JPH09500014A - 菌類のタンパク質ジスルフィドイソメラーゼ - Google Patents
菌類のタンパク質ジスルフィドイソメラーゼInfo
- Publication number
- JPH09500014A JPH09500014A JP7502358A JP50235895A JPH09500014A JP H09500014 A JPH09500014 A JP H09500014A JP 7502358 A JP7502358 A JP 7502358A JP 50235895 A JP50235895 A JP 50235895A JP H09500014 A JPH09500014 A JP H09500014A
- Authority
- JP
- Japan
- Prior art keywords
- enzyme
- protein disulfide
- protein
- seq
- disulfide isomerase
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Ceased
Links
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 title claims abstract description 127
- 108010058643 Fungal Proteins Proteins 0.000 title abstract description 7
- 108020003519 protein disulfide isomerase Proteins 0.000 claims abstract description 125
- 238000004519 manufacturing process Methods 0.000 claims abstract description 16
- 241000228212 Aspergillus Species 0.000 claims abstract description 13
- 241000233866 Fungi Species 0.000 claims abstract description 13
- 108090000623 proteins and genes Proteins 0.000 claims description 65
- 102000004190 Enzymes Human genes 0.000 claims description 64
- 108090000790 Enzymes Proteins 0.000 claims description 64
- 210000004027 cell Anatomy 0.000 claims description 54
- 229940088598 enzyme Drugs 0.000 claims description 54
- 238000000034 method Methods 0.000 claims description 51
- 108020004414 DNA Proteins 0.000 claims description 48
- 102000004169 proteins and genes Human genes 0.000 claims description 48
- 235000018102 proteins Nutrition 0.000 claims description 47
- 150000001413 amino acids Chemical class 0.000 claims description 34
- 239000000203 mixture Substances 0.000 claims description 27
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 26
- 241000209094 Oryza Species 0.000 claims description 19
- 230000000694 effects Effects 0.000 claims description 19
- 239000013598 vector Substances 0.000 claims description 15
- 241000282414 Homo sapiens Species 0.000 claims description 12
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 10
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 claims description 9
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 9
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 9
- 210000004209 hair Anatomy 0.000 claims description 9
- 241000228245 Aspergillus niger Species 0.000 claims description 8
- 230000002538 fungal effect Effects 0.000 claims description 8
- 239000013604 expression vector Substances 0.000 claims description 7
- 229920001184 polypeptide Polymers 0.000 claims description 7
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 7
- 241000894006 Bacteria Species 0.000 claims description 6
- 241001465754 Metazoa Species 0.000 claims description 6
- 108010065511 Amylases Proteins 0.000 claims description 5
- 108091005804 Peptidases Proteins 0.000 claims description 5
- 102000035195 Peptidases Human genes 0.000 claims description 5
- 238000010367 cloning Methods 0.000 claims description 5
- 150000002019 disulfides Chemical class 0.000 claims description 5
- 102000013142 Amylases Human genes 0.000 claims description 4
- 235000019418 amylase Nutrition 0.000 claims description 4
- 230000001580 bacterial effect Effects 0.000 claims description 4
- 235000013305 food Nutrition 0.000 claims description 4
- 239000007788 liquid Substances 0.000 claims description 4
- 239000000523 sample Substances 0.000 claims description 4
- 239000004365 Protease Substances 0.000 claims description 3
- 229940025131 amylases Drugs 0.000 claims description 3
- 239000004744 fabric Substances 0.000 claims description 3
- 239000010985 leather Substances 0.000 claims description 3
- 230000000813 microbial effect Effects 0.000 claims description 3
- 235000015927 pasta Nutrition 0.000 claims description 3
- 238000003259 recombinant expression Methods 0.000 claims description 3
- 208000002177 Cataract Diseases 0.000 claims description 2
- 241000223218 Fusarium Species 0.000 claims description 2
- 108010068370 Glutens Proteins 0.000 claims description 2
- 108090001060 Lipase Proteins 0.000 claims description 2
- 102000004882 Lipase Human genes 0.000 claims description 2
- 239000004367 Lipase Substances 0.000 claims description 2
- 108700020962 Peroxidase Proteins 0.000 claims description 2
- 102000003992 Peroxidases Human genes 0.000 claims description 2
- 241000235070 Saccharomyces Species 0.000 claims description 2
- 239000003599 detergent Substances 0.000 claims description 2
- 125000002228 disulfide group Chemical group 0.000 claims description 2
- 230000001747 exhibiting effect Effects 0.000 claims description 2
- 235000021312 gluten Nutrition 0.000 claims description 2
- 235000019421 lipase Nutrition 0.000 claims description 2
- 230000000087 stabilizing effect Effects 0.000 claims description 2
- 230000008719 thickening Effects 0.000 claims description 2
- 210000005253 yeast cell Anatomy 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 101710167800 Capsid assembly scaffolding protein Proteins 0.000 claims 2
- 101710130420 Probable capsid assembly scaffolding protein Proteins 0.000 claims 2
- 102000001708 Protein Isoforms Human genes 0.000 claims 2
- 108010029485 Protein Isoforms Proteins 0.000 claims 2
- 101710204410 Scaffold protein Proteins 0.000 claims 2
- 241000193830 Bacillus <bacterium> Species 0.000 claims 1
- 108010059892 Cellulase Proteins 0.000 claims 1
- 102000010911 Enzyme Precursors Human genes 0.000 claims 1
- 108010062466 Enzyme Precursors Proteins 0.000 claims 1
- 241000588722 Escherichia Species 0.000 claims 1
- 244000043158 Lens esculenta Species 0.000 claims 1
- 229940106157 cellulase Drugs 0.000 claims 1
- 230000035617 depilation Effects 0.000 claims 1
- 239000008187 granular material Substances 0.000 claims 1
- 239000008194 pharmaceutical composition Substances 0.000 claims 1
- 230000001681 protective effect Effects 0.000 claims 1
- 230000017854 proteolysis Effects 0.000 claims 1
- 230000003248 secreting effect Effects 0.000 claims 1
- 241000894007 species Species 0.000 claims 1
- 108060008226 thioredoxin Proteins 0.000 description 25
- 102000002933 Thioredoxin Human genes 0.000 description 22
- 239000012634 fragment Substances 0.000 description 15
- 240000006439 Aspergillus oryzae Species 0.000 description 14
- 239000000047 product Substances 0.000 description 13
- 235000001014 amino acid Nutrition 0.000 description 12
- 229940024606 amino acid Drugs 0.000 description 12
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 11
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 11
- 239000013612 plasmid Substances 0.000 description 11
- 108020004705 Codon Proteins 0.000 description 10
- 125000000539 amino acid group Chemical group 0.000 description 10
- 102220201851 rs143406017 Human genes 0.000 description 10
- 238000003752 polymerase chain reaction Methods 0.000 description 9
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 7
- 101150070377 PDI gene Proteins 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 239000002299 complementary DNA Substances 0.000 description 7
- 239000002265 redox agent Substances 0.000 description 6
- 230000009466 transformation Effects 0.000 description 6
- 241000287828 Gallus gallus Species 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 108020004707 nucleic acids Proteins 0.000 description 5
- 102000039446 nucleic acids Human genes 0.000 description 5
- 150000007523 nucleic acids Chemical class 0.000 description 5
- 229940081969 saccharomyces cerevisiae Drugs 0.000 description 5
- 235000014469 Bacillus subtilis Nutrition 0.000 description 4
- 241000283690 Bos taurus Species 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 239000011543 agarose gel Substances 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 230000010076 replication Effects 0.000 description 4
- 108010001535 sulfhydryl oxidase Proteins 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 244000063299 Bacillus subtilis Species 0.000 description 3
- 240000004658 Medicago sativa Species 0.000 description 3
- 101100182721 Mus musculus Ly6e gene Proteins 0.000 description 3
- 238000012408 PCR amplification Methods 0.000 description 3
- 241000700157 Rattus norvegicus Species 0.000 description 3
- 102100036407 Thioredoxin Human genes 0.000 description 3
- 108090000637 alpha-Amylases Proteins 0.000 description 3
- 102000004139 alpha-Amylases Human genes 0.000 description 3
- 229940024171 alpha-amylase Drugs 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 210000000349 chromosome Anatomy 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 239000013613 expression plasmid Substances 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 238000005342 ion exchange Methods 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 229940124276 oligodeoxyribonucleotide Drugs 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 230000008929 regeneration Effects 0.000 description 3
- 238000011069 regeneration method Methods 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 210000002268 wool Anatomy 0.000 description 3
- 101150025017 440 gene Proteins 0.000 description 2
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 2
- 241001598984 Bromius obscurus Species 0.000 description 2
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 102000004195 Isomerases Human genes 0.000 description 2
- 108090000769 Isomerases Proteins 0.000 description 2
- 235000017587 Medicago sativa ssp. sativa Nutrition 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 238000002105 Southern blotting Methods 0.000 description 2
- 108010006785 Taq Polymerase Proteins 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 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 2
- -1 amyL Chemical class 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 230000010354 integration Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 239000002751 oligonucleotide probe Substances 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 210000001938 protoplast Anatomy 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 229940094937 thioredoxin Drugs 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- 101150056632 1.6 gene Proteins 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- 101710097567 12 kDa protein Proteins 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 241000193375 Bacillus alcalophilus Species 0.000 description 1
- 241000193752 Bacillus circulans Species 0.000 description 1
- 241000193749 Bacillus coagulans Species 0.000 description 1
- 241000193422 Bacillus lentus Species 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 108010029675 Bacillus licheniformis alpha-amylase Proteins 0.000 description 1
- 241000194107 Bacillus megaterium Species 0.000 description 1
- 241000193364 Bacillus thuringiensis serovar thuringiensis Species 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 101001072209 Bos taurus Protein disulfide-isomerase Proteins 0.000 description 1
- 241000193764 Brevibacillus brevis Species 0.000 description 1
- 101100208421 Candida albicans (strain SC5314 / ATCC MYA-2876) TMP1 gene Proteins 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 101800004637 Communis Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 101100342470 Dictyostelium discoideum pkbA gene Proteins 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 101100385973 Escherichia coli (strain K12) cycA gene Proteins 0.000 description 1
- 206010015958 Eye pain Diseases 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 241000223221 Fusarium oxysporum Species 0.000 description 1
- 241001149959 Fusarium sp. Species 0.000 description 1
- 101100001650 Geobacillus stearothermophilus amyM gene Proteins 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 101100295959 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) arcB gene Proteins 0.000 description 1
- 101100182720 Homo sapiens LY6E gene Proteins 0.000 description 1
- 102220547770 Inducible T-cell costimulator_A23L_mutation Human genes 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 102100032131 Lymphocyte antigen 6E Human genes 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 235000010624 Medicago sativa Nutrition 0.000 description 1
- 101710164418 Movement protein TGB2 Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000194109 Paenibacillus lautus Species 0.000 description 1
- 239000005662 Paraffin oil Substances 0.000 description 1
- 244000046052 Phaseolus vulgaris Species 0.000 description 1
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108030003943 Protein-disulfide reductases Proteins 0.000 description 1
- 241000235403 Rhizomucor miehei Species 0.000 description 1
- 101000968489 Rhizomucor miehei Lipase Proteins 0.000 description 1
- 101710184528 Scaffolding protein Proteins 0.000 description 1
- 241000235346 Schizosaccharomyces Species 0.000 description 1
- 101100153788 Schizosaccharomyces pombe (strain 972 / ATCC 24843) tpx1 gene Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241000187432 Streptomyces coelicolor Species 0.000 description 1
- 241000187398 Streptomyces lividans Species 0.000 description 1
- 101150048440 TSA1 gene Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 101100157012 Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) xynB gene Proteins 0.000 description 1
- 101100002024 Thermus aquaticus pstI gene Proteins 0.000 description 1
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
- 108010048241 acetamidase Proteins 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 101150069003 amdS gene Proteins 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 101150008194 argB gene Proteins 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 229940054340 bacillus coagulans Drugs 0.000 description 1
- 230000010310 bacterial transformation Effects 0.000 description 1
- 108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- 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 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000007796 conventional method 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
- 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 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
- 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 1
- 101150005799 dagA gene Proteins 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 150000004662 dithiols Chemical class 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 230000008571 general function Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 235000020191 long-life milk Nutrition 0.000 description 1
- 101150039489 lysZ gene Proteins 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 125000000896 monocarboxylic acid group Chemical group 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 101150095344 niaD gene Proteins 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 230000004792 oxidative damage Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000006072 paste Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- RGCLLPNLLBQHPF-HJWRWDBZSA-N phosphamidon Chemical compound CCN(CC)C(=O)C(\Cl)=C(/C)OP(=O)(OC)OC RGCLLPNLLBQHPF-HJWRWDBZSA-N 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 101150110790 xylB gene Proteins 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 239000007206 ypm medium Substances 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
- D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
-
- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT OF FLOUR OR DOUGH FOR BAKING, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS
- A21D8/00—Methods for preparing or baking dough
- A21D8/02—Methods for preparing dough; Treating dough prior to baking
- A21D8/04—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes
- A21D8/042—Methods for preparing dough; Treating dough prior to baking treating dough with microorganisms or enzymes with enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K10/00—Animal feeding-stuffs
- A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
- A23K10/14—Pretreatment of feeding-stuffs with enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/06—Enzymes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/66—Enzymes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q5/00—Preparations for care of the hair
-
- 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
- C12N9/90—Isomerases (5.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y503/00—Intramolecular oxidoreductases (5.3)
- C12Y503/04—Intramolecular oxidoreductases (5.3) transposing S-S bonds (5.3.4)
- C12Y503/04001—Protein disulfide-isomerase (5.3.4.1), i.e. disufide bond-forming enzyme
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Polymers & Plastics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Food Science & Technology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Molecular Biology (AREA)
- Public Health (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Medicinal Chemistry (AREA)
- Textile Engineering (AREA)
- General Chemical & Material Sciences (AREA)
- Physiology (AREA)
- Animal Husbandry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nutrition Science (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK0768/93 | 1993-06-28 | ||
| DK93768A DK76893D0 (enExample) | 1993-06-28 | 1993-06-28 | |
| PCT/DK1994/000266 WO1995000636A1 (en) | 1993-06-28 | 1994-06-28 | A fungal protein disulfide isomerase |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH09500014A true JPH09500014A (ja) | 1997-01-07 |
Family
ID=8097335
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP7502358A Ceased JPH09500014A (ja) | 1993-06-28 | 1994-06-28 | 菌類のタンパク質ジスルフィドイソメラーゼ |
Country Status (6)
| Country | Link |
|---|---|
| US (2) | US5879664A (enExample) |
| EP (1) | EP0708825A1 (enExample) |
| JP (1) | JPH09500014A (enExample) |
| AU (1) | AU7068494A (enExample) |
| DK (1) | DK76893D0 (enExample) |
| WO (1) | WO1995000636A1 (enExample) |
Families Citing this family (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK76893D0 (enExample) * | 1993-06-28 | 1993-06-28 | Novo Nordisk As | |
| CN1158393C (zh) * | 1994-10-07 | 2004-07-21 | 诺沃奇梅兹有限公司 | 用具有胰蛋白酶作用的微生物蛋白酶酶处理生皮或表皮而将其加工成皮革的方法 |
| EP0799321A1 (en) * | 1994-12-21 | 1997-10-08 | Novo Nordisk A/S | Method for dehairing of hides or skins by means of enzymes |
| US6248872B1 (en) * | 1996-12-03 | 2001-06-19 | Heska Corporation | Parasitic nematode transglutaminase, nucleic acid molecules, and uses thereof |
| US6383774B1 (en) * | 1996-12-03 | 2002-05-07 | Heska Corporation | Parasitic nematode transglutaminase, nucleic acid molecules and uses thereof |
| SE9704494D0 (sv) | 1997-12-02 | 1997-12-02 | Hoeganaes Ab | Lubricant for metallurgical powder compositions |
| DK1525798T3 (da) | 1997-12-22 | 2012-03-05 | Novozymes As | Carbohydrat-oxidase og anvendelse deraf i bagning |
| EP1183373A1 (en) * | 1999-05-17 | 2002-03-06 | Novozymes A/S | Polypeptides with protein disulfide reducing properties |
| DE60142226D1 (de) | 2000-03-14 | 2010-07-08 | Novozymes As | Pilz transkriptionsaktivator zur verwendung in verfahren zur herstellung von polypeptiden |
| AU7235901A (en) | 2000-07-06 | 2002-01-21 | Novozymes As | Method of preparing a dough or a baked product made from a dough, with addition of lipolytic enzymes |
| EP1326497B1 (en) | 2000-10-12 | 2006-05-24 | Novozymes A/S | Preparation of baked product from dough |
| KR100414182B1 (ko) * | 2001-07-02 | 2004-01-07 | 대한민국 | 누에 배양세포로부터 분리한 프로테인 디설피드이소머레이즈를 코딩하는 ｃＤＮＡ 유전자의 염기서열 및그의 연역 아미노산 |
| DK2295556T3 (en) | 2002-01-16 | 2015-01-26 | Novozymes As | Lipolytic Enzyme Variants and Method of Preparation thereof. |
| DK1506291T3 (da) | 2002-05-21 | 2010-10-18 | Dsm Ip Assets Bv | Nye phospholipaser og anvendelser deraf |
| EP1530630A2 (en) | 2002-08-19 | 2005-05-18 | DSM IP Assets B.V. | Novel lipases and uses thereof |
| US20040203132A1 (en) * | 2003-02-28 | 2004-10-14 | Cognetix, Inc. | Conus protein disulfide isomerase |
| KR20100014954A (ko) | 2007-03-09 | 2010-02-11 | 다니스코 유에스 인크. | 호알칼리성 바실러스 종 α-아밀라아제 변이체, α-아밀라아제 변이체를 함유하는 조성물 및 사용 방법 |
| CN101657537B (zh) | 2007-03-14 | 2013-06-19 | 丹尼斯科美国公司 | 里氏木霉α-淀粉酶增强玉米淀粉的糖化 |
| CN101918545A (zh) | 2008-01-02 | 2010-12-15 | 丹尼斯科美国公司 | 应用嗜糖假单胞菌g4-淀粉酶和其变体获得乙醇的无葡糖淀粉酶的方法 |
| WO2009109602A1 (en) * | 2008-03-04 | 2009-09-11 | Danisco A/S | Improving enzymatic treatment of a proteinaceous substrate by enzymatic removal of free thiols |
| EP2103219A1 (en) | 2008-03-10 | 2009-09-23 | Novozymes A/S | Dough with fructan and fructan-degrading enzyme |
| JP5560266B2 (ja) | 2008-06-06 | 2014-07-23 | ダニスコ・ユーエス・インク | バシルススブチリス（Ｂ．ｓｕｂｔｉｌｉｓ）由来アルファ‐アミラーゼを用いるデンプンからのグルコースの生産 |
| DK2291526T3 (da) | 2008-06-06 | 2014-10-06 | Danisco Us Inc | Saccharificering af enzymsammensætning med bacillus subtilis alpha-amylase |
| MX364987B (es) | 2008-06-06 | 2019-05-17 | Danisco Us Inc | Alfa-amilasas variantes de bacillus subtilis y metodos de uso de las mismas. |
| FR2933773B1 (fr) * | 2008-07-10 | 2013-02-15 | Biomerieux Sa | Procede de dosage de la proteine disulfide isomerase pour le diagnostic in vitro du cancer colorectal |
| WO2010102976A1 (en) | 2009-03-10 | 2010-09-16 | Dsm Ip Assets B.V. | Pregastric esterase and derivatives thereof |
| EP2432875B1 (en) | 2009-05-19 | 2016-09-07 | DuPont Nutrition Biosciences ApS | Amylase polypeptides |
| EA201200408A1 (ru) | 2009-09-03 | 2012-09-28 | ДСМ АйПи АССЕТС Б. В. | Ферментная композиция для выпечки в качестве замены ssl |
| DE102009051013A1 (de) | 2009-10-28 | 2011-06-09 | Ab Enzymes Gmbh | Klonierung, Expression und Verwendung saurer Phospholipasen |
| EP2486799A1 (en) | 2011-02-14 | 2012-08-15 | DSM IP Assets B.V. | Method to produce cake with lipolytic enzyme and alpha-amylase |
| EP3246404B1 (en) | 2011-10-28 | 2019-02-27 | Danisco US Inc. | Variant maltohexaose-forming alpha-amylase variants |
| ES2546630T3 (es) | 2012-01-30 | 2015-09-25 | Dsm Ip Assets B.V. | Alfa-amilasa |
| MX2014013402A (es) | 2012-05-11 | 2014-11-26 | Danisco Inc | Uso de alfa-amilasa de aspergillus clavatus para sacarificacion. |
| ES2909509T3 (es) | 2012-06-08 | 2022-05-06 | Danisco Us Inc | Variante de alfa-amilasas con mayor actividad en polímeros de almidón |
| AR092112A1 (es) | 2012-08-16 | 2015-03-25 | Danisco Us Inc | METODO DE USAR a-AMILASA DE ASPERGILLUS CLAVATUS Y PULULANASA PARA LA SACARIFICACION |
| EP2922951B1 (en) | 2012-11-20 | 2017-08-23 | Danisco US Inc. | Amylase with maltogenic properties |
| WO2014092960A1 (en) | 2012-12-11 | 2014-06-19 | Danisco Us Inc. | Trichoderma reesei host cells expressing a glucoamylase from aspergillus fumigatus and methods of use thereof |
| CA2894513A1 (en) | 2012-12-14 | 2014-06-19 | Danisco Us Inc. | Method of using alpha-amylase from aspergillus fumigatus and isoamylase for saccharification |
| EP2904105A1 (en) | 2012-12-20 | 2015-08-12 | Danisco US Inc. | Method of using alpha-amylase from aspergillus terreus and pullulanase for saccharification |
| WO2014099525A1 (en) | 2012-12-21 | 2014-06-26 | Danisco Us Inc. | Paenibacillus curdlanolyticus amylase, and methods of use, thereof |
| US20160053243A1 (en) | 2012-12-21 | 2016-02-25 | Danisco Us Inc. | Alpha-amylase variants |
| US20160017303A1 (en) | 2013-03-11 | 2016-01-21 | Danisco Us Inc. | Alpha-amylase combinatorial variants |
| WO2014200657A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces xiamenensis |
| WO2014200658A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from promicromonospora vindobonensis |
| WO2014200656A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces umbrinus |
| EP3011020A1 (en) | 2013-06-17 | 2016-04-27 | Danisco US Inc. | Alpha-amylase from bacillaceae family member |
| EP3052622B1 (en) | 2013-10-03 | 2018-09-19 | Danisco US Inc. | Alpha-amylases from a subset of exiguobacterium, and methods of use, thereof |
| US20160160199A1 (en) | 2013-10-03 | 2016-06-09 | Danisco Us Inc. | Alpha-amylases from exiguobacterium, and methods of use, thereof |
| EP3071691B1 (en) | 2013-11-20 | 2019-10-23 | Danisco US Inc. | Variant alpha-amylases having reduced susceptibility to protease cleavage, and methods of use, thereof |
| WO2015094809A1 (en) | 2013-12-19 | 2015-06-25 | Danisco Us Inc. | Chimeric fungal alpha-amylases comprising carbohydrate binding module and the use thereof |
| WO2017050652A1 (en) | 2015-09-25 | 2017-03-30 | Dsm Ip Assets B.V. | Asparaginase |
| DK3387124T3 (da) | 2015-12-09 | 2021-08-23 | William Cuevas | Kombinatoriske alfa-amylasevarianter |
| WO2017173324A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
| WO2017173190A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
| MX2019007375A (es) | 2016-12-21 | 2019-09-18 | Dsm Ip Assets Bv | Variante de enzima lipolitica. |
| WO2018114938A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| WO2018114912A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| US10918113B2 (en) | 2016-12-21 | 2021-02-16 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| EP3809852A1 (en) | 2018-06-19 | 2021-04-28 | DSM IP Assets B.V. | Lipolytic enzyme variants |
| US20250034609A1 (en) | 2021-11-18 | 2025-01-30 | Danisco Us Inc. | High performance alpha-amylases for starch liquefaction |
| WO2023222614A1 (en) | 2022-05-16 | 2023-11-23 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| EP4547024A1 (en) | 2022-06-29 | 2025-05-07 | DSM IP Assets B.V. | Use of peptidylarginine deiminase to obtain an improved baked good |
| WO2025012325A1 (en) | 2023-07-11 | 2025-01-16 | Dsm Ip Assets B.V. | Protein arginine deiminase |
| WO2025132821A1 (en) | 2023-12-19 | 2025-06-26 | Firmenich Sa | Comestible products having high fiber and low sugar |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8626356D0 (en) * | 1986-11-04 | 1986-12-03 | Reading University Of | Treatment of hair |
| GB8626357D0 (en) * | 1986-11-04 | 1986-12-03 | Reading University Of | Treatment of wool textiles |
| WO1988005816A1 (fr) * | 1987-01-28 | 1988-08-11 | Takeda Chemical Industries, Ltd. | Polypeptide |
| IL86455A0 (en) * | 1987-06-01 | 1988-11-15 | Takeda Chemical Industries Ltd | Polypeptide and production thereof |
| US4894340A (en) * | 1987-12-21 | 1990-01-16 | Suomen Sokeri Oy | Microbial sulfhydryl oxidase and method |
| US5496719A (en) * | 1992-05-27 | 1996-03-05 | Kabushiki Kaisha Toyota Chuo Kenkyusho | Polypeptide from Humicola insolens possessing protein disulfide isomerase activity gene encoding the same |
| US6291205B1 (en) * | 1992-06-12 | 2001-09-18 | Merck & Co., Inc. | Method of increasing production of disulfide bonded recombinant proteins by saccharomyces cerevisiae |
| DK76893D0 (enExample) * | 1993-06-28 | 1993-06-28 | Novo Nordisk As |
-
1993
- 1993-06-28 DK DK93768A patent/DK76893D0/da not_active Application Discontinuation
-
1994
- 1994-06-28 JP JP7502358A patent/JPH09500014A/ja not_active Ceased
- 1994-06-28 AU AU70684/94A patent/AU7068494A/en not_active Abandoned
- 1994-06-28 WO PCT/DK1994/000266 patent/WO1995000636A1/en not_active Ceased
- 1994-06-28 EP EP94919570A patent/EP0708825A1/en not_active Withdrawn
- 1994-06-28 US US08/557,122 patent/US5879664A/en not_active Expired - Fee Related
-
1999
- 1999-03-04 US US09/262,666 patent/US6346244B1/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| WO1995000636A1 (en) | 1995-01-05 |
| US6346244B1 (en) | 2002-02-12 |
| AU7068494A (en) | 1995-01-17 |
| US5879664A (en) | 1999-03-09 |
| EP0708825A1 (en) | 1996-05-01 |
| DK76893D0 (enExample) | 1993-06-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5879664A (en) | Fungal protein disulfide isomerase | |
| AU682028B2 (en) | An alpha-galactosidase enzyme | |
| CA2209617C (en) | Animal feed additives comprising xylanase | |
| US5879921A (en) | Recombinant expression of a glucose oxidase from a cladosporium strain | |
| EP0871712A1 (en) | Transglutaminases from oomycetes | |
| US5834280A (en) | Glucose oxidases obtained from a cladosporium | |
| EP0804558B1 (en) | Tripeptidyl aminopeptidase | |
| JP4267696B2 (ja) | ガラクタナーゼ活性を有する酵素 | |
| US5681715A (en) | Process for preparing lipases | |
| CN112410322A (zh) | 一种地衣芽孢杆菌β-甘露聚糖酶突变体及应用 | |
| US6602700B1 (en) | Phenolic acid esterases, coding sequences and methods | |
| CZ304969B6 (cs) | Způsob přípravy rekombinantní proteinázy K, vektor obsahující DNA kódující zymogenní prekurzor proteinázy K a kvasinková hostitelská buňka transformovaná tímto vektorem | |
| Ui et al. | Sequence analysis of the gene for and characterization of D-acetoin forming meso-2, 3-butanediol dehydrogenase of Klebsiella pneumoniae expressed in Escherichia coli | |
| EP1183373A1 (en) | Polypeptides with protein disulfide reducing properties | |
| WO1995001425A1 (en) | Compositions comprising protein disulfide redox agents | |
| CN108251401A (zh) | 脂肪酶及其应用 | |
| Kainuma et al. | Purification and characterization of protein disulfide isomerase from soybean | |
| CN112877306B (zh) | 一种超耐热葡萄糖氧化酶AtGOD及其基因和应用 | |
| FR2786784A1 (fr) | FRAGMENT D'ADN CODANT POUR LA XYLANASE THERMOSTABLE XynA DE THERMOASCUS | |
| CN101084306B (zh) | 过量表达和纯化的无花果曲霉氧化酶及其编码核酸 | |
| AU695995C (en) | Transglutaminases from oomycetes | |
| Matsumoto et al. | High-level production of recombinant glutamic acid-specific protease from Bacilllus licheniformis in Bacillus subtilis expression system | |
| JPH10327886A (ja) | コムギ種子に由来するシステインプロテイナーゼをコードするｄｎａ、該ｄｎａを含む形質転換大腸菌、及び該菌から発現する組換えシステインプロテイナーゼ | |
| CN106666177A (zh) | 一种含有耐高温木聚糖酶的动物饲料及其应用 | |
| JP2002186483A (ja) | リパーゼ遺伝子 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A313 | Final decision of rejection without a dissenting response from the applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A313 Effective date: 20031224 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20040120 |