BG61081B1 - МУТАНТНИ МИКРОБИАЛНИ α-АМИЛАЗИ С ПОВИШЕНА ТЕРМИЧНА, КИСЕЛИННА И/ИЛИ АЛКАЛНА УСТОЙЧИВОСТ - Google Patents
МУТАНТНИ МИКРОБИАЛНИ α-АМИЛАЗИ С ПОВИШЕНА ТЕРМИЧНА, КИСЕЛИННА И/ИЛИ АЛКАЛНА УСТОЙЧИВОСТ Download PDFInfo
- Publication number
- BG61081B1 BG61081B1 BG93814A BG9381491A BG61081B1 BG 61081 B1 BG61081 B1 BG 61081B1 BG 93814 A BG93814 A BG 93814A BG 9381491 A BG9381491 A BG 9381491A BG 61081 B1 BG61081 B1 BG 61081B1
- Authority
- BG
- Bulgaria
- Prior art keywords
- amylase
- mutant
- dna sequence
- starch
- amylases
- Prior art date
Links
- 230000001965 increasing effect Effects 0.000 title claims description 15
- 229940025131 amylases Drugs 0.000 title description 5
- 230000002378 acidificating effect Effects 0.000 title description 2
- 230000000813 microbial effect Effects 0.000 title 1
- 108090000637 alpha-Amylases Proteins 0.000 claims abstract description 140
- 102000004139 alpha-Amylases Human genes 0.000 claims abstract description 126
- 238000000034 method Methods 0.000 claims abstract description 50
- 229920002472 Starch Polymers 0.000 claims abstract description 40
- 239000008107 starch Substances 0.000 claims abstract description 39
- 235000019698 starch Nutrition 0.000 claims abstract description 39
- 241000193830 Bacillus <bacterium> Species 0.000 claims abstract description 21
- 238000004519 manufacturing process Methods 0.000 claims abstract description 14
- 239000004753 textile Substances 0.000 claims abstract description 12
- 238000006731 degradation reaction Methods 0.000 claims abstract description 8
- 230000015556 catabolic process Effects 0.000 claims abstract description 6
- 244000005700 microbiome Species 0.000 claims abstract description 6
- 229940024171 alpha-amylase Drugs 0.000 claims description 102
- 102000004190 Enzymes Human genes 0.000 claims description 43
- 108090000790 Enzymes Proteins 0.000 claims description 43
- 229940088598 enzyme Drugs 0.000 claims description 43
- 231100000350 mutagenesis Toxicity 0.000 claims description 30
- 238000002703 mutagenesis Methods 0.000 claims description 29
- 239000004382 Amylase Substances 0.000 claims description 26
- 108010065511 Amylases Proteins 0.000 claims description 20
- 150000001413 amino acids Chemical class 0.000 claims description 18
- 102000013142 Amylases Human genes 0.000 claims description 17
- 235000019418 amylase Nutrition 0.000 claims description 17
- 239000013604 expression vector Substances 0.000 claims description 12
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 10
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 10
- 241000194108 Bacillus licheniformis Species 0.000 claims description 9
- 238000006467 substitution reaction Methods 0.000 claims description 9
- 230000009466 transformation Effects 0.000 claims description 6
- 241000193385 Geobacillus stearothermophilus Species 0.000 claims description 5
- 238000005034 decoration Methods 0.000 claims description 3
- 239000001963 growth medium Substances 0.000 claims description 3
- 239000000463 material Substances 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims description 2
- 238000006911 enzymatic reaction Methods 0.000 claims 2
- 241000831652 Salinivibrio sharmensis Species 0.000 claims 1
- 230000003625 amylolytic effect Effects 0.000 claims 1
- 230000004071 biological effect Effects 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 31
- 239000002253 acid Substances 0.000 abstract description 16
- 239000000126 substance Substances 0.000 abstract description 11
- 108091027305 Heteroduplex Proteins 0.000 abstract description 5
- 238000013461 design Methods 0.000 abstract description 5
- 238000012216 screening Methods 0.000 description 33
- 108020004414 DNA Proteins 0.000 description 32
- 241000588724 Escherichia coli Species 0.000 description 30
- 239000013598 vector Substances 0.000 description 27
- 230000000694 effects Effects 0.000 description 26
- 230000035772 mutation Effects 0.000 description 25
- 239000013612 plasmid Substances 0.000 description 25
- 235000001014 amino acid Nutrition 0.000 description 21
- 239000012634 fragment Substances 0.000 description 17
- 229940024606 amino acid Drugs 0.000 description 16
- 239000002773 nucleotide Substances 0.000 description 15
- 229920001817 Agar Polymers 0.000 description 14
- 239000008272 agar Substances 0.000 description 14
- 125000003729 nucleotide group Chemical group 0.000 description 14
- 238000006243 chemical reaction Methods 0.000 description 12
- 239000000243 solution Substances 0.000 description 12
- 238000012360 testing method Methods 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 10
- 239000011575 calcium Substances 0.000 description 9
- 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 9
- 231100000219 mutagenic Toxicity 0.000 description 9
- 230000003505 mutagenic effect Effects 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 8
- 229960005091 chloramphenicol Drugs 0.000 description 8
- 238000011534 incubation Methods 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 102000004169 proteins and genes Human genes 0.000 description 8
- 239000000872 buffer Substances 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 230000010076 replication Effects 0.000 description 7
- 102000053602 DNA Human genes 0.000 description 6
- 108010076504 Protein Sorting Signals Proteins 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 239000002585 base Substances 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 230000002255 enzymatic effect Effects 0.000 description 6
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 108020004682 Single-Stranded DNA Proteins 0.000 description 5
- 230000003115 biocidal effect Effects 0.000 description 5
- 238000010276 construction Methods 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 125000001475 halogen functional group Chemical group 0.000 description 5
- 230000002779 inactivation Effects 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 4
- 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 4
- 239000007993 MOPS buffer Substances 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 229910052740 iodine Inorganic materials 0.000 description 4
- 239000011630 iodine Substances 0.000 description 4
- 238000002708 random mutagenesis Methods 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 238000002741 site-directed mutagenesis Methods 0.000 description 4
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 3
- 235000014469 Bacillus subtilis Nutrition 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 102100034343 Integrase Human genes 0.000 description 3
- 102000008300 Mutant Proteins Human genes 0.000 description 3
- 108010021466 Mutant Proteins Proteins 0.000 description 3
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 3
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 3
- 108020005038 Terminator Codon Proteins 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 239000013611 chromosomal DNA Substances 0.000 description 3
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 3
- NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 230000035784 germination Effects 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 101150009573 phoA gene Proteins 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 239000013605 shuttle vector Substances 0.000 description 3
- 230000008961 swelling Effects 0.000 description 3
- 239000006188 syrup Substances 0.000 description 3
- 235000020357 syrup Nutrition 0.000 description 3
- 241001515965 unidentified phage Species 0.000 description 3
- 229920000945 Amylopectin Polymers 0.000 description 2
- 229920000856 Amylose Polymers 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- -1 DGTP Chemical compound 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108090000204 Dipeptidase 1 Proteins 0.000 description 2
- 241000702374 Enterobacteria phage fd Species 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 238000012411 cloning technique Methods 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 239000008121 dextrose Substances 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000001704 evaporation Methods 0.000 description 2
- 230000008020 evaporation Effects 0.000 description 2
- 239000004744 fabric Substances 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- 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 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 235000011121 sodium hydroxide Nutrition 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000008399 tap water Substances 0.000 description 2
- 235000020679 tap water Nutrition 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- KRQUFUKTQHISJB-YYADALCUSA-N 2-[(E)-N-[2-(4-chlorophenoxy)propoxy]-C-propylcarbonimidoyl]-3-hydroxy-5-(thian-3-yl)cyclohex-2-en-1-one Chemical compound CCC\C(=N/OCC(C)OC1=CC=C(Cl)C=C1)C1=C(O)CC(CC1=O)C1CCCSC1 KRQUFUKTQHISJB-YYADALCUSA-N 0.000 description 1
- IQUPABOKLQSFBK-UHFFFAOYSA-N 2-nitrophenol Chemical compound OC1=CC=CC=C1[N+]([O-])=O IQUPABOKLQSFBK-UHFFFAOYSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000304886 Bacilli Species 0.000 description 1
- 241000193749 Bacillus coagulans Species 0.000 description 1
- 238000009631 Broth culture Methods 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 208000016057 CHAND syndrome Diseases 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 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 1
- 241000196324 Embryophyta Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- OWXMKDGYPWMGEB-UHFFFAOYSA-N HEPPS Chemical compound OCCN1CCN(CCCS(O)(=O)=O)CC1 OWXMKDGYPWMGEB-UHFFFAOYSA-N 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
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 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
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- NBGXQZRRLOGAJF-UHFFFAOYSA-N Maltulose Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)(CO)OCC1O NBGXQZRRLOGAJF-UHFFFAOYSA-N 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 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
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-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
- 239000004809 Teflon Substances 0.000 description 1
- 229920006362 Teflon® Polymers 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
- FTNIPWXXIGNQQF-UHFFFAOYSA-N UNPD130147 Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(OC4C(OC(O)C(O)C4O)CO)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O FTNIPWXXIGNQQF-UHFFFAOYSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 108020002494 acetyltransferase Proteins 0.000 description 1
- 102000005421 acetyltransferase Human genes 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 239000007621 bhi medium Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000011545 carbonate/bicarbonate buffer Substances 0.000 description 1
- 230000000747 cardiac effect Effects 0.000 description 1
- 230000002490 cerebral effect Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
- HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 230000009088 enzymatic function Effects 0.000 description 1
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- BCQZXOMGPXTTIC-UHFFFAOYSA-N halothane Chemical compound FC(F)(F)C(Cl)Br BCQZXOMGPXTTIC-UHFFFAOYSA-N 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- FJCUPROCOFFUSR-UHFFFAOYSA-N malto-pentaose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(OC2C(C(O)C(OC3C(C(O)C(O)C(CO)O3)O)C(CO)O2)O)C(CO)O1 FJCUPROCOFFUSR-UHFFFAOYSA-N 0.000 description 1
- FJCUPROCOFFUSR-GMMZZHHDSA-N maltopentaose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O[C@H]([C@H](O)CO)[C@H](O)[C@@H](O)C=O)O[C@H](CO)[C@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O[C@@H]3[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)[C@@H](CO)O2)O)[C@@H](CO)O1 FJCUPROCOFFUSR-GMMZZHHDSA-N 0.000 description 1
- JCQLYHFGKNRPGE-HFZVAGMNSA-N maltulose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 JCQLYHFGKNRPGE-HFZVAGMNSA-N 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 125000000896 monocarboxylic acid group Chemical group 0.000 description 1
- 230000036438 mutation frequency Effects 0.000 description 1
- GHLZUHZBBNDWHW-UHFFFAOYSA-N nonanamide Chemical group CCCCCCCCC(N)=O GHLZUHZBBNDWHW-UHFFFAOYSA-N 0.000 description 1
- 238000010606 normalization Methods 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000013021 overheating Methods 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 235000011056 potassium acetate Nutrition 0.000 description 1
- 229920001592 potato starch Polymers 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000004153 renaturation Methods 0.000 description 1
- 101150066583 rep gene Proteins 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000002804 saturated mutagenesis Methods 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000037432 silent mutation Effects 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 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
- 241000894007 species Species 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 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
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 229940035893 uracil Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000011800 void material Substances 0.000 description 1
- 229940100445 wheat starch Drugs 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
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/74—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
- C12N15/75—Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Bacillus
-
- 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
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
-
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
-
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Plant Pathology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Medicinal Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Cigarettes, Filters, And Manufacturing Of Filters (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Tires In General (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP89201735 | 1989-06-29 | ||
| PCT/EP1990/001042 WO1991000353A2 (fr) | 1989-06-29 | 1990-06-27 | α-AMYLASES MICROBIENNES MUTANTES PRESENTANT UNE MEILLEURE STABILITE THERMIQUE, AUX ACIDES ET/OU AUX ALCALINS |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| BG93814A BG93814A (bg) | 1993-12-24 |
| BG61081B1 true BG61081B1 (bg) | 1996-10-31 |
Family
ID=8202426
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| BG93814A BG61081B1 (bg) | 1989-06-29 | 1991-02-11 | МУТАНТНИ МИКРОБИАЛНИ α-АМИЛАЗИ С ПОВИШЕНА ТЕРМИЧНА, КИСЕЛИННА И/ИЛИ АЛКАЛНА УСТОЙЧИВОСТ |
Country Status (17)
| Country | Link |
|---|---|
| US (1) | US5364782A (fr) |
| EP (1) | EP0410498B1 (fr) |
| JP (2) | JP3086249B2 (fr) |
| KR (1) | KR0165550B1 (fr) |
| CN (1) | CN1050220A (fr) |
| AT (1) | ATE166922T1 (fr) |
| BG (1) | BG61081B1 (fr) |
| BR (1) | BR9006818A (fr) |
| CA (1) | CA2030554C (fr) |
| DD (1) | DD301620A9 (fr) |
| DE (1) | DE69032360T2 (fr) |
| DK (1) | DK0410498T3 (fr) |
| ES (1) | ES2117625T3 (fr) |
| FI (1) | FI103285B1 (fr) |
| IE (1) | IE902369A1 (fr) |
| PT (1) | PT94560B (fr) |
| WO (1) | WO1991000353A2 (fr) |
Families Citing this family (132)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU1654692A (en) * | 1991-05-06 | 1992-12-21 | Valio Finnish Co-Operative Dairies Association | Acid alpha-amylase |
| WO1993010248A1 (fr) * | 1991-11-14 | 1993-05-27 | Novo Nordisk A/S | PROCEDE D'EXPRESSION DES GENES DANS $i(BACILLUS LICHENIFORMIS) |
| WO1994013792A1 (fr) * | 1992-12-09 | 1994-06-23 | Yoshiyuki Takasaki | NOUVELLE α-AMYLASE RESISTANT AUX ACIDES ET A LA CHALEUR, SON PROCEDE DE PRODUCTION, ET PROCEDE DE LIQUEFACTION DE L'AMIDON AU MOYEN DE CETTE α-AMYLASE |
| DK154292D0 (da) * | 1992-12-23 | 1992-12-23 | Novo Nordisk As | Nyt enzym |
| JPH08506491A (ja) * | 1993-02-11 | 1996-07-16 | ジェネンカー インターナショナル，インコーポレイティド | 酸化安定性アルファ−アミラーゼ |
| WO1994026881A1 (fr) * | 1993-05-19 | 1994-11-24 | Kao Corporation | α-AMYLASE ALCALINE LIQUEFIANTE, PROCEDE ET PRODUCTION ET COMPOSITION DETERGENTE LA CONTENANT |
| EP2199386A1 (fr) | 1993-10-08 | 2010-06-23 | Novozymes A/S | Variants d'amylase |
| US5830837A (en) * | 1994-11-22 | 1998-11-03 | Novo Nordisk A/S | Amylase variants |
| WO1995010603A1 (fr) * | 1993-10-08 | 1995-04-20 | Novo Nordisk A/S | Variants d'amylase |
| MY111537A (en) * | 1994-02-02 | 2000-07-31 | Novo Nordisk As | A combined desizing and bleaching process. |
| BR9507229A (pt) * | 1994-03-29 | 1997-09-16 | Novo Nordisk As | Amilase composição detergente aditivo detergente uso de um detergente e de uma amilase construç~o de dna vetor de expressão recombinante célula e processo para produzir amilase |
| TW255887B (en) * | 1994-05-25 | 1995-09-01 | Lilly Co Eli | Synthesis of benzoquinolinones |
| CA2194571C (fr) * | 1994-06-17 | 2009-02-24 | Jan Metske Van Der Laan | Nouvelles enzymes amylolytiques derivees de b. licheniformis .alpha.-amylase, possedant des caracteristiques ameliorees |
| WO1996017056A1 (fr) * | 1994-12-02 | 1996-06-06 | Institut Pasteur | Hypermutagenese |
| ES2329528T3 (es) * | 1995-02-03 | 2009-11-26 | Novozymes A/S | Metodo para diseñar mutantes alfa-amilasa con propiedades determinadas. |
| US6093562A (en) * | 1996-02-05 | 2000-07-25 | Novo Nordisk A/S | Amylase variants |
| US6440716B1 (en) | 1995-02-03 | 2002-08-27 | Novozymes A/S | α-amylase mutants |
| US7115409B1 (en) | 1995-02-03 | 2006-10-03 | Novozymes A/S | α-amylase mutants |
| CN101117629B (zh) * | 1995-02-03 | 2014-06-11 | 诺维信公司 | 淀粉酶变体 |
| AR000862A1 (es) | 1995-02-03 | 1997-08-06 | Novozymes As | Variantes de una ó-amilasa madre, un metodo para producir la misma, una estructura de adn y un vector de expresion, una celula transformada por dichaestructura de adn y vector, un aditivo para detergente, composicion detergente, una composicion para lavado de ropa y una composicion para la eliminacion del |
| KR19980702782A (ko) * | 1995-03-09 | 1998-08-05 | 혼 마가렛 에이. | 녹말 액화 방법 |
| US5736499A (en) * | 1995-06-06 | 1998-04-07 | Genencor International, Inc. | Mutant A-amylase |
| JP3025627B2 (ja) | 1995-06-14 | 2000-03-27 | 花王株式会社 | 液化型アルカリα−アミラーゼ遺伝子 |
| AR003020A1 (es) * | 1995-07-24 | 1998-05-27 | Procter & Gamble | Composicion detergente que comprende una amilasa de estabilidad oxidativa aumentada y un sistema surfactante especifico. |
| WO1997010342A1 (fr) * | 1995-09-13 | 1997-03-20 | Genencor International, Inc. | Micro-organismes alcaliphiles et thermophiles et enzymes obtenues a partir de ceux-ci |
| ES2432519T3 (es) | 1996-04-30 | 2013-12-04 | Novozymes A/S | Mutantes de alfa-amilasa |
| US6197070B1 (en) | 1996-05-15 | 2001-03-06 | The Procter & Gamble Company | Detergent compositions comprising alpha combination of α-amylases for malodor stripping |
| US5958739A (en) * | 1996-06-06 | 1999-09-28 | Genencor International Inc. | Mutant α-amylase |
| EP0982981A4 (fr) * | 1997-04-28 | 2004-03-24 | Wengui Yan | Heterosis des plantes cultivees et herbicide |
| US6080568A (en) * | 1997-08-19 | 2000-06-27 | Genencor International, Inc. | Mutant α-amylase comprising modification at residues corresponding to A210, H405 and/or T412 in Bacillus licheniformis |
| US6361989B1 (en) | 1997-10-13 | 2002-03-26 | Novozymes A/S | α-amylase and α-amylase variants |
| ATE423192T1 (de) * | 1997-10-13 | 2009-03-15 | Novozymes As | Mutanten der alpha-amylase |
| CA2308119C (fr) | 1997-10-30 | 2014-06-03 | Novo Nordisk A/S | Mutants d'alpha-amylase |
| CA2331199C (fr) | 1998-06-10 | 2012-10-23 | Markus Sakari Kauppinen | Mannanases isolees pour le traitement de fibres cellulosiques ou synthetiques |
| US6410295B1 (en) | 1999-03-30 | 2002-06-25 | Novozymes A/S | Alpha-amylase variants |
| CN1252256C (zh) * | 1999-03-30 | 2006-04-19 | 诺维信公司 | α－淀粉酶变体 |
| WO2001016348A1 (fr) * | 1999-09-01 | 2001-03-08 | Novozymes A/S | Derives d'amidon modifies par amylase maltogenique |
| CN101532000A (zh) | 2000-03-08 | 2009-09-16 | 诺维信公司 | 具有改变的特性的变体 |
| MXPA03000793A (es) | 2000-07-28 | 2003-06-04 | Henkel Kgaa | Enzima amilolitica novedosa, extraida de bacilo sp a 7-7 (dsm 12368) y agentes de lavado y limpiadores que contienen esta enzima amilolitica novedosa. |
| CN101857858A (zh) | 2000-08-01 | 2010-10-13 | 诺维信公司 | 具有改变特性的α-淀粉酶突变体 |
| US20020155574A1 (en) * | 2000-08-01 | 2002-10-24 | Novozymes A/S | Alpha-amylase mutants with altered properties |
| WO2002044350A2 (fr) | 2000-11-28 | 2002-06-06 | Henkel Kommanditgesellschaft Auf Aktien | Nouvelle cyclodextrine-glucanotransferase (cgtase) issue de bacillus agaradherens (dsm 9948) et produits detergents et de nettoyage comprenant cette nouvelle cyclodextrine-glucanotransferase |
| JP3753945B2 (ja) | 2001-02-14 | 2006-03-08 | ヒゲタ醤油株式会社 | 大腸菌とブレビバチルス属細菌間のプラスミドシャトルベクター |
| US7498158B2 (en) | 2001-05-15 | 2009-03-03 | Novozymes A/S | Alpha-amylase variant with altered properties |
| DE10138753B4 (de) * | 2001-08-07 | 2017-07-20 | Henkel Ag & Co. Kgaa | Wasch- und Reinigungsmittel mit Hybrid-Alpha-Amylasen |
| DE10163748A1 (de) | 2001-12-21 | 2003-07-17 | Henkel Kgaa | Neue Glykosylhydrolasen |
| US20060042020A1 (en) * | 2002-12-20 | 2006-03-02 | Novozymes North America, Inc. | Treatment of fabrics, fibers, or yarns |
| US7459299B2 (en) | 2003-04-01 | 2008-12-02 | Danisco A/S, Genencor Division | Variant Humicola grisea CBH1.1 |
| WO2006002643A2 (fr) | 2004-07-05 | 2006-01-12 | Novozymes A/S | Variants d'alpha-amylases presentant des proprietes modifiees |
| DE102004047777B4 (de) | 2004-10-01 | 2018-05-09 | Basf Se | Alpha-Amylase-Varianten mit erhöhter Lösungsmittelstabilität, Verfahren zu deren Herstellung sowie deren Verwendung |
| CN100396777C (zh) * | 2005-10-28 | 2008-06-25 | 南开大学 | 一种嗜热碱性α-淀粉酶及其编码基因 |
| EP1876285A1 (fr) * | 2006-07-05 | 2008-01-09 | DyStar Textilfarben GmbH & Co. Deutschland KG | Déminéralisation et désencollage de matériaux textiles en une seule operation |
| CA2704745C (fr) | 2007-11-05 | 2019-01-15 | Danisco Us Inc. | Variants d'alpha-amylase a proprietes modifiees |
| NZ584434A (en) | 2007-11-05 | 2011-12-22 | Danisco Us Inc | VARIANTS OF BACILLUS sp. TS-23 ALPHA-AMYLASE WITH ALTERED PROPERTIES |
| US8236545B2 (en) | 2008-02-04 | 2012-08-07 | Danisco Us Inc., Genencor Division | TS23 alpha-amylase variants with altered properties |
| US8084240B2 (en) | 2008-06-06 | 2011-12-27 | Danisco Us Inc. | Geobacillus stearothermophilus α-amylase (AmyS) variants with improved properties |
| CN102112605B (zh) * | 2008-06-06 | 2014-02-26 | 丹尼斯科美国公司 | 来自枯草芽孢杆菌的变体α-淀粉酶及其使用方法 |
| BRPI0920891B1 (pt) | 2008-09-25 | 2023-01-10 | Danisco Us Inc | Mistura de alfa-amilase e método para produção de um açúcar fermentável |
| WO2011076897A1 (fr) | 2009-12-22 | 2011-06-30 | Novozymes A/S | Utilisation de variants d'amylase à basse température |
| US8435577B2 (en) | 2010-01-04 | 2013-05-07 | Novozymes A/S | Alpha-amylases |
| EP2357220A1 (fr) | 2010-02-10 | 2011-08-17 | The Procter & Gamble Company | Compositions de nettoyage comprenant des variantes de l'amylase de grande stabilité en présence d'un agent chélateur |
| CN113186178A (zh) | 2010-02-10 | 2021-07-30 | 诺维信公司 | 在螯合剂存在下具有高稳定性的变体和包含变体的组合物 |
| EP2726607B1 (fr) | 2011-06-30 | 2018-08-08 | Novozymes A/S | Variants d'alpha-amylase |
| US20160160202A1 (en) | 2013-05-29 | 2016-06-09 | Danisco Us Inc. | Novel metalloproteases |
| EP3636662B1 (fr) | 2013-05-29 | 2022-07-13 | Danisco US Inc. | Nouvelles métalloprotéases |
| EP3260538B1 (fr) | 2013-05-29 | 2021-04-14 | Danisco US Inc. | Nouvelles métalloprotéases |
| JP6367930B2 (ja) | 2013-05-29 | 2018-08-01 | ダニスコ・ユーエス・インク | 新規メタロプロテアーゼ |
| WO2015089447A1 (fr) | 2013-12-13 | 2015-06-18 | Danisco Us Inc. | Sérines protéases du clade du bacillus gibsonii |
| TR201906371T4 (tr) | 2013-12-13 | 2019-05-21 | Danisco Inc | Bacillus türlerinin serin proteazları. |
| EP3083705B1 (fr) | 2013-12-18 | 2020-09-30 | DuPont Industrial Biosciences USA, LLC | Éthers de poly(alpha-1,3-glucane) cationiques |
| EP3105256A1 (fr) | 2014-02-14 | 2016-12-21 | E. I. du Pont de Nemours and Company | Poly-alpha-1,3-1,6-glucanes utilisables en vue de la modification de la viscosité |
| WO2015138283A1 (fr) | 2014-03-11 | 2015-09-17 | E. I. Du Pont De Nemours And Company | Poly(alpha-1,3-glucane) oxydé en tant qu'adjuvant pour détergent |
| WO2015143360A2 (fr) | 2014-03-21 | 2015-09-24 | Danisco Us Inc. | Sérine-protéases de l'espèce bacillus |
| WO2015195777A1 (fr) | 2014-06-19 | 2015-12-23 | E. I. Du Pont De Nemours And Company | Compositions contenant un ou plusieurs composés d'éther de poly alpha-1,3-glucane |
| US9714403B2 (en) | 2014-06-19 | 2017-07-25 | E I Du Pont De Nemours And Company | Compositions containing one or more poly alpha-1,3-glucan ether compounds |
| WO2016061438A1 (fr) | 2014-10-17 | 2016-04-21 | Danisco Us Inc. | Sérines protéases de l'espèce bacillus |
| WO2016069544A1 (fr) | 2014-10-27 | 2016-05-06 | Danisco Us Inc. | Sérines protéases |
| WO2016069557A1 (fr) | 2014-10-27 | 2016-05-06 | Danisco Us Inc. | Sérine-protéases de l'espèce bacillus |
| EP3212662B1 (fr) | 2014-10-27 | 2020-04-08 | Danisco US Inc. | Sérines protéases |
| WO2016069569A2 (fr) | 2014-10-27 | 2016-05-06 | Danisco Us Inc. | Sérine protéases |
| WO2016069548A2 (fr) | 2014-10-27 | 2016-05-06 | Danisco Us Inc. | Sérine-protéases |
| JP6770519B2 (ja) | 2014-12-23 | 2020-10-14 | イー・アイ・デュポン・ドウ・ヌムール・アンド・カンパニーＥ．Ｉ．Ｄｕ Ｐｏｎｔ Ｄｅ Ｎｅｍｏｕｒｓ Ａｎｄ Ｃｏｍｐａｎｙ | 酵素により製造されるセルロース |
| EP4219704A3 (fr) | 2015-05-13 | 2023-08-23 | Danisco US Inc | Variants de protéase aprl-clade et leurs utilisations |
| WO2016201044A1 (fr) | 2015-06-09 | 2016-12-15 | Danisco Us Inc | Produits encapsulés osmotiques à éclatement |
| WO2016201040A1 (fr) | 2015-06-09 | 2016-12-15 | Danisco Us Inc. | Suspension d'enzyme activée par l'eau |
| WO2016201069A1 (fr) | 2015-06-09 | 2016-12-15 | Danisco Us Inc | Particules contenant une enzyme basse densité |
| CN107849549B (zh) | 2015-06-17 | 2024-04-05 | 丹尼斯科美国公司 | 吉氏芽孢杆菌进化枝丝氨酸蛋白酶 |
| US20180320158A1 (en) | 2015-11-05 | 2018-11-08 | Danisco Us Inc. | Paenibacillus and bacillus spp. mannanases |
| JP7364331B2 (ja) | 2015-11-05 | 2023-10-18 | ダニスコ・ユーエス・インク | パエニバチルス（Ｐａｅｎｉｂａｃｉｌｌｕｓ）属種マンナナーゼ |
| EP3374488B1 (fr) | 2015-11-13 | 2020-10-14 | DuPont Industrial Biosciences USA, LLC | Compositions de fibre de glucane à utiliser dans l'entretien du linge et l'entretien de tissu |
| WO2017083229A1 (fr) | 2015-11-13 | 2017-05-18 | E. I. Du Pont De Nemours And Company | Compositions de fibres de glucane utiles pour la lessive et l'entretien des tissus |
| US10844324B2 (en) | 2015-11-13 | 2020-11-24 | Dupont Industrial Biosciences Usa, Llc | Glucan fiber compositions for use in laundry care and fabric care |
| US11920170B2 (en) | 2015-12-09 | 2024-03-05 | Danisco Us Inc. | Alpha-amylase combinatorial variants |
| EP3390625B1 (fr) | 2015-12-18 | 2023-09-06 | Danisco US Inc. | Polypeptides ayant une activité endoglucanase et leurs utilisations |
| CN105802940B (zh) * | 2016-04-18 | 2019-04-16 | 广西大学 | 一种地衣芽胞杆菌高温α-淀粉酶突变体及其应用 |
| US20190194636A1 (en) | 2016-05-03 | 2019-06-27 | Danisco Us Inc | Protease variants and uses thereof |
| EP3845642B1 (fr) | 2016-05-05 | 2023-08-09 | Danisco US Inc. | Variantes de protéase et leurs utilisations |
| CA3026064A1 (fr) | 2016-05-31 | 2017-12-07 | Danisco Us Inc. | Variants de protease et leurs utilisations |
| US11946080B2 (en) | 2016-06-17 | 2024-04-02 | Danisco Us Inc. | Protease variants and uses thereof |
| US20190264138A1 (en) | 2016-11-07 | 2019-08-29 | Danisco Us Inc. | Laundry detergent composition |
| US20200392477A1 (en) | 2016-12-21 | 2020-12-17 | Danisco Us Inc. | Protease variants and uses thereof |
| CN110312794B (zh) | 2016-12-21 | 2024-04-12 | 丹尼斯科美国公司 | 吉氏芽孢杆菌进化枝丝氨酸蛋白酶 |
| WO2018169750A1 (fr) | 2017-03-15 | 2018-09-20 | Danisco Us Inc | Sérine protéases de type trypsine et leurs utilisations |
| WO2018183662A1 (fr) | 2017-03-31 | 2018-10-04 | Danisco Us Inc | Formulations d'enzyme à libération retardée pour détergents contenant un agent de blanchiment |
| MX2019014556A (es) | 2017-06-30 | 2020-02-07 | Danisco Us Inc | Particulas que contienen enzimas de baja aglomeracion. |
| WO2019108599A1 (fr) | 2017-11-29 | 2019-06-06 | Danisco Us Inc | Variants de subtilisine à stabilité améliorée |
| US20210222148A1 (en) | 2017-12-21 | 2021-07-22 | Danisco Us Inc. | Enzyme-containing, hot-melt granules comprising a thermotolerant desiccant |
| WO2019156670A1 (fr) | 2018-02-08 | 2019-08-15 | Danisco Us Inc. | Particules de matrice de cire résistant à la chaleur pour encapsulation d'enzymes |
| WO2019245704A1 (fr) | 2018-06-19 | 2019-12-26 | Danisco Us Inc | Variantes de subtilisine |
| US20210363470A1 (en) | 2018-06-19 | 2021-11-25 | Danisco Us Inc | Subtilisin variants |
| WO2020047215A1 (fr) | 2018-08-30 | 2020-03-05 | Danisco Us Inc | Granulés contenant des enzymes |
| CN113166682A (zh) | 2018-09-27 | 2021-07-23 | 丹尼斯科美国公司 | 用于医疗器械清洁的组合物 |
| WO2020112599A1 (fr) | 2018-11-28 | 2020-06-04 | Danisco Us Inc | Variants de subtilisine à stabilité améliorée |
| CN114174504A (zh) | 2019-05-24 | 2022-03-11 | 丹尼斯科美国公司 | 枯草杆菌蛋白酶变体和使用方法 |
| EP3980517A1 (fr) | 2019-06-06 | 2022-04-13 | Danisco US Inc. | Procédés et compositions de nettoyage |
| EP4204553A1 (fr) | 2020-08-27 | 2023-07-05 | Danisco US Inc. | Enzymes et compositions d'enzymes pour le nettoyage |
| EP4284906A1 (fr) | 2021-01-29 | 2023-12-06 | Danisco US Inc. | Compositions pour le nettoyage et procédés associés |
| WO2023278297A1 (fr) | 2021-06-30 | 2023-01-05 | Danisco Us Inc | Variants de lipases et leurs utilisations |
| CN117916354A (zh) | 2021-09-03 | 2024-04-19 | 丹尼斯科美国公司 | 用于清洁的衣物洗涤组合物 |
| CN117957318A (zh) | 2021-09-13 | 2024-04-30 | 丹尼斯科美国公司 | 含有生物活性物质的颗粒 |
| WO2023114939A2 (fr) | 2021-12-16 | 2023-06-22 | Danisco Us Inc. | Variants de subtilisine et procédés d'utilisation |
| WO2023114936A2 (fr) | 2021-12-16 | 2023-06-22 | Danisco Us Inc. | Variants de subtilisine et procédés d'utilisation |
| WO2023114932A2 (fr) | 2021-12-16 | 2023-06-22 | Danisco Us Inc. | Variants de subtilisine et procédés d'utilisation |
| WO2023168234A1 (fr) | 2022-03-01 | 2023-09-07 | Danisco Us Inc. | Enzymes et compositions enzymatiques pour le nettoyage |
| WO2023225459A2 (fr) | 2022-05-14 | 2023-11-23 | Novozymes A/S | Compositions et procédés de prévention, de traitement, de suppression et/ou d'élimination d'infestations et d'infections phytopathogènes |
| CN114875057A (zh) * | 2022-06-14 | 2022-08-09 | 中农华威生物制药(湖北)有限公司 | 一种可高效表达饲用低温酸性α-淀粉酶的枯草芽孢杆菌的构建方法 |
| WO2023250301A1 (fr) | 2022-06-21 | 2023-12-28 | Danisco Us Inc. | Procédés et compositions de nettoyage comprenant un polypeptide ayant une activité de thermolysine |
| WO2024050343A1 (fr) | 2022-09-02 | 2024-03-07 | Danisco Us Inc. | Variants de subtilisine et procédés associés |
| WO2024050346A1 (fr) | 2022-09-02 | 2024-03-07 | Danisco Us Inc. | Compositions détergentes et procédés associés |
| WO2024050339A1 (fr) | 2022-09-02 | 2024-03-07 | Danisco Us Inc. | Variants de mannanases et procédés d'utilisation |
| WO2024102698A1 (fr) | 2022-11-09 | 2024-05-16 | Danisco Us Inc. | Variants de subtilisine et procédés d'utilisation |
| CN117305279B (zh) * | 2023-10-08 | 2024-03-26 | 态创生物科技(广州)有限公司 | 高活性和高耐热性的α-淀粉酶突变体及其制备方法和应用 |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4394443A (en) * | 1980-12-18 | 1983-07-19 | Yale University | Method for cloning genes |
| ZA82133B (en) * | 1981-01-15 | 1983-02-23 | Cpc International Inc | A process for cloning the gene coding for a thermostabic alpha amylase into escherichia coli and bacillus subtilis |
| EP0134048B2 (fr) * | 1983-07-06 | 1996-08-14 | Gist-Brocades N.V. | Clonage moléculaire et expression dans des espèces de micro-organismes industriels |
| US4740461A (en) * | 1983-12-27 | 1988-04-26 | Genetics Institute, Inc. | Vectors and methods for transformation of eucaryotic cells |
| US4717662A (en) * | 1985-01-31 | 1988-01-05 | Miles Laboratories, Inc. | Thermal stabilization of alpha-amylase |
| EP0208491B1 (fr) * | 1985-07-03 | 1993-08-25 | Genencor International, Inc. | Polypeptides hybrides et procédé pour leur préparation |
| US5024943A (en) * | 1985-11-07 | 1991-06-18 | Gist-Brocades | Regulatory region cloning and analysis plasmid for bacillus |
| DK311186D0 (da) * | 1986-06-30 | 1986-06-30 | Novo Industri As | Enzymer |
| IL83192A (en) * | 1986-07-18 | 1992-11-15 | Gist Brocades Nv | Method for the preparation of proteins with factor viii activity by microbial host cells;expression vectors,host cells,antibodies |
| EP0285123A3 (fr) * | 1987-04-03 | 1989-02-01 | Stabra AG | Méthode de mutagénèse complète d'acides nucléiques |
| AU2421588A (en) * | 1987-08-11 | 1989-03-09 | Cetus Corporation | Procaryotic xylose isomerase muteins and method to increase protein stability |
-
1990
- 1990-06-27 DE DE69032360T patent/DE69032360T2/de not_active Expired - Lifetime
- 1990-06-27 JP JP02509959A patent/JP3086249B2/ja not_active Expired - Lifetime
- 1990-06-27 EP EP90201706A patent/EP0410498B1/fr not_active Expired - Lifetime
- 1990-06-27 BR BR909006818A patent/BR9006818A/pt not_active Application Discontinuation
- 1990-06-27 DK DK90201706T patent/DK0410498T3/da active
- 1990-06-27 KR KR1019910700227A patent/KR0165550B1/ko not_active IP Right Cessation
- 1990-06-27 US US07/623,953 patent/US5364782A/en not_active Expired - Lifetime
- 1990-06-27 WO PCT/EP1990/001042 patent/WO1991000353A2/fr active IP Right Grant
- 1990-06-27 ES ES90201706T patent/ES2117625T3/es not_active Expired - Lifetime
- 1990-06-27 AT AT90201706T patent/ATE166922T1/de not_active IP Right Cessation
- 1990-06-27 CA CA002030554A patent/CA2030554C/fr not_active Expired - Lifetime
- 1990-06-29 DD DD90342352A patent/DD301620A9/de unknown
- 1990-06-29 CN CN90106811A patent/CN1050220A/zh active Pending
- 1990-06-29 PT PT94560A patent/PT94560B/pt not_active IP Right Cessation
- 1990-06-29 IE IE236990A patent/IE902369A1/en unknown
-
1991
- 1991-02-11 BG BG93814A patent/BG61081B1/bg unknown
- 1991-02-25 FI FI910907A patent/FI103285B1/fi active
-
1999
- 1999-10-27 JP JP11305433A patent/JP2000197491A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| DD301620A9 (de) | 1993-04-29 |
| IE902369A1 (en) | 1991-06-19 |
| IE902369L (en) | 1990-12-29 |
| BR9006818A (pt) | 1991-08-06 |
| DE69032360T2 (de) | 1998-12-03 |
| JP2000197491A (ja) | 2000-07-18 |
| PT94560A (pt) | 1991-02-08 |
| KR0165550B1 (ko) | 1999-01-15 |
| AU5953890A (en) | 1991-01-17 |
| WO1991000353A3 (fr) | 1991-02-21 |
| ES2117625T3 (es) | 1998-08-16 |
| FI103285B (fi) | 1999-05-31 |
| JP3086249B2 (ja) | 2000-09-11 |
| CA2030554C (fr) | 2001-08-28 |
| EP0410498B1 (fr) | 1998-06-03 |
| JPH04500756A (ja) | 1992-02-13 |
| US5364782A (en) | 1994-11-15 |
| FI910907A0 (fi) | 1991-02-25 |
| ATE166922T1 (de) | 1998-06-15 |
| AU638263B2 (en) | 1993-06-24 |
| KR920701449A (ko) | 1992-08-11 |
| EP0410498A3 (en) | 1991-11-06 |
| CN1050220A (zh) | 1991-03-27 |
| DE69032360D1 (de) | 1998-07-09 |
| EP0410498A2 (fr) | 1991-01-30 |
| DK0410498T3 (da) | 1999-03-22 |
| WO1991000353A2 (fr) | 1991-01-10 |
| FI103285B1 (fi) | 1999-05-31 |
| PT94560B (pt) | 1998-01-30 |
| BG93814A (bg) | 1993-12-24 |
| CA2030554A1 (fr) | 1990-12-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| BG61081B1 (bg) | МУТАНТНИ МИКРОБИАЛНИ α-АМИЛАЗИ С ПОВИШЕНА ТЕРМИЧНА, КИСЕЛИННА И/ИЛИ АЛКАЛНА УСТОЙЧИВОСТ | |
| KR102375732B1 (ko) | 바실러스 리체니포르미스에서 단백질 생산을 증가시키기 위한 조성물 및 방법 | |
| EP1419255B1 (fr) | Nouveau groupe d'alpha-amylases, et procede d'identification et d'obtention de nouvelles alpha-amylases | |
| EP1066374B1 (fr) | Variantes d'enzymes amylolytiques | |
| US5731174A (en) | Process for the saccharification of starch | |
| JP2018532413A (ja) | タンパク質発現の増強およびその方法 | |
| JPH04507346A (ja) | アルカリ性タンパク質分解酵素およびその製造方法 | |
| JPH0829091B2 (ja) | ハイブリッドｐｍａ配列の製造方法及び該方法に使用するベクター | |
| AU629959B2 (en) | Mutant enzyme having reduced stability under industrial application conditions | |
| WO2020156903A1 (fr) | Co-expression de foldase parente | |
| EP2451954A1 (fr) | Promoteur modifié | |
| CN115335503A (zh) | 用于增强芽孢杆菌属细胞中蛋白质产生的组合物和方法 | |
| AU638263C (en) | Mutant microbial alpha-amylases with increased thermal, acid and/or alkaline stability | |
| WO2024146919A1 (fr) | Utilisation de foldases pour améliorer l'expression hétérologue de molécules sécrétées | |
| WO2024040043A1 (fr) | Systèmes d'expression pour phosphatases | |
| CN117769597A (zh) | 用于增强芽孢杆菌属细胞中蛋白质产生的组合物和方法 | |
| EP1710303A1 (fr) | Variantes d'enzymes amylolytiques |