DK162776B - Ekspressionsvektor indeholdende et amylasekodningsgen og fremgangsmaade til fremstilling deraf, genetisk konstruerede mikroorganismer med evne til massiv produktion af amylolytiske enzymer og fremgangsmaade til fremstilling af saadanne enzymer - Google Patents
Ekspressionsvektor indeholdende et amylasekodningsgen og fremgangsmaade til fremstilling deraf, genetisk konstruerede mikroorganismer med evne til massiv produktion af amylolytiske enzymer og fremgangsmaade til fremstilling af saadanne enzymer Download PDFInfo
- Publication number
- DK162776B DK162776B DK062881A DK62881A DK162776B DK 162776 B DK162776 B DK 162776B DK 062881 A DK062881 A DK 062881A DK 62881 A DK62881 A DK 62881A DK 162776 B DK162776 B DK 162776B
- Authority
- DK
- Denmark
- Prior art keywords
- dna
- ncib
- phage
- amylase
- coli
- Prior art date
Links
- 239000004382 Amylase Substances 0.000 title claims description 68
- 108010065511 Amylases Proteins 0.000 title claims description 65
- 102000013142 Amylases Human genes 0.000 title claims description 61
- 235000019418 amylase Nutrition 0.000 title claims description 61
- 244000005700 microbiome Species 0.000 title claims description 60
- 238000000034 method Methods 0.000 title claims description 59
- 108090000623 proteins and genes Proteins 0.000 title claims description 37
- 239000013604 expression vector Substances 0.000 title claims description 19
- 238000004519 manufacturing process Methods 0.000 title description 25
- 230000003625 amylolytic effect Effects 0.000 title description 6
- 108020004414 DNA Proteins 0.000 claims description 90
- 239000013612 plasmid Substances 0.000 claims description 80
- 241000588724 Escherichia coli Species 0.000 claims description 61
- 239000013598 vector Substances 0.000 claims description 23
- 241000701959 Escherichia virus Lambda Species 0.000 claims description 22
- 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 claims description 22
- 229960005091 chloramphenicol Drugs 0.000 claims description 21
- 239000012634 fragment Substances 0.000 claims description 21
- 239000002609 medium Substances 0.000 claims description 17
- 229920002472 Starch Polymers 0.000 claims description 16
- 238000003199 nucleic acid amplification method Methods 0.000 claims description 16
- 235000019698 starch Nutrition 0.000 claims description 16
- 230000003321 amplification Effects 0.000 claims description 15
- 239000008107 starch Substances 0.000 claims description 15
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 claims description 13
- 241000194107 Bacillus megaterium Species 0.000 claims description 13
- 229910052740 iodine Inorganic materials 0.000 claims description 13
- 239000011630 iodine Substances 0.000 claims description 13
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 12
- 239000001963 growth medium Substances 0.000 claims description 12
- 101100135809 Mus musculus Pcp2 gene Proteins 0.000 claims description 11
- 239000004373 Pullulan Substances 0.000 claims description 11
- 229920001218 Pullulan Polymers 0.000 claims description 11
- 238000000338 in vitro Methods 0.000 claims description 11
- 235000019423 pullulan Nutrition 0.000 claims description 11
- 230000001580 bacterial effect Effects 0.000 claims description 10
- 241000193749 Bacillus coagulans Species 0.000 claims description 9
- 101100135798 Caenorhabditis elegans pcp-1 gene Proteins 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 8
- 241000588747 Klebsiella pneumoniae Species 0.000 claims description 7
- 229940054340 bacillus coagulans Drugs 0.000 claims description 7
- 238000010186 staining Methods 0.000 claims description 6
- 241000193755 Bacillus cereus Species 0.000 claims description 5
- 238000010438 heat treatment Methods 0.000 claims description 5
- 230000008569 process Effects 0.000 claims description 5
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 4
- 238000000605 extraction Methods 0.000 claims description 4
- 230000002101 lytic effect Effects 0.000 claims description 4
- 108010050327 trypticase-soy broth Proteins 0.000 claims description 4
- 238000003776 cleavage reaction Methods 0.000 claims description 3
- 230000001320 lysogenic effect Effects 0.000 claims description 3
- 230000007017 scission Effects 0.000 claims description 3
- 238000012216 screening Methods 0.000 claims 3
- 230000005526 G1 to G0 transition Effects 0.000 claims 2
- 238000007747 plating Methods 0.000 claims 2
- 241001158232 Bacillus magaterium Species 0.000 claims 1
- 241001660259 Cereus <cactus> Species 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 description 43
- 108090000790 Enzymes Proteins 0.000 description 43
- 229940088598 enzyme Drugs 0.000 description 42
- 230000000694 effects Effects 0.000 description 38
- 108090000637 alpha-Amylases Proteins 0.000 description 32
- 210000004027 cell Anatomy 0.000 description 29
- 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 19
- 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 18
- 102000004139 alpha-Amylases Human genes 0.000 description 17
- 229940024171 alpha-amylase Drugs 0.000 description 17
- 241000894006 Bacteria Species 0.000 description 16
- 238000010367 cloning Methods 0.000 description 16
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- 108091008146 restriction endonucleases Proteins 0.000 description 12
- 238000003780 insertion Methods 0.000 description 11
- 230000037431 insertion Effects 0.000 description 11
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 10
- 239000004098 Tetracycline Substances 0.000 description 9
- 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 9
- 229960002180 tetracycline Drugs 0.000 description 9
- 229930101283 tetracycline Natural products 0.000 description 9
- 235000019364 tetracycline Nutrition 0.000 description 9
- 150000003522 tetracyclines Chemical class 0.000 description 9
- 229960000723 ampicillin Drugs 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- DBTMGCOVALSLOR-UHFFFAOYSA-N 32-alpha-galactosyl-3-alpha-galactosyl-galactose Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(OC2C(C(CO)OC(O)C2O)O)OC(CO)C1O DBTMGCOVALSLOR-UHFFFAOYSA-N 0.000 description 7
- RXVWSYJTUUKTEA-UHFFFAOYSA-N D-maltotriose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(O)C(CO)O1 RXVWSYJTUUKTEA-UHFFFAOYSA-N 0.000 description 7
- 108010061982 DNA Ligases Proteins 0.000 description 7
- 230000002068 genetic effect Effects 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- FYGDTMLNYKFZSV-UHFFFAOYSA-N mannotriose Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(O)C(O)C2O)CO)C(O)C1O FYGDTMLNYKFZSV-UHFFFAOYSA-N 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- FYGDTMLNYKFZSV-BYLHFPJWSA-N β-1,4-galactotrioside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@H](CO)O[C@@H](O[C@@H]2[C@@H](O[C@@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-BYLHFPJWSA-N 0.000 description 7
- 229920000856 Amylose Polymers 0.000 description 6
- 244000063299 Bacillus subtilis Species 0.000 description 6
- 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 6
- 108010019077 beta-Amylase Proteins 0.000 description 6
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 6
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 238000012215 gene cloning Methods 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 230000009466 transformation Effects 0.000 description 6
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 230000002255 enzymatic effect Effects 0.000 description 5
- 238000010353 genetic engineering Methods 0.000 description 5
- 239000008103 glucose Substances 0.000 description 5
- 230000007062 hydrolysis Effects 0.000 description 5
- 238000006460 hydrolysis reaction Methods 0.000 description 5
- 230000000644 propagated effect Effects 0.000 description 5
- 238000011084 recovery Methods 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 102000012410 DNA Ligases Human genes 0.000 description 4
- 241001131785 Escherichia coli HB101 Species 0.000 description 4
- SIKJAQJRHWYJAI-UHFFFAOYSA-N Indole Chemical compound C1=CC=C2NC=CC2=C1 SIKJAQJRHWYJAI-UHFFFAOYSA-N 0.000 description 4
- 102000003960 Ligases Human genes 0.000 description 4
- 108090000364 Ligases Proteins 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 239000006166 lysate Substances 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 230000003204 osmotic effect Effects 0.000 description 4
- 239000002245 particle Substances 0.000 description 4
- 210000001938 protoplast Anatomy 0.000 description 4
- 229920006395 saturated elastomer Polymers 0.000 description 4
- 230000035939 shock Effects 0.000 description 4
- 240000001817 Cereus hexagonus Species 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 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 3
- 229930006000 Sucrose Natural products 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 3
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 230000009089 cytolysis Effects 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 230000002906 microbiologic effect Effects 0.000 description 3
- 238000012261 overproduction Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- ROWKJAVDOGWPAT-UHFFFAOYSA-N Acetoin Chemical compound CC(O)C(C)=O ROWKJAVDOGWPAT-UHFFFAOYSA-N 0.000 description 2
- 102000016938 Catalase Human genes 0.000 description 2
- 108010053835 Catalase Proteins 0.000 description 2
- 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 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 2
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 2
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 241000701533 Escherichia virus T4 Species 0.000 description 2
- 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 2
- 108010010803 Gelatin Proteins 0.000 description 2
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 2
- 102100022624 Glucoamylase Human genes 0.000 description 2
- SQUHHTBVTRBESD-UHFFFAOYSA-N Hexa-Ac-myo-Inositol Natural products CC(=O)OC1C(OC(C)=O)C(OC(C)=O)C(OC(C)=O)C(OC(C)=O)C1OC(C)=O SQUHHTBVTRBESD-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- 206010027439 Metal poisoning Diseases 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 101150010882 S gene Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 2
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 229940077731 carbohydrate nutrients Drugs 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000013611 chromosomal DNA Substances 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 238000012136 culture method Methods 0.000 description 2
- 238000005520 cutting process Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 229960002737 fructose Drugs 0.000 description 2
- FBPFZTCFMRRESA-GUCUJZIJSA-N galactitol Chemical compound OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-GUCUJZIJSA-N 0.000 description 2
- 229930182830 galactose Natural products 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- PZOUSPYUWWUPPK-UHFFFAOYSA-N indole Natural products CC1=CC=CC2=C1C=CN2 PZOUSPYUWWUPPK-UHFFFAOYSA-N 0.000 description 2
- RKJUIXBNRJVNHR-UHFFFAOYSA-N indolenine Natural products C1=CC=C2CC=NC2=C1 RKJUIXBNRJVNHR-UHFFFAOYSA-N 0.000 description 2
- CDAISMWEOUEBRE-GPIVLXJGSA-N inositol Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O CDAISMWEOUEBRE-GPIVLXJGSA-N 0.000 description 2
- 229960000367 inositol Drugs 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- -1 melibiosis Chemical compound 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 238000010899 nucleation Methods 0.000 description 2
- 239000006916 nutrient agar Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 238000006395 oxidase reaction Methods 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 238000004806 packaging method and process Methods 0.000 description 2
- 229920005862 polyol Polymers 0.000 description 2
- 150000003077 polyols Chemical class 0.000 description 2
- 238000001243 protein synthesis Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- CDAISMWEOUEBRE-UHFFFAOYSA-N scyllo-inosotol Natural products OC1C(O)C(O)C(O)C(O)C1O CDAISMWEOUEBRE-UHFFFAOYSA-N 0.000 description 2
- 239000000600 sorbitol Substances 0.000 description 2
- 238000009331 sowing Methods 0.000 description 2
- 238000007447 staining method Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- 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 1
- FBFJAXUYHGSVFN-UHFFFAOYSA-N 25(R)-pennogenin-3-O-alpha-L-rhamnopyranosyl-(14)-alpha-L-rhamnopyranosyl-(14)-[alpha-L-rhamnopyranosyl-(12)]-beta-D-glucopyranoside Natural products O1C2CC3C4CC=C5CC(OC6C(C(O)C(OC7C(C(O)C(OC8C(C(O)C(O)C(C)O8)O)C(C)O7)O)C(CO)O6)OC6C(C(O)C(O)C(C)O6)O)CCC5(C)C4CCC3(C)C2(O)C(C)C21CCC(C)CO2 FBFJAXUYHGSVFN-UHFFFAOYSA-N 0.000 description 1
- FBFJAXUYHGSVFN-IYUYFXHASA-N 68124-04-9 Chemical compound C([C@@]12[C@H]([C@@]3([C@@]4(C)CC[C@@H]5[C@@]6(C)CC[C@@H](CC6=CC[C@H]5[C@@H]4C[C@@H]3O2)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]4[C@@H]([C@H](O)[C@@H](O)[C@H](C)O4)O)[C@H](C)O3)O)[C@@H](CO)O2)O[C@H]2[C@@H]([C@H](O)[C@@H](O)[C@H](C)O2)O)O)C)C[C@@H](C)CO1 FBFJAXUYHGSVFN-IYUYFXHASA-N 0.000 description 1
- 241000186046 Actinomyces Species 0.000 description 1
- 229920000945 Amylopectin Polymers 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 241000193752 Bacillus circulans Species 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 229920000858 Cyclodextrin Polymers 0.000 description 1
- 102000000634 Cytochrome c oxidase subunit IV Human genes 0.000 description 1
- 108050008072 Cytochrome c oxidase subunit IV Proteins 0.000 description 1
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
- ZCLAHGAZPPEVDX-UHFFFAOYSA-N D-panose Natural products OC1C(O)C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC1COC1C(O)C(O)C(O)C(CO)O1 ZCLAHGAZPPEVDX-UHFFFAOYSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 101150013191 E gene Proteins 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
- 241000644323 Escherichia coli C Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 229920001202 Inulin Polymers 0.000 description 1
- 108010028688 Isoamylase Proteins 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- SHZGCJCMOBCMKK-JFNONXLTSA-N L-rhamnopyranose Chemical compound C[C@@H]1OC(O)[C@H](O)[C@H](O)[C@H]1O SHZGCJCMOBCMKK-JFNONXLTSA-N 0.000 description 1
- PNNNRSAQSRJVSB-UHFFFAOYSA-N L-rhamnose Natural products CC(O)C(O)C(O)C(O)C=O PNNNRSAQSRJVSB-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 229920002774 Maltodextrin Polymers 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- 208000012868 Overgrowth Diseases 0.000 description 1
- 206010035148 Plague Diseases 0.000 description 1
- MUPFEKGTMRGPLJ-RMMQSMQOSA-N Raffinose Natural products O(C[C@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O[C@@]2(CO)[C@H](O)[C@@H](O)[C@@H](CO)O2)O1)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 MUPFEKGTMRGPLJ-RMMQSMQOSA-N 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- MUPFEKGTMRGPLJ-UHFFFAOYSA-N UNPD196149 Natural products OC1C(O)C(CO)OC1(CO)OC1C(O)C(O)C(O)C(COC2C(C(O)C(O)C(CO)O2)O)O1 MUPFEKGTMRGPLJ-UHFFFAOYSA-N 0.000 description 1
- 241000607479 Yersinia pestis Species 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000007864 aqueous solution 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
- 239000011324 bead Substances 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229910052792 caesium Inorganic materials 0.000 description 1
- TVFDJXOCXUVLDH-UHFFFAOYSA-N caesium atom Chemical compound [Cs] TVFDJXOCXUVLDH-UHFFFAOYSA-N 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 239000002361 compost Substances 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 208000010501 heavy metal poisoning Diseases 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- JYJIGFIDKWBXDU-MNNPPOADSA-N inulin Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)OC[C@]1(OC[C@]2(OC[C@]3(OC[C@]4(OC[C@]5(OC[C@]6(OC[C@]7(OC[C@]8(OC[C@]9(OC[C@]%10(OC[C@]%11(OC[C@]%12(OC[C@]%13(OC[C@]%14(OC[C@]%15(OC[C@]%16(OC[C@]%17(OC[C@]%18(OC[C@]%19(OC[C@]%20(OC[C@]%21(OC[C@]%22(OC[C@]%23(OC[C@]%24(OC[C@]%25(OC[C@]%26(OC[C@]%27(OC[C@]%28(OC[C@]%29(OC[C@]%30(OC[C@]%31(OC[C@]%32(OC[C@]%33(OC[C@]%34(OC[C@]%35(OC[C@]%36(O[C@@H]%37[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O%37)O)[C@H]([C@H](O)[C@@H](CO)O%36)O)[C@H]([C@H](O)[C@@H](CO)O%35)O)[C@H]([C@H](O)[C@@H](CO)O%34)O)[C@H]([C@H](O)[C@@H](CO)O%33)O)[C@H]([C@H](O)[C@@H](CO)O%32)O)[C@H]([C@H](O)[C@@H](CO)O%31)O)[C@H]([C@H](O)[C@@H](CO)O%30)O)[C@H]([C@H](O)[C@@H](CO)O%29)O)[C@H]([C@H](O)[C@@H](CO)O%28)O)[C@H]([C@H](O)[C@@H](CO)O%27)O)[C@H]([C@H](O)[C@@H](CO)O%26)O)[C@H]([C@H](O)[C@@H](CO)O%25)O)[C@H]([C@H](O)[C@@H](CO)O%24)O)[C@H]([C@H](O)[C@@H](CO)O%23)O)[C@H]([C@H](O)[C@@H](CO)O%22)O)[C@H]([C@H](O)[C@@H](CO)O%21)O)[C@H]([C@H](O)[C@@H](CO)O%20)O)[C@H]([C@H](O)[C@@H](CO)O%19)O)[C@H]([C@H](O)[C@@H](CO)O%18)O)[C@H]([C@H](O)[C@@H](CO)O%17)O)[C@H]([C@H](O)[C@@H](CO)O%16)O)[C@H]([C@H](O)[C@@H](CO)O%15)O)[C@H]([C@H](O)[C@@H](CO)O%14)O)[C@H]([C@H](O)[C@@H](CO)O%13)O)[C@H]([C@H](O)[C@@H](CO)O%12)O)[C@H]([C@H](O)[C@@H](CO)O%11)O)[C@H]([C@H](O)[C@@H](CO)O%10)O)[C@H]([C@H](O)[C@@H](CO)O9)O)[C@H]([C@H](O)[C@@H](CO)O8)O)[C@H]([C@H](O)[C@@H](CO)O7)O)[C@H]([C@H](O)[C@@H](CO)O6)O)[C@H]([C@H](O)[C@@H](CO)O5)O)[C@H]([C@H](O)[C@@H](CO)O4)O)[C@H]([C@H](O)[C@@H](CO)O3)O)[C@H]([C@H](O)[C@@H](CO)O2)O)[C@@H](O)[C@H](O)[C@@H](CO)O1 JYJIGFIDKWBXDU-MNNPPOADSA-N 0.000 description 1
- 229940029339 inulin Drugs 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 125000003071 maltose group Chemical group 0.000 description 1
- HEBKCHPVOIAQTA-UHFFFAOYSA-N meso ribitol Natural products OCC(O)C(O)C(O)CO HEBKCHPVOIAQTA-UHFFFAOYSA-N 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
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 150000002823 nitrates Chemical class 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- ZCLAHGAZPPEVDX-MQHGYYCBSA-N panose Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@@H](O[C@H]([C@H](O)CO)[C@H](O)[C@@H](O)C=O)O[C@@H]1CO[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 ZCLAHGAZPPEVDX-MQHGYYCBSA-N 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 108700010839 phage proteins Proteins 0.000 description 1
- 210000004180 plasmocyte Anatomy 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- MUPFEKGTMRGPLJ-ZQSKZDJDSA-N raffinose 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[C@@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)O1 MUPFEKGTMRGPLJ-ZQSKZDJDSA-N 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- HEBKCHPVOIAQTA-ZXFHETKHSA-N ribitol Chemical compound OC[C@H](O)[C@H](O)[C@H](O)CO HEBKCHPVOIAQTA-ZXFHETKHSA-N 0.000 description 1
- 239000007320 rich medium Substances 0.000 description 1
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 101150118377 tet gene Proteins 0.000 description 1
- 238000004809 thin layer chromatography Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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)
- C12N9/24—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
-
- 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
-
- 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
-
- 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
- C12N9/2425—Beta-amylase (3.2.1.2)
-
- 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
- C12N9/2451—Glucanases acting on alpha-1,6-glucosidic bonds
- C12N9/2457—Pullulanase (3.2.1.41)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01041—Pullulanase (3.2.1.41)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/832—Bacillus
- Y10S435/839—Bacillus subtilis
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/848—Escherichia
- Y10S435/849—Escherichia coli
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB8005184 | 1980-02-15 | ||
| GB8005184 | 1980-02-15 | ||
| GB8011842 | 1980-04-10 | ||
| GB8011842 | 1980-04-10 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DK62881A DK62881A (da) | 1981-08-16 |
| DK162776B true DK162776B (da) | 1991-12-09 |
Family
ID=26274508
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK062881A DK162776B (da) | 1980-02-15 | 1981-02-13 | Ekspressionsvektor indeholdende et amylasekodningsgen og fremgangsmaade til fremstilling deraf, genetisk konstruerede mikroorganismer med evne til massiv produktion af amylolytiske enzymer og fremgangsmaade til fremstilling af saadanne enzymer |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US4469791A (index.php) |
| EP (1) | EP0034470B1 (index.php) |
| CA (1) | CA1183090A (index.php) |
| DD (3) | DD207553A5 (index.php) |
| DE (1) | DE3177286T2 (index.php) |
| DK (1) | DK162776B (index.php) |
| ES (1) | ES8202362A1 (index.php) |
| FI (1) | FI70424C (index.php) |
| GB (1) | GB2069503B (index.php) |
| GR (1) | GR73678B (index.php) |
| HU (1) | HU195533B (index.php) |
| IE (1) | IE50919B1 (index.php) |
| IL (1) | IL61982A (index.php) |
| KE (1) | KE3310A (index.php) |
| RU (1) | RU1838410C (index.php) |
| YU (2) | YU43634B (index.php) |
Families Citing this family (48)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU545912B2 (en) * | 1980-03-10 | 1985-08-08 | Cetus Corporation | Cloned heterologous jive products in bacillies |
| US4874702A (en) * | 1980-09-08 | 1989-10-17 | Biogen, Inc. | Vectors and methods for making such vectors and for expressive cloned genes |
| FI64813C (fi) * | 1980-12-31 | 1984-01-10 | Ilkka Antero Palva | Foerfarande foer producering av ett utvalt aeggviteaemne och vid foerfarandet anvaenda rekombinantplasmidvektorer |
| US4493893A (en) * | 1981-01-15 | 1985-01-15 | Cpc International Inc. | Process for cloning the gene coding for a thermostable alpha-amylase into Escherichia coli and Bacillus subtilis |
| IE52434B1 (en) * | 1981-01-15 | 1987-10-28 | Cpc International Inc | A process for cloning the gene coding for a thermostable alpha-amylase into escherichia coli and bacillus subtilis |
| US5525484A (en) * | 1981-01-16 | 1996-06-11 | Genome Therapeutics Corp. | Recombinant DNA means and method for producing rennin, prorenin and pre-prorennin |
| DE3279270D1 (en) * | 1981-09-02 | 1989-01-12 | Biogen Nv | Amplified expression of dna sequences |
| US5254463A (en) * | 1981-09-18 | 1993-10-19 | Genentech, Inc. | Method for expression of bovine growth hormone |
| US4508826A (en) * | 1982-04-15 | 1985-04-02 | Merck & Co., Inc. | Bacteriophage DNA cloning vector TG1 and microorganisms containing TG1 |
| US4460689A (en) * | 1982-04-15 | 1984-07-17 | Merck & Co., Inc. | DNA Cloning vector TG1, derivatives, and processes of making |
| FR2537602B2 (fr) * | 1982-09-24 | 1986-10-24 | Centre Nat Rech Scient | Nouvel adn recombinant perfectionne utile dans la preparation d'a-amylase par bacillus subtilis |
| FR2533583A1 (fr) * | 1982-09-24 | 1984-03-30 | Centre Nat Rech Scient | Nouvel adn recombinant utile dans la preparation d'a-amylase |
| ATE48156T1 (de) * | 1982-11-01 | 1989-12-15 | Miles Inc | Verfahren zur heterologen klonierung eines gens in einem bacillus-mikroorganismus. |
| NO840200L (no) * | 1983-01-28 | 1984-07-30 | Cefus Corp | Glukoamylase cdna. |
| DK135983D0 (da) * | 1983-03-25 | 1983-03-25 | Novo Industri As | Maltogen amylaseenzymprodukt og fremgangsmade til dets fremstilling og anvendelse |
| JPS59196092A (ja) * | 1983-04-25 | 1984-11-07 | Sanraku Inc | 組換えプラスミドによる耐熱性α−アミラ−ゼの新規製造法 |
| GR82200B (index.php) * | 1983-07-06 | 1984-12-13 | Gist Brocades Nv | |
| US5624829A (en) * | 1984-07-03 | 1997-04-29 | Gist-Brocades, B.V. | Transformed industrial bacillus strains and methods for making and using them |
| US4578352A (en) * | 1983-07-13 | 1986-03-25 | Cpc International Inc. | Novel thermostable, aciduric alpha-amylase and method for its production |
| FR2556008B1 (fr) * | 1983-12-06 | 1987-06-26 | Centre Nat Rech Scient | Vecteurs plasmidiques de clonage et d'expression d'une proteine dans un micro-organisme, comportant au moins le promoteur d'expression de la b-glucosidase dans les levures; micro-organismes les contenant; procede de fermentation et enzymes obtenues |
| GB8333797D0 (en) * | 1983-12-19 | 1984-01-25 | Searle & Co | Starch utilization |
| PH23920A (en) * | 1983-12-20 | 1990-01-23 | Cetus Corp | Glucoamylase cdna |
| GB8414272D0 (en) * | 1984-06-05 | 1984-07-11 | Cpc International Inc | Enzymatic hydrolysis |
| GB8414271D0 (en) * | 1984-06-05 | 1984-07-11 | Cpc International Inc | Recombinant dna |
| JPH062061B2 (ja) * | 1984-06-14 | 1994-01-12 | 協和醗酵工業株式会社 | Ｎ−アセチルノイラミン酸リア−ゼの製法 |
| US5489529A (en) * | 1984-07-19 | 1996-02-06 | De Boer; Herman A. | DNA for expression of bovine growth hormone |
| JPH0630586B2 (ja) * | 1984-12-15 | 1994-04-27 | サントリー株式会社 | グルコアミラ−ゼ遺伝子 |
| JPS61162183A (ja) * | 1985-01-07 | 1986-07-22 | Agency Of Ind Science & Technol | プルラナ−ゼ様酵素の製造法 |
| US4769327A (en) * | 1985-03-29 | 1988-09-06 | Biotechnica International, Inc. | Secretion vector |
| DE3688920D1 (de) * | 1985-07-03 | 1993-09-30 | Genencor Int | Hybride Polypeptide und Verfahren zu deren Herstellung. |
| JPH0616711B2 (ja) * | 1985-09-27 | 1994-03-09 | メルシャン株式会社 | 高温で自律増殖するプラスミド |
| SE8505027D0 (sv) * | 1985-10-24 | 1985-10-24 | Kabigen Ab | A lytic virulent phage, a hostcell containing same and a process for protein production |
| US5017477A (en) * | 1985-10-25 | 1991-05-21 | Biotechnica International, Inc. | Enhancing DNA sequencies derived from the sacQ gene |
| FR2598431B1 (fr) * | 1986-05-09 | 1990-02-09 | Transgene Sa | Souches de saccharomyces produisant de l'alpha-amylase |
| US4962026A (en) * | 1986-09-15 | 1990-10-09 | Enzyme Bio-Systems, Ltd. | Process for the production of panosyl derivatives |
| WO1988006623A1 (en) * | 1987-02-27 | 1988-09-07 | Gist-Brocades N.V. | Stable gene amplification in chromosomal dna of prokaryotic microorganisms |
| JPH01218589A (ja) * | 1988-02-26 | 1989-08-31 | Juzo Udaka | 耐熱性β−アミラーゼ遺伝子 |
| US5171673A (en) * | 1988-07-18 | 1992-12-15 | Biotechnica International, Inc. | Expression of heterologous dna using the bacillus coagulans amylase gene |
| US5209938A (en) * | 1989-09-13 | 1993-05-11 | Cpc International Inc. | Method for retarding staling of baked goods |
| US5583039A (en) * | 1990-06-07 | 1996-12-10 | Sunkyong Industries Ltd. | Escherichia coli containing a gene encoding a maltogenic amylase BLMA of Bacillus licheniformis and gene product produced by same |
| JPH05508997A (ja) * | 1990-08-01 | 1993-12-16 | ノボ ノルディスク アクティーゼルスカブ | 新規熱安定性プルラナーゼ |
| DE4029844A1 (de) * | 1990-09-20 | 1992-03-26 | Boehringer Mannheim Gmbh | Carbamoylsarcosinhydrolase, kloniert |
| DK47291D0 (da) * | 1991-03-15 | 1991-03-15 | Novo Nordisk As | Pullulanase |
| WO1994026881A1 (fr) * | 1993-05-19 | 1994-11-24 | Kao Corporation | α-AMYLASE ALCALINE LIQUEFIANTE, PROCEDE ET PRODUCTION ET COMPOSITION DETERGENTE LA CONTENANT |
| CA2173453C (en) * | 1993-10-05 | 2001-02-13 | Patricia A. Bower | Cloned pullulanase |
| US6300115B1 (en) | 1998-05-18 | 2001-10-09 | Enzyme Bio-Systems Ltd. | Pullulanase expression constructs containing α-amylase promoter and leader sequences |
| US7220542B2 (en) * | 2000-07-17 | 2007-05-22 | Van Den Brink Johannes Maarten | Expression cloning in filamentous fungi |
| CN115029336B (zh) * | 2022-01-10 | 2025-05-16 | 昆明理工大学 | 一种具有洗涤剂抗性的普鲁兰酶PulY103B及其应用 |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1521032A (en) * | 1974-08-08 | 1978-08-09 | Ici Ltd | Biological treatment |
| US4237224A (en) * | 1974-11-04 | 1980-12-02 | Board Of Trustees Of The Leland Stanford Jr. University | Process for producing biologically functional molecular chimeras |
| JPS5811998B2 (ja) * | 1975-12-19 | 1983-03-05 | マルオ ブンジ | シンキナアミラ−ゼノセイゾウホウホウ |
| NZ187300A (en) * | 1977-05-27 | 1982-08-17 | Univ California | Dna transfer vector and micro-organism modified to contain a nucleotide sequence equivalent to the gene of a higher organism |
| IL58308A (en) * | 1978-10-23 | 1983-10-31 | Upjohn Co | Process for preparing glucose isomerase using a recombinant plasmid |
-
1981
- 1981-01-26 IL IL61982A patent/IL61982A/xx unknown
- 1981-02-12 FI FI810425A patent/FI70424C/fi not_active IP Right Cessation
- 1981-02-12 EP EP81300578A patent/EP0034470B1/en not_active Expired
- 1981-02-12 DE DE8181300578T patent/DE3177286T2/de not_active Expired - Lifetime
- 1981-02-12 GB GB8104473A patent/GB2069503B/en not_active Expired
- 1981-02-13 ES ES499391A patent/ES8202362A1/es not_active Expired
- 1981-02-13 YU YU377/81A patent/YU43634B/xx unknown
- 1981-02-13 DK DK062881A patent/DK162776B/da unknown
- 1981-02-13 GR GR64133A patent/GR73678B/el unknown
- 1981-02-13 CA CA000370775A patent/CA1183090A/en not_active Expired
- 1981-02-13 US US06/234,140 patent/US4469791A/en not_active Expired - Fee Related
- 1981-02-13 IE IE297/81A patent/IE50919B1/en not_active IP Right Cessation
- 1981-02-13 HU HU81363A patent/HU195533B/hu not_active IP Right Cessation
- 1981-02-16 DD DD81245452A patent/DD207553A5/de unknown
- 1981-02-16 DD DD81227656A patent/DD158917A5/de unknown
- 1981-02-16 DD DD81245456A patent/DD207221A5/de unknown
-
1982
- 1982-06-11 RU SU823451221A patent/RU1838410C/ru active
-
1983
- 1983-04-15 YU YU867/83A patent/YU44739B/xx unknown
- 1983-07-22 KE KE3310A patent/KE3310A/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| ES499391A0 (es) | 1982-01-01 |
| GB2069503A (en) | 1981-08-26 |
| EP0034470A3 (en) | 1982-02-10 |
| IE810297L (en) | 1981-08-15 |
| IE50919B1 (en) | 1986-08-20 |
| DK62881A (da) | 1981-08-16 |
| YU44739B (en) | 1991-02-28 |
| IL61982A0 (en) | 1981-02-27 |
| DE3177286D1 (de) | 1992-09-17 |
| FI70424C (fi) | 1986-09-19 |
| YU43634B (en) | 1989-10-31 |
| GB2069503B (en) | 1983-04-20 |
| FI810425L (fi) | 1981-08-16 |
| GR73678B (index.php) | 1984-03-30 |
| IL61982A (en) | 1984-01-31 |
| EP0034470A2 (en) | 1981-08-26 |
| HU195533B (en) | 1988-05-30 |
| DD207221A5 (de) | 1984-02-22 |
| RU1838410C (ru) | 1993-08-30 |
| KE3310A (en) | 1983-08-26 |
| FI70424B (fi) | 1986-03-27 |
| US4469791A (en) | 1984-09-04 |
| CA1183090A (en) | 1985-02-26 |
| DD207553A5 (de) | 1984-03-07 |
| ES8202362A1 (es) | 1982-01-01 |
| YU86783A (en) | 1985-10-31 |
| EP0034470B1 (en) | 1992-08-12 |
| DD158917A5 (de) | 1983-02-09 |
| YU37781A (en) | 1985-03-20 |
| DE3177286T2 (de) | 1992-12-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DK162776B (da) | Ekspressionsvektor indeholdende et amylasekodningsgen og fremgangsmaade til fremstilling deraf, genetisk konstruerede mikroorganismer med evne til massiv produktion af amylolytiske enzymer og fremgangsmaade til fremstilling af saadanne enzymer | |
| US4493893A (en) | Process for cloning the gene coding for a thermostable alpha-amylase into Escherichia coli and Bacillus subtilis | |
| US6432689B1 (en) | Alkaliphilic and thermophilic microorganisms and enzymes obtained therefrom | |
| EP0120693B1 (en) | Maltogenic amylase enzyme product, preparation and use thereof | |
| Cornet et al. | Characterization of two cel (cellulose degradation) genes of Clostridium thermocellum coding for endoglucanases | |
| WO1992002614A1 (en) | Novel thermostable pullulanases | |
| JPH04500756A (ja) | 熱、酸及び／またはアルカリに高い安定性を有する細菌由来突然変異体α―アミラーゼ | |
| EP0057976B1 (en) | a process for cloning the gene coding for a thermostable alpha-amylase into escherichia coli and bacillus subtilis | |
| US5912150A (en) | Pyrodictium xylanase, amylase and pullulanase | |
| US4612287A (en) | Plasmids containing a gene coding for a thermostable pullulanase and pullulanase-producing strains of Escherichia coli and Bacillus subtilis containing the plasmids | |
| NO159863B (no) | Fremgangsmaate for fremstilling og seleksjon av en rekombinant bakteriofag som inneholder et genetisk fragment og koder for alfa-amylase, egnet for bruk i heterolog transformering av en bacillus-verts-mikroorganisme. | |
| US6338959B1 (en) | Gene for enzyme having both alkaline pullulanase and alkaline α-amylase activities | |
| EP0149915A2 (en) | Starch utilization by gram negative microorganisms | |
| EP0640138B1 (en) | Dna fragment containing gene for alkaline pullulanase | |
| FI75367C (fi) | Foerfarande foer framstaellning av en genetiskt manipulerad mikroorganism innehaollande en foer amylas kodande rekombinant-dna, och ett foerfarande foer framstaellning av amylas. | |
| JP2913411B2 (ja) | セルラーゼ遺伝子 | |
| JPH0223872A (ja) | 組換えプラスミド，それにより形質転換された枯草菌及びそれによる耐熱性プルラナーゼの製造法 | |
| JPS6243677B2 (index.php) | ||
| Hillarby | A Study of the Thermostable Alpha-Amylase bacillus Licheniformis | |
| JPH02227083A (ja) | 新規プラスミド |