWECSIRJ-UHFFFAOYSA-N 0.000 description 1
239000005662 Paraffin oil Substances 0.000 description 1
101710173835 Penton protein Proteins 0.000 description 1
206010037660 Pyrexia Diseases 0.000 description 1
239000004115 Sodium Silicate Substances 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
239000004473 Threonine Substances 0.000 description 1
GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
230000009471 action Effects 0.000 description 1
239000012190 activator Substances 0.000 description 1
239000004480 active ingredient Substances 0.000 description 1
150000001298 alcohols Polymers 0.000 description 1
150000001335 aliphatic alkanes Chemical group 0.000 description 1
125000000217 alkyl group Chemical group 0.000 description 1
150000008051 alkyl sulfates Chemical class 0.000 description 1
230000004075 alteration Effects 0.000 description 1
239000003945 anionic surfactant Substances 0.000 description 1
125000003118 aryl group Chemical group 0.000 description 1
229940077388 benzenesulfonate Drugs 0.000 description 1
SRSXLGNVWSONIS-UHFFFAOYSA-M benzenesulfonate Chemical compound [O-]S(=O)(=O)C1=CC=CC=C1 SRSXLGNVWSONIS-UHFFFAOYSA-M 0.000 description 1
230000001851 biosynthetic effect Effects 0.000 description 1
229910021538 borax Inorganic materials 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 1
238000012219 cassette mutagenesis Methods 0.000 description 1
230000003197 catalytic effect Effects 0.000 description 1
238000005341 cation exchange Methods 0.000 description 1
238000005277 cation exchange chromatography Methods 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
230000003749 cleanliness Effects 0.000 description 1
238000011109 contamination Methods 0.000 description 1
NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
238000012937 correction Methods 0.000 description 1
239000012531 culture fluid Substances 0.000 description 1
238000005202 decontamination Methods 0.000 description 1
230000003588 decontaminative effect Effects 0.000 description 1
230000007547 defect Effects 0.000 description 1
230000002950 deficient Effects 0.000 description 1
238000004925 denaturation Methods 0.000 description 1
230000036425 denaturation Effects 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
229910001873 dinitrogen Inorganic materials 0.000 description 1
238000005538 encapsulation Methods 0.000 description 1
230000009144 enzymatic modification Effects 0.000 description 1
AJIPIJNNOJSSQC-NYLIRDPKSA-N estetrol Chemical compound OC1=CC=C2[C@H]3CC[C@](C)([C@H]([C@H](O)[C@@H]4O)O)[C@@H]4[C@@H]3CCC2=C1 AJIPIJNNOJSSQC-NYLIRDPKSA-N 0.000 description 1
238000011049 filling Methods 0.000 description 1
239000000706 filtrate Substances 0.000 description 1
238000001914 filtration Methods 0.000 description 1
239000010419 fine particle Substances 0.000 description 1
230000005021 gait Effects 0.000 description 1
238000001502 gel electrophoresis Methods 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
238000010353 genetic engineering Methods 0.000 description 1
238000005469 granulation Methods 0.000 description 1
230000003179 granulation Effects 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
235000008216 herbs Nutrition 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
229910052739 hydrogen Inorganic materials 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
239000012535 impurity Substances 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
238000009776 industrial production Methods 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
230000000977 initiatory effect Effects 0.000 description 1
239000000976 ink Substances 0.000 description 1
238000003780 insertion Methods 0.000 description 1
230000037431 insertion Effects 0.000 description 1
230000010354 integration Effects 0.000 description 1
238000011835 investigation Methods 0.000 description 1
QXJSBBXBKPUZAA-UHFFFAOYSA-N isooleic acid Natural products CCCCCCCC=CCCCCCCCCC(O)=O QXJSBBXBKPUZAA-UHFFFAOYSA-N 0.000 description 1
238000009533 lab test Methods 0.000 description 1
238000012417 linear regression Methods 0.000 description 1
239000006194 liquid suspension Substances 0.000 description 1
210000004185 liver Anatomy 0.000 description 1
HCWCAKKEBCNQJP-UHFFFAOYSA-N magnesium orthosilicate Chemical compound [Mg+2].[Mg+2].[O-][Si]([O-])([O-])[O-] HCWCAKKEBCNQJP-UHFFFAOYSA-N 0.000 description 1
239000000395 magnesium oxide Substances 0.000 description 1
CPLXHLVBOLITMK-UHFFFAOYSA-N magnesium oxide Inorganic materials [Mg]=O CPLXHLVBOLITMK-UHFFFAOYSA-N 0.000 description 1
239000000391 magnesium silicate Substances 0.000 description 1
229910052919 magnesium silicate Inorganic materials 0.000 description 1
235000019792 magnesium silicate Nutrition 0.000 description 1
AXZKOIWUVFPNLO-UHFFFAOYSA-N magnesium;oxygen(2-) Chemical compound [O-2].[Mg+2] AXZKOIWUVFPNLO-UHFFFAOYSA-N 0.000 description 1
238000012423 maintenance Methods 0.000 description 1
239000011159 matrix material Substances 0.000 description 1
125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
235000013336 milk Nutrition 0.000 description 1
239000008267 milk Substances 0.000 description 1
210000004080 milk Anatomy 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
DNIAPMSPPWPWGF-UHFFFAOYSA-N monopropylene glycol Natural products CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 1
231100000219 mutagenic Toxicity 0.000 description 1
230000003505 mutagenic effect Effects 0.000 description 1
ZQPPMHVWECSIRJ-KTKRTIGZSA-N oleic acid Chemical compound CCCCCCCC\C=C/CCCCCCCC(O)=O ZQPPMHVWECSIRJ-KTKRTIGZSA-N 0.000 description 1
239000006072 paste Substances 0.000 description 1
239000008188 pellet Substances 0.000 description 1
HWGNBUXHKFFFIH-UHFFFAOYSA-I pentasodium;[oxido(phosphonatooxy)phosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O HWGNBUXHKFFFIH-UHFFFAOYSA-I 0.000 description 1
210000001322 periplasm Anatomy 0.000 description 1
230000002688 persistence Effects 0.000 description 1
239000013612 plasmid Substances 0.000 description 1
229920000728 polyester Polymers 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
239000001267 polyvinylpyrrolidone Substances 0.000 description 1
IOLCXVTUBQKXJR-UHFFFAOYSA-M potassium bromide Chemical class [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
230000001376 precipitating effect Effects 0.000 description 1
235000019260 propionic acid Nutrition 0.000 description 1
229960004063 propylene glycol Drugs 0.000 description 1
235000013772 propylene glycol Nutrition 0.000 description 1
238000002731 protein assay Methods 0.000 description 1
230000006337 proteolytic cleavage Effects 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
230000005855 radiation Effects 0.000 description 1
238000002708 random mutagenesis Methods 0.000 description 1
238000002310 reflectometry Methods 0.000 description 1
238000009877 rendering Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
230000028043 self proteolysis Effects 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000012163 sequencing technique Methods 0.000 description 1
238000007873 sieving Methods 0.000 description 1
239000001632 sodium acetate Substances 0.000 description 1
235000017281 sodium acetate Nutrition 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
239000001488 sodium phosphate Substances 0.000 description 1
229910000162 sodium phosphate Inorganic materials 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
239000004328 sodium tetraborate Substances 0.000 description 1
235000010339 sodium tetraborate Nutrition 0.000 description 1
239000002904 solvent Substances 0.000 description 1
239000002594 sorbent Substances 0.000 description 1
239000000600 sorbitol Substances 0.000 description 1
238000013112 stability test Methods 0.000 description 1
238000012430 stability testing Methods 0.000 description 1
239000003381 stabilizer Substances 0.000 description 1
230000000087 stabilizing effect Effects 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
238000000528 statistical test Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000000725 suspension Substances 0.000 description 1
230000002459 sustained effect Effects 0.000 description 1
230000002195 synergetic effect Effects 0.000 description 1
239000008399 tap water Substances 0.000 description 1
235000020679 tap water Nutrition 0.000 description 1
230000002277 temperature effect Effects 0.000 description 1
238000010998 test method Methods 0.000 description 1
239000012085 test solution Substances 0.000 description 1
150000004685 tetrahydrates Chemical class 0.000 description 1
238000013518 transcription Methods 0.000 description 1
230000035897 transcription Effects 0.000 description 1
238000012546 transfer Methods 0.000 description 1
238000013519 translation Methods 0.000 description 1
YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
239000012137 tryptone Substances 0.000 description 1
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
230000003442 weekly effect Effects 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

Classifications

- 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)
- 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
- 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)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus

Landscapes

Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
Wood Science & Technology (AREA)
Organic Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
Molecular Biology (AREA)
General Engineering & Computer Science (AREA)
Microbiology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Oil, Petroleum & Natural Gas (AREA)
Chemical Kinetics & Catalysis (AREA)
Physics & Mathematics (AREA)
Biophysics (AREA)
Plant Pathology (AREA)
Detergent Compositions (AREA)
Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Immobilizing And Processing Of Enzymes And Microorganisms (AREA)

LTIP1650A 1988-02-11 1993-12-21 Enzymatic product containing mutant proteolytic enzyme, process for selecting proteolytic enzyme, mutant gene, expression vector, procariotic host-strain, process for preparing mutant proteolytic enzyme, detergent composition LT3963B (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
EP88200255		1988-02-11

Publications (2)

Publication Number	Publication Date
LTIP1650A LTIP1650A (en)	1995-07-25
LT3963B true LT3963B (en)	1996-05-27

Family

ID=8199752

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
LTIP1650A LT3963B (en)	1988-02-11	1993-12-21	Enzymatic product containing mutant proteolytic enzyme, process for selecting proteolytic enzyme, mutant gene, expression vector, procariotic host-strain, process for preparing mutant proteolytic enzyme, detergent composition

Country Status (21)

Country	Link
US (1)	US5336611A (fr)
EP (3)	EP0571049B2 (fr)
JP (1)	JP2849141B2 (fr)
KR (1)	KR970005249B1 (fr)
CN (1)	CN1056187C (fr)
AT (1)	ATE250669T1 (fr)
AU (1)	AU629814B2 (fr)
BG (1)	BG60566B1 (fr)
BR (1)	BR8905580A (fr)
CA (1)	CA1340366C (fr)
DE (2)	DE68912359T3 (fr)
DK (1)	DK175813B1 (fr)
ES (1)	ES2061929T5 (fr)
FI (1)	FI105481B (fr)
GR (1)	GR3021934T3 (fr)
IE (2)	IE940164L (fr)
LT (1)	LT3963B (fr)
LV (1)	LV10652B (fr)
PT (1)	PT89702B (fr)
RU (1)	RU2069695C1 (fr)
WO (1)	WO1989007642A1 (fr)

Families Citing this family (127)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4760025A (en) *	1984-05-29	1988-07-26	Genencor, Inc.	Modified enzymes and methods for making same
US5185258A (en) †	1984-05-29	1993-02-09	Genencor International, Inc.	Subtilisin mutants
JP2731407B2 (ja) *	1987-04-03	1998-03-25	アムジエン・インコーポレーテツド	新規なプロテアーゼ酵素
US6287841B1 (en) *	1988-02-11	2001-09-11	Genencor International, Inc.	High alkaline serine protease
US5665587A (en) *	1989-06-26	1997-09-09	Novo Nordisk A/S	Modified subtilisins and detergent compositions containing same
BR9006827A (pt) *	1989-06-26	1991-08-06	Unilever Nv	Composicoes detergentes enzimaticas
EP0414297B1 (fr) *	1989-08-11	1996-10-16	Gist-Brocades N.V.	Production effective de protéases mutantes
DE4023458A1 (de) *	1989-08-31	1991-03-07	Kali Chemie Ag	Neue hochalkalische proteasen
US5352603A (en) *	1989-08-31	1994-10-04	Kali-Chemie Ag	Highly alkaline proteases
US6271012B1 (en) *	1989-10-11	2001-08-07	Genencor International, Inc.	Protease muteins and their use in detergents
DK97190D0 (da) *	1990-04-19	1990-04-19	Novo Nordisk As	Oxidationsstabile detergentenzymer
DK271490D0 (da) *	1990-11-14	1990-11-14	Novo Nordisk As	Detergentkomposition
EP0486073B1 (fr) *	1990-11-14	1996-07-24	The Procter & Gamble Company	Composition détergente liquide contenant une lipase et une protéase
US5733473A (en) *	1990-11-14	1998-03-31	The Procter & Gamble Company	Liquid detergent composition containing lipase and protease
GB9027836D0 (en) *	1990-12-21	1991-02-13	Unilever Plc	Enzymes and enzymatic detergent compositions
US5482849A (en) *	1990-12-21	1996-01-09	Novo Nordisk A/S	Subtilisin mutants
DE4106525A1 (de) *	1991-03-01	1992-09-10	Solvay Enzymes Gmbh & Co Kg	Verfahren zur verbesserung der stabilitaet von hochalkalischen proteasen
US5863783A (en) *	1991-03-27	1999-01-26	Gist-Brocades, N.V.	Cloning and expression of DNA molecules encoding arabinan-degrading enzymes of fungal origin
DK58391D0 (da) *	1991-04-03	1991-04-03	Novo Nordisk As	Hidtil ukendte proteaser
ES2121014T3 (es) *	1991-05-01	1998-11-16	Novo Nordisk As	Enzimas estabilizadas y composiciones detergentes.
US5340735A (en)	1991-05-29	1994-08-23	Cognis, Inc.	Bacillus lentus alkaline protease variants with increased stability
US5510048A (en) *	1991-05-31	1996-04-23	Colgate Palmolive Co.	Nonaqueous liquid, phosphate-free, improved autoamatic dishwashing composition containing enzymes
EP0525610A3 (en) *	1991-07-27	1993-03-24	Solvay Enzymes Gmbh & Co. Kg	Process for increasing the stability of enzymes and stabilized enzymes
AT397390B (de) *	1992-04-06	1994-03-25	Immuno Ag	Verfahren zur spaltung von proteinen
US5792623A (en) *	1992-04-06	1998-08-11	Immuno Aktiengesellschaft	Method for producing activated blood factors with a protease and a detergent
EP0571014B1 (fr) *	1992-05-18	2004-03-31	Genencor International, Inc.	Bactéries produisant des protéases alcalines et production de ces protéases alcalines
KR950702633A (ko) *	1992-07-17	1995-07-29	한스 발터 라벤	고알칼리성 세린 프로테아제(high alkaline serine proteases)
WO1994002597A1 (fr) *	1992-07-23	1994-02-03	Novo Nordisk A/S	Alpha-amylase mutante, detergent, agent de lavage de vaisselle et de liquefaction
US5989887A (en) *	1992-11-25	1999-11-23	Dsm N.V.	Cloning and expression of DNA molecules incoding arabinan-degrading enzymes of fungal origin
DE4304161A1 (de) *	1993-02-12	1994-08-25	Solvay Enzymes Gmbh & Co Kg	Verbesserte hochalkalische Proteasen
US6436690B1 (en)	1993-09-15	2002-08-20	The Procter & Gamble Company	BPN′ variants having decreased adsorption and increased hydrolysis wherein one or more loop regions are substituted
US6440717B1 (en) *	1993-09-15	2002-08-27	The Procter & Gamble Company	BPN′ variants having decreased adsorption and increased hydrolysis
DE69434962T2 (de) *	1993-10-14	2008-01-17	The Procter & Gamble Company, Cincinnati	Proteasehaltige reinigungsmittel
MA23346A1 (fr)	1993-10-14	1995-04-01	Genencor Int	Variantes de la subtilisine
EP0723580B1 (fr) *	1993-10-14	2003-07-16	The Procter & Gamble Company	Compositions contenant un agent de blanchiment et des proteases
US5932532A (en) *	1993-10-14	1999-08-03	Procter & Gamble Company	Bleach compositions comprising protease enzyme
ES2364774T3 (es)	1994-02-24	2011-09-14	HENKEL AG & CO. KGAA	Enzimas mejoradas y detergentes que las contienen.
DE4411223A1 (de) *	1994-03-31	1995-10-05	Solvay Enzymes Gmbh & Co Kg	Verwendung alkalischer Proteasen in gewerblichen Textilwaschverfahren
US6599730B1 (en) *	1994-05-02	2003-07-29	Procter & Gamble Company	Subtilisin 309 variants having decreased adsorption and increased hydrolysis
ES2180645T3 (es) *	1994-06-17	2003-02-16	Genencor Int	Metodo de limpieza basado en composiciones que contienen una enzima capaz de degradar las paredes celulares de las plantas y su uso en metodos de limpieza.
US6066611A (en) *	1994-10-13	2000-05-23	The Procter & Gamble Company	Bleaching compositions comprising protease enzymes
US5714373A (en) *	1995-02-27	1998-02-03	Recombinant Biocatalysis, Inc.	Thermococcus AV4 and enzymes produced by the same
US6455295B1 (en)	1995-03-08	2002-09-24	The Procter & Gamble Company	Subtilisin Carlsberg variants having decreased adsorption and increased hydrolysis
IL117350A0 (en) *	1995-03-09	1996-07-23	Procter & Gamble	Proteinase k variants having decreased adsorption and increased hydrolysis
US6475765B1 (en)	1995-03-09	2002-11-05	Procter & Gamble Company	Subtilisin DY variants having decreased adsorption and increased hydrolysis
US6682924B1 (en) *	1995-05-05	2004-01-27	Novozymes A/S	Protease variants and compositions
DE19530816A1 (de)	1995-08-23	1997-02-27	Cognis Bio Umwelt	Verwendung von mutierter Subtilisin-Protease in kosmetischen Produkten
CN1246146A (zh) *	1996-11-26	2000-03-01	金克克国际有限公司	化学修饰的酶
RU2252254C2 (ru) *	1997-10-23	2005-05-20	Джененкор Интернэшнл, Инк.	Вариант субтилизина bacillus (варианты), кодирующая его днк, экспрессирующий вектор и очищающая композиция
AR015977A1 (es) *	1997-10-23	2001-05-30	Genencor Int	Variantes de proteasa multiplemente substituida con carga neta alterada para su empleo en detergentes
ES2368718T3 (es)	1997-10-23	2011-11-21	Danisco Us Inc.	Variantes de subtilisina con múltiples sustituciones.
US6395532B1 (en)	1998-01-23	2002-05-28	Genencor International, Inc.	Modified enzymes and their use for peptide synthesis
US6642011B2 (en)	1998-04-15	2003-11-04	Genencor International, Inc.	Human protease and use of such protease for pharmaceutical applications and for reducing the allergenicity of non-human proteins
DE69939538D1 (de)	1998-07-02	2008-10-23	Univ Toronto	Mit einer kohlenhydratgruppe chemisch modifizierte proteine
US6831053B1 (en)	1998-10-23	2004-12-14	The Procter & Gamble Company	Bleaching compositions comprising multiply-substituted protease variants
WO2000028007A2 (fr)	1998-11-10	2000-05-18	Genencor International, Inc.	Serines hydrolases mutantes chimiquement modifiees presentant une activite catalytique et une selectivite chirale ameliorees
AU2200100A (en)	1998-12-21	2000-07-12	Genencor International, Inc.	Chemically modified enzymes with multiple charged variants
KR20000065867A (ko) *	1999-04-09	2000-11-15	손경식	세탁세제용 알칼리성 단백질 분해효소 브이에이피케이, 이를 코딩하는 유전자, 재조합 발현벡터 및 형질전환된 균주
EP1185302B1 (fr)	1999-04-28	2013-07-24	Genencor International, Inc.	Antagonistes catalytiques specifiquement cibles et leurs utilisations
US6627744B2 (en)	1999-07-02	2003-09-30	Genencor International, Inc.	Synthesis of glycodendrimer reagents
US6727085B2 (en) *	1999-12-15	2004-04-27	Fanoe Tina Sejersgaard	Subtilase variants having an improved wash performance on egg stains
US6777218B1 (en) *	2000-03-14	2004-08-17	Novozymes A/S	Subtilase enzymes having an improved wash performance on egg stains
US6541234B1 (en) *	2000-09-11	2003-04-01	University Of Maryland Biotechnology Institute	Calcium free subtilisin mutants
US6541235B1 (en) *	2000-09-29	2003-04-01	University Of Maryland Biotechnology Institute	Calcium free subtilisin mutants
DK200101090A (da)	2001-07-12	2001-08-16	Novozymes As	Subtilase variants
DE10153792A1 (de)	2001-10-31	2003-05-22	Henkel Kgaa	Neue Alkalische Protease-Varianten und Wasch- und Reinigungsmittel enthaltend diese neuen Alkalischen Protease-Varianten
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
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
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
JP2005535284A (ja)	2001-12-31	2005-11-24	ジェネンコー・インターナショナル・インク	免疫反応の変化を生じるプロテアーゼ、ならびにその製造および利用方法
EP2287320B1 (fr) *	2002-01-16	2014-10-01	Danisco US Inc.	Variantes multiples de protéase substituée
ES2336092T3 (es) *	2002-01-16	2010-04-08	Genencor International, Inc.	Variantes de proteasas con multiples sustituciones.
DK1495128T3 (da)	2002-03-29	2014-08-11	Genencor Int	Forstærket proteinekspression i Bacillus
US7888093B2 (en) *	2002-11-06	2011-02-15	Novozymes A/S	Subtilase variants
DE10260903A1 (de) *	2002-12-20	2004-07-08	Henkel Kgaa	Neue Perhydrolasen
WO2006033668A2 (fr) *	2004-04-09	2006-03-30	Genencor International, Inc.	Modifications de pcka et expression amelioree de proteine chez un bacille
BRPI0708504A8 (pt) *	2006-03-02	2017-03-01	Danisco Us Inc Genecor Div	alvejante ativo na superfície e ph dinâmico
KR20090031906A (ko) *	2006-07-18	2009-03-30	다니스코 유에스 인크.	광범위한 온도에 걸쳐 활성인 프로테아제 변이형
US20080090745A1 (en) *	2006-10-13	2008-04-17	Fox Bryan P	Expression of Streptomyces subtilism inhibitor (SSI) proteins in Bacillus and Streptomyces sp.
EP2129779B2 (fr) *	2007-03-12	2018-12-26	Danisco US Inc.	Protéases modifiées
DK2152732T3 (da)	2007-05-10	2012-06-04	Danisco Us Inc	Modificeret sekretionssystem til at øge ekspression af polypeptider i bakterier
CA2690055A1 (fr)	2007-06-06	2008-12-18	Danisco Us Inc.	Procedes d'amelioration de la performance des proteines
RU2569106C2 (ru) *	2007-06-06	2015-11-20	ДАНИСКО ЮЭс, ИНК., ДЖЕНЕНКОР ДИВИЖН	Способы улучшения эффективности белков
DE102007044415A1 (de)	2007-09-17	2009-03-19	Henkel Ag & Co. Kgaa	Leistungsverbesserte Proteasen und Wasch- und Reinigungsmittel enthaltend diese Proteasen
US20110147419A1 (en) *	2007-12-14	2011-06-23	Atsushi Tada	Pressure accumulation dispenser
AU2008348270A1 (en)	2007-12-21	2009-07-30	Danisco Us Inc.	Enhanced protein production in bacillus
US20090233830A1 (en) *	2008-03-14	2009-09-17	Penny Sue Dirr	Automatic detergent dishwashing composition
EP2100947A1 (fr) *	2008-03-14	2009-09-16	The Procter and Gamble Company	Composition détergente de lave-vaisselle automatique
NZ587540A (en) *	2008-03-28	2012-06-29	Danisco Us Inc	Method for amplifying locus in bacterial cell
WO2010056671A1 (fr) *	2008-11-11	2010-05-20	Danisco Us Inc.	Compositions et procédés comprenant un variant de subtilisine
MX2011004801A (es)	2008-11-11	2011-06-16	Danisco Inc	Composiciones y metodos que comprenden una variante de subtilisina.
EP2216391A1 (fr) *	2009-02-02	2010-08-11	The Procter & Gamble Company	Composition de détergent liquide pour lavage de la vaisselle à la main
ES2461892T3 (es) *	2009-02-02	2014-05-21	The Procter & Gamble Company	Composición detergente líquida para lavado de vajillas a mano
ES2484002T3 (es) *	2009-02-02	2014-08-08	The Procter & Gamble Company	Composición detergente líquida para lavado de vajillas a mano
EP2213715A1 (fr) *	2009-02-02	2010-08-04	The Procter & Gamble Company	Composition de détergent liquide pour lavage de la vaisselle à la main
EP2216390B1 (fr) *	2009-02-02	2013-11-27	The Procter and Gamble Company	Méthode pour lavage de la vaisselle à la main
EP2216392B1 (fr) *	2009-02-02	2013-11-13	The Procter and Gamble Company	Composition de détergent liquide pour lavage de la vaisselle à la main
EP2216393B1 (fr) *	2009-02-09	2024-04-24	The Procter & Gamble Company	Composition de détergent
AR076941A1 (es)	2009-06-11	2011-07-20	Danisco Us Inc	Cepa de bacillus para una mayor produccion de proteina
GB0915572D0 (en) *	2009-09-07	2009-10-07	Reckitt Benckiser Nv	Detergent composition
CN102648277B (zh) *	2009-09-25	2015-05-20	诺维信公司	蛋白酶变体的用途
JP6448904B2 (ja) *	2010-05-06	2019-01-09	ダニスコ・ユーエス・インク	サブチリシン変異体を含む組成物及び方法
US9434932B2 (en)	2011-06-30	2016-09-06	Novozymes A/S	Alpha-amylase variants
CN102277344B (zh) *	2011-08-03	2012-12-12	天津科技大学	一种低温碱性蛋白酶及其制备方法
DE102013219467A1 (de) *	2013-09-26	2015-03-26	Henkel Ag & Co. Kgaa	Stabilisierte Inhibitor-Proteasevarianten
EP3089991B1 (fr)	2013-12-31	2019-08-28	Danisco US Inc.	Expression améliorée de protéine
DE102014212639A1 (de) *	2014-06-30	2015-12-31	Henkel Ag & Co. Kgaa	Reinigungsmittel enthaltend Proteasen
DK3212780T3 (da) *	2014-10-27	2020-03-23	Danisco Us Inc	Serinprotease
KR102588719B1 (ko)	2014-12-16	2023-10-12	다니스코 유에스 인크.	향상된 단백질 발현
CN107278230B (zh)	2014-12-19	2021-10-29	丹尼斯科美国公司	增强的蛋白质表达
AU2016259703B2 (en)	2015-05-08	2021-12-23	Novozymes A/S	Alpha-amylase variants and polynucleotides encoding same
WO2016180749A1 (fr)	2015-05-08	2016-11-17	Novozymes A/S	Variants d'alpha-amylase et polynucléotides codant pour ces derniers
WO2017089366A1 (fr) *	2015-11-24	2017-06-01	Novozymes A/S	Polypeptides ayant une activité de protéase et polynucléotides codant pour ceux-ci
WO2017210188A1 (fr) *	2016-05-31	2017-12-07	Novozymes A/S	Compositions stabilisées de peroxyde liquide
DE102016210628A1 (de) *	2016-06-15	2017-12-21	Henkel Ag & Co. Kgaa	Bacillus gibsonii Protease und Varianten davon
JP7231228B2 (ja)	2017-02-24	2023-03-01	ダニスコ・ユーエス・インク	バチルス・リケニフォルミスにおける増加したタンパク質産生のための組成物及び方法
WO2019040412A1 (fr)	2017-08-23	2019-02-28	Danisco Us Inc	Procédés et compositions pour modifications génétiques efficaces de souches de bacillus licheniformis
KR20200047668A (ko)	2017-09-13	2020-05-07	다니스코 유에스 인크.	바실러스에서 증가된 단백질 생산을 위한 변형된 5'-비번역 영역(utr) 서열
EP3703661A1 (fr)	2017-11-02	2020-09-09	Danisco US Inc.	Compositions de matrices solides à point de congélation abaissé pour la granulation à l'état fondu d'enzymes
KR102715197B1 (ko)	2018-01-03	2024-10-08	다니스코 유에스 인크.	증가된 단백질 생산을 위한 돌연변이체 및 유전자 변형된 바실러스 세포 및 이의 방법
US20200032178A1 (en) *	2018-07-27	2020-01-30	The Procter & Gamble Company	Water-soluble unit dose articles comprising water-soluble fibrous structures and particles
CN114945665A (zh)	2020-01-15	2022-08-26	丹尼斯科美国公司	用于增强地衣芽孢杆菌中蛋白产生的组合物和方法
WO2022043563A1 (fr) *	2020-08-28	2022-03-03	Novozymes A/S	Variants de protéase dégradant le polyester
WO2023023644A1 (fr)	2021-08-20	2023-02-23	Danisco Us Inc.	Polynucléotides codant pour de nouvelles nucléases, leurs compositions et leurs procédés d'élimination de l'adn lors de la préparations de protéines
EP4525615A2 (fr)	2022-05-14	2025-03-26	Novozymes A/S	Compositions et procédés de prévention, de traitement, de suppression et/ou d'élimination d'infestations et d'infections phytopathogènes
CN121915017A (zh) *	2022-10-27	2026-04-24	青岛蔚蓝生物集团有限公司	一种碱性蛋白酶突变体
CN120712348A (zh) *	2023-03-06	2025-09-26	丹尼斯科美国公司	枯草杆菌蛋白酶变体和使用方法

Citations (12)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB1353317A (en)	1970-03-03	1974-05-15	Koninklijke Gist Spiritus	Enzyme-polymer complexes
US4318818A (en)	1979-11-09	1982-03-09	The Procter & Gamble Company	Stabilized aqueous enzyme composition
US4480037A (en)	1982-02-08	1984-10-30	Showa Denko Kabushiki Kaisha	Alkaline protease and preparation method thereof
EP0126505A1 (fr)	1983-04-26	1984-11-28	Unilever N.V.	Compositions aqueuses stables contenant des enzymes
EP0130756A1 (fr)	1983-06-24	1985-01-09	Genencor International, Inc.	Carbonyl-hydrolases procaryotiques, méthodes, ADN, vecteurs et hôtes transformés pour leur production, et compositions des détergents contenant les dites hydrolases
EP0170360A1 (fr)	1984-05-29	1986-02-05	Novo Nordisk A/S	Granulés contenant des enzymes appropriés pour l'utilisation comme additifs détergents
EP0199405A2 (fr)	1985-04-15	1986-10-29	The Procter & Gamble Company	Détergents liquides contenant un composé tensioactif, une enzyme protéolytique et de l'acide borique
GB2178055A (en)	1985-07-26	1987-02-04	Colgate Palmolive Co	Stabilized built liquid detergent composition containing enzymes
EP0220921A2 (fr)	1985-10-22	1987-05-06	Genex Corporation	Protéases alcalines stables à chaud produites par un bacillus
EP0232269A1 (fr)	1984-10-05	1987-08-19	Zahnradfabrik Friedrichshafen	Servosysteme de direction, surtout pour vehicules motorises.
WO1987005050A1 (fr)	1986-02-12	1987-08-27	Genex Corporation	Procede de mutagenese et de criblage et produit obtenu
EP0238216A1 (fr)	1986-02-20	1987-09-23	Albright & Wilson Limited	Systèmes d'enzymes protégés

Family Cites Families (11)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB1240058A (en) *	1968-04-12	1971-07-21	Procter & Gamble	Enzyme-containing detergent compositions
GB1519148A (en) *	1974-11-19	1978-07-26	Gist Brocades Nv	Compositions of matter
US4760025A (en) *	1984-05-29	1988-07-26	Genencor, Inc.	Modified enzymes and methods for making same
US4511490A (en) *	1983-06-27	1985-04-16	The Clorox Company	Cooperative enzymes comprising alkaline or mixtures of alkaline and neutral proteases without stabilizers
EP0254735B2 (fr) *	1986-01-15	1998-06-17	Amgen Inc.	PROCEDE DE PRODUCTION D'ANALOGUES DE SUBTILISINE THERMIQUEMENT STABLE ET STABLE AU pH
US4990452A (en) *	1986-02-12	1991-02-05	Genex Corporation	Combining mutations for stabilization of subtilisin
IE65767B1 (en) *	1986-04-30	1995-11-15	Genencor Int	Non-human carbonyl hydrolase mutants DNA sequences and vectors encoding same and hosts transformed with said vectors
ES2135386T3 (es) *	1987-02-27	1999-11-01	Genencor Int	Transformacion de cepas de bacillus alcalofilas.
DE3856593D1 (de) *	1987-04-06	2007-10-04	Novozymes As	Regelung von elektrostatischen interaktionen an metallionen-Bindungsstellen zur Stabilisierung von Proteinen
US4914031A (en) *	1987-04-10	1990-04-03	Amgen, Inc.	Subtilisin analogs
DK6488D0 (da) *	1988-01-07	1988-01-07	Novo Industri As	Enzymer

1989
- 1989-02-10 CN CN89101995A patent/CN1056187C/zh not_active Expired - Fee Related
- 1989-02-10 PT PT89702A patent/PT89702B/pt not_active IP Right Cessation
- 1989-02-13 EP EP93201605A patent/EP0571049B2/fr not_active Expired - Lifetime
- 1989-02-13 RU SU894742168A patent/RU2069695C1/ru active
- 1989-02-13 EP EP01120309A patent/EP1160327A3/fr not_active Withdrawn
- 1989-02-13 ES ES89200350T patent/ES2061929T5/es not_active Expired - Lifetime
- 1989-02-13 WO PCT/NL1989/000005 patent/WO1989007642A1/fr not_active Ceased
- 1989-02-13 AU AU30501/89A patent/AU629814B2/en not_active Ceased
- 1989-02-13 US US07/427,103 patent/US5336611A/en not_active Expired - Lifetime
- 1989-02-13 DE DE68912359T patent/DE68912359T3/de not_active Expired - Lifetime
- 1989-02-13 IE IE940164A patent/IE940164L/xx unknown
- 1989-02-13 EP EP89200350A patent/EP0328229B2/fr not_active Expired - Lifetime
- 1989-02-13 CA CA000594259A patent/CA1340366C/fr not_active Expired - Lifetime
- 1989-02-13 IE IE44689A patent/IE63248B1/en not_active IP Right Cessation
- 1989-02-13 DE DE68929484T patent/DE68929484T3/de not_active Expired - Lifetime
- 1989-02-13 BR BR898905580A patent/BR8905580A/pt not_active IP Right Cessation
- 1989-02-13 JP JP1502126A patent/JP2849141B2/ja not_active Expired - Lifetime
- 1989-02-13 KR KR1019890701867A patent/KR970005249B1/ko not_active Expired - Lifetime
- 1989-02-13 AT AT93201605T patent/ATE250669T1/de not_active IP Right Cessation
- 1989-10-09 BG BG89942A patent/BG60566B1/bg unknown
- 1989-10-10 DK DK198905012A patent/DK175813B1/da not_active IP Right Cessation
- 1989-10-10 FI FI894799A patent/FI105481B/fi not_active IP Right Cessation
1993
- 1993-12-21 LT LTIP1650A patent/LT3963B/lt not_active IP Right Cessation
- 1993-12-28 LV LVP-93-1384A patent/LV10652B/en unknown
1996
- 1996-12-06 GR GR960403345T patent/GR3021934T3/el unknown

Patent Citations (12)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB1353317A (en)	1970-03-03	1974-05-15	Koninklijke Gist Spiritus	Enzyme-polymer complexes
US4318818A (en)	1979-11-09	1982-03-09	The Procter & Gamble Company	Stabilized aqueous enzyme composition
US4480037A (en)	1982-02-08	1984-10-30	Showa Denko Kabushiki Kaisha	Alkaline protease and preparation method thereof
EP0126505A1 (fr)	1983-04-26	1984-11-28	Unilever N.V.	Compositions aqueuses stables contenant des enzymes
EP0130756A1 (fr)	1983-06-24	1985-01-09	Genencor International, Inc.	Carbonyl-hydrolases procaryotiques, méthodes, ADN, vecteurs et hôtes transformés pour leur production, et compositions des détergents contenant les dites hydrolases
EP0170360A1 (fr)	1984-05-29	1986-02-05	Novo Nordisk A/S	Granulés contenant des enzymes appropriés pour l'utilisation comme additifs détergents
EP0232269A1 (fr)	1984-10-05	1987-08-19	Zahnradfabrik Friedrichshafen	Servosysteme de direction, surtout pour vehicules motorises.
EP0199405A2 (fr)	1985-04-15	1986-10-29	The Procter & Gamble Company	Détergents liquides contenant un composé tensioactif, une enzyme protéolytique et de l'acide borique
GB2178055A (en)	1985-07-26	1987-02-04	Colgate Palmolive Co	Stabilized built liquid detergent composition containing enzymes
EP0220921A2 (fr)	1985-10-22	1987-05-06	Genex Corporation	Protéases alcalines stables à chaud produites par un bacillus
WO1987005050A1 (fr)	1986-02-12	1987-08-27	Genex Corporation	Procede de mutagenese et de criblage et produit obtenu
EP0238216A1 (fr)	1986-02-20	1987-09-23	Albright & Wilson Limited	Systèmes d'enzymes protégés

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
C. E. STAUFFER AND DON ETSON: "The Effect on Subtilisin Activity of Oxidizing a Methionine Residue", J. BIOL. CHEM., 1969, pages 5333 - 5338
HUI A. ET AL.: "Mutagenesis of the three bases preceding the start codon of the beta-galactosidase mRNA and its effect on translation in Escherichia coli.", EMBO J., 1984
LIN Y, MEANS GE, FEENEY RE: "The action of proteolytic enzymes on N,N-dimethyl proteins. Basis for a microassay for proteolytic enzymes", J. BIOL. CHEM., 1969, pages 789 - 793
ROBERT J. DELANGE AND EMIL L. SMITH: "Subtilisin Carlsberg: II. SEQUENCES OF THE TRYPTIC PEPTIDES", J. BIOL. CHEM., 1968, pages 2143 - 2164

Also Published As

Publication number	Publication date
CN1036602A (zh)	1989-10-25
DE68912359T2 (de)	1994-06-09
IE940164L (en)	1989-08-11
LV10652B (en)	1995-08-20
CN1056187C (zh)	2000-09-06
EP0328229B1 (fr)	1994-01-19
DK501289D0 (da)	1989-10-10
JP2849141B2 (ja)	1999-01-20
ES2061929T3 (es)	1994-12-16
DE68929484T3 (de)	2009-06-25
ES2061929T5 (es)	1997-03-16
BG89942A (bg)	1993-12-24
AU3050189A (en)	1989-09-06
DK501289A (da)	1989-12-07
IE63248B1 (en)	1995-04-05
EP0328229B2 (fr)	1996-10-30
DK175813B1 (da)	2005-03-07
DE68929484D1 (de)	2003-10-30
US5336611A (en)	1994-08-09
AU629814B2 (en)	1992-10-15
EP1160327A3 (fr)	2002-11-06
BG60566B1 (en)	1995-08-28
RU2069695C1 (ru)	1996-11-27
DE68929484T2 (de)	2004-07-22
JPH02503986A (ja)	1990-11-22
EP1160327A2 (fr)	2001-12-05
EP0571049B2 (fr)	2008-09-03
FI894799A0 (fi)	1989-10-10
GR3021934T3 (en)	1997-03-31
DE68912359D1 (de)	1994-03-03
FI105481B (fi)	2000-08-31
PT89702A (pt)	1989-10-04
LV10652A (lv)	1995-04-20
EP0571049A1 (fr)	1993-11-24
KR970005249B1 (ko)	1997-04-14
IE890446L (en)	1989-08-11
EP0328229A1 (fr)	1989-08-16
WO1989007642A1 (fr)	1989-08-24
CA1340366C (fr)	1999-02-02
LTIP1650A (en)	1995-07-25
BR8905580A (pt)	1990-08-14
PT89702B (pt)	1994-04-29
ATE250669T1 (de)	2003-10-15
KR900700597A (ko)	1990-08-16
DE68912359T3 (de)	1998-01-08
EP0571049B1 (fr)	2003-09-24

Legal Events

Date	Code	Title	Description
1996-10-25	PC9A	Transfer of patents	Free format text: GENENCOR INTERNATIONAL INC., 4 CAMDRIDGE PLACE, 1870 SOUTH WINTON ROAD, ROCHESTER NY 14618,US,960826
1998-08-25	MM9A	Lapsed patents	Effective date: 19971221

Publication	Publication Date	Title
LT3963B (en)	1996-05-27	Enzymatic product containing mutant proteolytic enzyme, process for selecting proteolytic enzyme, mutant gene, expression vector, procariotic host-strain, process for preparing mutant proteolytic enzyme, detergent composition
US5324653A (en)	1994-06-28	Recombinant genetic means for the production of serine protease muteins
US6271012B1 (en)	2001-08-07	Protease muteins and their use in detergents
US6808913B2 (en)	2004-10-26	Useful mutations of bacterial alkaline protease
DE69839076T2 (de)	2009-01-22	Proteasevarianten und zusammensetzungen
US5801039A (en)	1998-09-01	Enzymes for detergents
DE69535736T2 (de)	2009-04-30	Verbesserte enzyme und diese enthaltene detergentien
JPH09512433A (ja)	1997-12-16	ズブチリシンｂｐｎ′変異体を含む布帛クリーニング組成物
DK175855B1 (da)	2005-04-04	Mutantprotease og protease til anvendelse i vaskemidler, DNA-sekvens, der koder for en sådan protease, ekspressionsvektor, der omfatter denne DNA-sekvens, prokaryotisk værtsstamme transformeret med en sådan vektor, fremgangsmåde til.....
MXPA99004150A (en)	1999-09-01	Subtilase variants and compositions