CN109136114A - 在丝状真菌宿主细胞中产生多种重组多肽的方法 - Google Patents
在丝状真菌宿主细胞中产生多种重组多肽的方法 Download PDFInfo
- Publication number
- CN109136114A CN109136114A CN201810953356.5A CN201810953356A CN109136114A CN 109136114 A CN109136114 A CN 109136114A CN 201810953356 A CN201810953356 A CN 201810953356A CN 109136114 A CN109136114 A CN 109136114A
- Authority
- CN
- China
- Prior art keywords
- cellobiohydrolase
- homologous
- seq
- sequence
- gene
- 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.)
- Pending
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 457
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 448
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 433
- 230000002538 fungal effect Effects 0.000 title claims abstract description 86
- 238000000034 method Methods 0.000 title claims abstract description 84
- 108090000623 proteins and genes Proteins 0.000 claims description 202
- 108010008885 Cellulose 1,4-beta-Cellobiosidase Proteins 0.000 claims description 189
- 108091033319 polynucleotide Proteins 0.000 claims description 169
- 102000040430 polynucleotide Human genes 0.000 claims description 169
- 239000002157 polynucleotide Substances 0.000 claims description 169
- 102000004190 Enzymes Human genes 0.000 claims description 135
- 108090000790 Enzymes Proteins 0.000 claims description 135
- 239000002773 nucleotide Substances 0.000 claims description 80
- 239000003550 marker Substances 0.000 claims description 79
- 125000003729 nucleotide group Chemical group 0.000 claims description 79
- 238000003780 insertion Methods 0.000 claims description 52
- 230000037431 insertion Effects 0.000 claims description 52
- 230000010354 integration Effects 0.000 claims description 52
- 150000001413 amino acids Chemical class 0.000 claims description 45
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 38
- 230000007062 hydrolysis Effects 0.000 claims description 36
- 238000006460 hydrolysis reaction Methods 0.000 claims description 36
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 35
- 238000009396 hybridization Methods 0.000 claims description 32
- 230000000295 complement effect Effects 0.000 claims description 31
- 239000000835 fiber Substances 0.000 claims description 27
- GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose 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)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 claims description 23
- 230000035800 maturation Effects 0.000 claims description 13
- 229910001868 water Inorganic materials 0.000 claims description 12
- 238000002744 homologous recombination Methods 0.000 claims description 11
- 230000006801 homologous recombination Effects 0.000 claims description 11
- 230000009286 beneficial effect Effects 0.000 claims description 6
- 238000004064 recycling Methods 0.000 claims 2
- 241000499912 Trichoderma reesei Species 0.000 description 207
- 238000006243 chemical reaction Methods 0.000 description 161
- 239000013615 primer Substances 0.000 description 152
- 229940088598 enzyme Drugs 0.000 description 123
- 230000004087 circulation Effects 0.000 description 112
- 210000004027 cell Anatomy 0.000 description 107
- 239000000499 gel Substances 0.000 description 101
- 108020004414 DNA Proteins 0.000 description 99
- 229940091771 aspergillus fumigatus Drugs 0.000 description 90
- 241001225321 Aspergillus fumigatus Species 0.000 description 89
- 239000000203 mixture Substances 0.000 description 82
- 230000002441 reversible effect Effects 0.000 description 66
- 239000013612 plasmid Substances 0.000 description 63
- 125000000188 beta-D-glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 62
- 239000000463 material Substances 0.000 description 59
- 239000000047 product Substances 0.000 description 54
- 239000000376 reactant Substances 0.000 description 54
- 239000008049 TAE buffer Substances 0.000 description 46
- HGEVZDLYZYVYHD-UHFFFAOYSA-N acetic acid;2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid Chemical compound CC(O)=O.OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O HGEVZDLYZYVYHD-UHFFFAOYSA-N 0.000 description 46
- 239000000523 sample Substances 0.000 description 46
- 108010059892 Cellulase Proteins 0.000 description 43
- 238000000246 agarose gel electrophoresis Methods 0.000 description 42
- 235000001014 amino acid Nutrition 0.000 description 40
- 239000000872 buffer Substances 0.000 description 40
- 229940024606 amino acid Drugs 0.000 description 39
- 230000029087 digestion Effects 0.000 description 39
- 230000014509 gene expression Effects 0.000 description 38
- 238000000605 extraction Methods 0.000 description 37
- 230000000694 effects Effects 0.000 description 36
- 108010076504 Protein Sorting Signals Proteins 0.000 description 35
- 239000000284 extract Substances 0.000 description 35
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 34
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 34
- 101100382641 Aspergillus aculeatus cbhB gene Proteins 0.000 description 31
- 241000223259 Trichoderma Species 0.000 description 31
- 229920002678 cellulose Polymers 0.000 description 31
- 239000001913 cellulose Substances 0.000 description 31
- 235000010980 cellulose Nutrition 0.000 description 31
- 238000000926 separation method Methods 0.000 description 31
- 238000004458 analytical method Methods 0.000 description 29
- 239000011535 reaction buffer Substances 0.000 description 29
- 239000001965 potato dextrose agar Substances 0.000 description 27
- 108091026890 Coding region Proteins 0.000 description 26
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 26
- 239000007788 liquid Substances 0.000 description 26
- -1 α-L-arabinose glycosides Chemical class 0.000 description 26
- 108010048241 acetamidase Proteins 0.000 description 25
- 239000001963 growth medium Substances 0.000 description 25
- 210000001938 protoplast Anatomy 0.000 description 25
- 102000035101 Aspartic proteases Human genes 0.000 description 24
- 108091005502 Aspartic proteases Proteins 0.000 description 24
- 101150085005 ku70 gene Proteins 0.000 description 24
- 239000000758 substrate Substances 0.000 description 24
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 23
- 101710098247 Exoglucanase 1 Proteins 0.000 description 23
- 241000223218 Fusarium Species 0.000 description 23
- 239000002253 acid Substances 0.000 description 23
- 238000011534 incubation Methods 0.000 description 23
- 230000008569 process Effects 0.000 description 23
- 241000894006 Bacteria Species 0.000 description 22
- 239000000243 solution Substances 0.000 description 22
- 241000959173 Rasamsonia emersonii Species 0.000 description 21
- 229960000723 ampicillin Drugs 0.000 description 21
- 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 21
- 101710174704 Subtilisin-like serine protease Proteins 0.000 description 20
- 239000002585 base Substances 0.000 description 20
- 229920001221 xylan Polymers 0.000 description 20
- 101710132690 Endo-1,4-beta-xylanase A Proteins 0.000 description 19
- 230000001461 cytolytic effect Effects 0.000 description 19
- 241000588724 Escherichia coli Species 0.000 description 18
- 238000010367 cloning Methods 0.000 description 18
- 101150047832 hpt gene Proteins 0.000 description 18
- 150000004823 xylans Chemical class 0.000 description 18
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 17
- 101100394813 Bacillus subtilis (strain 168) hprT gene Proteins 0.000 description 17
- 241000233866 Fungi Species 0.000 description 17
- 101100342585 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) mus-51 gene Proteins 0.000 description 17
- 101100342589 Schizosaccharomyces pombe (strain 972 / ATCC 24843) pku70 gene Proteins 0.000 description 17
- 238000002105 Southern blotting Methods 0.000 description 17
- 241000228212 Aspergillus Species 0.000 description 16
- 241000196324 Embryophyta Species 0.000 description 16
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 16
- 102000004157 Hydrolases Human genes 0.000 description 16
- 108090000604 Hydrolases Proteins 0.000 description 16
- 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 15
- 239000008367 deionised water Substances 0.000 description 15
- 229910021641 deionized water Inorganic materials 0.000 description 15
- 102000004169 proteins and genes Human genes 0.000 description 15
- 101001065065 Aspergillus awamori Feruloyl esterase A Proteins 0.000 description 14
- 241000351920 Aspergillus nidulans Species 0.000 description 14
- 229920002488 Hemicellulose Polymers 0.000 description 14
- 108091028043 Nucleic acid sequence Proteins 0.000 description 14
- 239000012634 fragment Substances 0.000 description 14
- 240000006439 Aspergillus oryzae Species 0.000 description 13
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 13
- 108010084185 Cellulases Proteins 0.000 description 13
- 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 13
- 230000001580 bacterial effect Effects 0.000 description 13
- 108010091371 endoglucanase 1 Proteins 0.000 description 13
- 239000011780 sodium chloride Substances 0.000 description 13
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 12
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 12
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 12
- DRTQHJPVMGBUCF-XVFCMESISA-N Uridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-XVFCMESISA-N 0.000 description 12
- 108010093941 acetylxylan esterase Proteins 0.000 description 12
- 108010080434 cephalosporin-C deacetylase Proteins 0.000 description 12
- 239000002299 complementary DNA Substances 0.000 description 12
- 239000013604 expression vector Substances 0.000 description 12
- 239000008103 glucose Substances 0.000 description 12
- 235000018102 proteins Nutrition 0.000 description 12
- 238000012360 testing method Methods 0.000 description 12
- 238000005406 washing Methods 0.000 description 12
- 102000005575 Cellulases Human genes 0.000 description 11
- 108090000371 Esterases Proteins 0.000 description 11
- 101710098246 Exoglucanase 2 Proteins 0.000 description 11
- 239000007983 Tris buffer Substances 0.000 description 11
- 229910021529 ammonia Inorganic materials 0.000 description 11
- 229940106157 cellulase Drugs 0.000 description 11
- 230000008859 change Effects 0.000 description 11
- 230000002708 enhancing effect Effects 0.000 description 11
- 230000002255 enzymatic effect Effects 0.000 description 11
- 108010002430 hemicellulase Proteins 0.000 description 11
- 238000002156 mixing Methods 0.000 description 11
- 239000000126 substance Substances 0.000 description 11
- 235000000346 sugar Nutrition 0.000 description 11
- 108010036927 trypsin-like serine protease Proteins 0.000 description 11
- 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 10
- 230000003321 amplification Effects 0.000 description 10
- 210000002421 cell wall Anatomy 0.000 description 10
- 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 10
- 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 10
- 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 10
- 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 10
- 238000009795 derivation Methods 0.000 description 10
- 238000001914 filtration Methods 0.000 description 10
- ODKNJVUHOIMIIZ-RRKCRQDMSA-N floxuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(F)=C1 ODKNJVUHOIMIIZ-RRKCRQDMSA-N 0.000 description 10
- 229940059442 hemicellulase Drugs 0.000 description 10
- 230000004048 modification Effects 0.000 description 10
- 238000012986 modification Methods 0.000 description 10
- 238000003199 nucleic acid amplification method Methods 0.000 description 10
- 150000007523 nucleic acids Chemical group 0.000 description 10
- 108010001682 Dextranase Proteins 0.000 description 9
- 101100166798 Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) cel3A gene Proteins 0.000 description 9
- 102000035195 Peptidases Human genes 0.000 description 9
- 108091005804 Peptidases Proteins 0.000 description 9
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 9
- 238000006555 catalytic reaction Methods 0.000 description 9
- 238000001962 electrophoresis Methods 0.000 description 9
- 238000002407 reforming Methods 0.000 description 9
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 9
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 9
- IAJILQKETJEXLJ-UHFFFAOYSA-N Galacturonsaeure Natural products O=CC(O)C(O)C(O)C(O)C(O)=O IAJILQKETJEXLJ-UHFFFAOYSA-N 0.000 description 8
- 241001480714 Humicola insolens Species 0.000 description 8
- 239000004365 Protease Substances 0.000 description 8
- 108010022999 Serine Proteases Proteins 0.000 description 8
- 108090000637 alpha-Amylases Proteins 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 8
- 239000012228 culture supernatant Substances 0.000 description 8
- 238000005520 cutting process Methods 0.000 description 8
- 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 8
- 230000000593 degrading effect Effects 0.000 description 8
- 229930182470 glycoside Natural products 0.000 description 8
- 102000039446 nucleic acids Human genes 0.000 description 8
- 108020004707 nucleic acids Proteins 0.000 description 8
- 229920001282 polysaccharide Polymers 0.000 description 8
- 239000005017 polysaccharide Substances 0.000 description 8
- 150000004804 polysaccharides Chemical class 0.000 description 8
- 235000019419 proteases Nutrition 0.000 description 8
- 239000000725 suspension Substances 0.000 description 8
- 238000013518 transcription Methods 0.000 description 8
- 230000035897 transcription Effects 0.000 description 8
- 238000011144 upstream manufacturing Methods 0.000 description 8
- 239000002023 wood Substances 0.000 description 8
- 108010013043 Acetylesterase Proteins 0.000 description 7
- 239000002028 Biomass Substances 0.000 description 7
- 108090000364 Ligases Proteins 0.000 description 7
- 102000003960 Ligases Human genes 0.000 description 7
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 7
- 108010047754 beta-Glucosidase Proteins 0.000 description 7
- 102000006995 beta-Glucosidase Human genes 0.000 description 7
- 238000006062 fragmentation reaction Methods 0.000 description 7
- 229940097043 glucuronic acid Drugs 0.000 description 7
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 7
- 239000010931 gold Substances 0.000 description 7
- 229910052737 gold Inorganic materials 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 230000035939 shock Effects 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 238000013519 translation Methods 0.000 description 7
- 230000014616 translation Effects 0.000 description 7
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- 239000004382 Amylase Substances 0.000 description 6
- 102000013142 Amylases Human genes 0.000 description 6
- 108010065511 Amylases Proteins 0.000 description 6
- 241000235349 Ascomycota Species 0.000 description 6
- 241000228245 Aspergillus niger Species 0.000 description 6
- 241000972773 Aulopiformes Species 0.000 description 6
- 230000004544 DNA amplification Effects 0.000 description 6
- 101150017040 I gene Proteins 0.000 description 6
- 108090000769 Isomerases Proteins 0.000 description 6
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical group OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 6
- 241000235403 Rhizomucor miehei Species 0.000 description 6
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 208000037065 Subacute sclerosing leukoencephalitis Diseases 0.000 description 6
- 206010042297 Subacute sclerosing panencephalitis Diseases 0.000 description 6
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 6
- IAJILQKETJEXLJ-QTBDOELSSA-N aldehydo-D-glucuronic acid Chemical compound O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C(O)=O IAJILQKETJEXLJ-QTBDOELSSA-N 0.000 description 6
- 102000004139 alpha-Amylases Human genes 0.000 description 6
- 229940024171 alpha-amylase Drugs 0.000 description 6
- 235000019418 amylase Nutrition 0.000 description 6
- DRTQHJPVMGBUCF-PSQAKQOGSA-N beta-L-uridine Natural products O[C@H]1[C@@H](O)[C@H](CO)O[C@@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-PSQAKQOGSA-N 0.000 description 6
- 244000309466 calf Species 0.000 description 6
- 229940041514 candida albicans extract Drugs 0.000 description 6
- 239000012876 carrier material Substances 0.000 description 6
- 230000001276 controlling effect Effects 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 238000013467 fragmentation Methods 0.000 description 6
- 230000002068 genetic effect Effects 0.000 description 6
- 150000002338 glycosides Chemical class 0.000 description 6
- 210000004209 hair Anatomy 0.000 description 6
- 230000008676 import Effects 0.000 description 6
- 230000000968 intestinal effect Effects 0.000 description 6
- 238000011068 loading method Methods 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 6
- 101150054232 pyrG gene Proteins 0.000 description 6
- 230000001105 regulatory effect Effects 0.000 description 6
- 108091008146 restriction endonucleases Proteins 0.000 description 6
- 235000019515 salmon Nutrition 0.000 description 6
- 239000001632 sodium acetate Substances 0.000 description 6
- 235000017281 sodium acetate Nutrition 0.000 description 6
- DRTQHJPVMGBUCF-UHFFFAOYSA-N uracil arabinoside Natural products OC1C(O)C(CO)OC1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-UHFFFAOYSA-N 0.000 description 6
- 229940045145 uridine Drugs 0.000 description 6
- 239000003643 water by type Substances 0.000 description 6
- 239000012138 yeast extract Substances 0.000 description 6
- 150000008495 β-glucosides Chemical class 0.000 description 6
- 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 5
- 229920001817 Agar Polymers 0.000 description 5
- 229920000936 Agarose Polymers 0.000 description 5
- 108010017640 Aspartic Acid Proteases Proteins 0.000 description 5
- 241000228215 Aspergillus aculeatus Species 0.000 description 5
- 101150062179 II gene Proteins 0.000 description 5
- 102000004195 Isomerases Human genes 0.000 description 5
- 229920000057 Mannan Polymers 0.000 description 5
- 241000589516 Pseudomonas Species 0.000 description 5
- 101150003725 TK gene Proteins 0.000 description 5
- 241000223258 Thermomyces lanuginosus Species 0.000 description 5
- 239000007984 Tris EDTA buffer Substances 0.000 description 5
- 240000008042 Zea mays Species 0.000 description 5
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 5
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 5
- 239000008272 agar Substances 0.000 description 5
- 108010084650 alpha-N-arabinofuranosidase Proteins 0.000 description 5
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 5
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 230000003197 catalytic effect Effects 0.000 description 5
- 235000005822 corn Nutrition 0.000 description 5
- 238000000354 decomposition reaction Methods 0.000 description 5
- 230000027832 depurination Effects 0.000 description 5
- 238000004043 dyeing Methods 0.000 description 5
- 108010091384 endoglucanase 2 Proteins 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 150000002148 esters Chemical class 0.000 description 5
- 238000000855 fermentation Methods 0.000 description 5
- 230000004151 fermentation Effects 0.000 description 5
- KSEBMYQBYZTDHS-UHFFFAOYSA-N ferulic acid Natural products COC1=CC(C=CC(O)=O)=CC=C1O KSEBMYQBYZTDHS-UHFFFAOYSA-N 0.000 description 5
- 125000003147 glycosyl group Chemical group 0.000 description 5
- 239000011159 matrix material Substances 0.000 description 5
- 108020004999 messenger RNA Proteins 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- 230000007935 neutral effect Effects 0.000 description 5
- 229920001223 polyethylene glycol Polymers 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 238000007639 printing Methods 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 239000010902 straw Substances 0.000 description 5
- 230000008685 targeting Effects 0.000 description 5
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 4
- KSEBMYQBYZTDHS-HWKANZROSA-M (E)-Ferulic acid Natural products COC1=CC(\C=C\C([O-])=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-M 0.000 description 4
- IFBHRQDFSNCLOZ-UHFFFAOYSA-N 2-(hydroxymethyl)-6-(4-nitrophenoxy)oxane-3,4,5-triol Chemical compound OC1C(O)C(O)C(CO)OC1OC1=CC=C([N+]([O-])=O)C=C1 IFBHRQDFSNCLOZ-UHFFFAOYSA-N 0.000 description 4
- 108020005065 3' Flanking Region Proteins 0.000 description 4
- 108020005029 5' Flanking Region Proteins 0.000 description 4
- DLFVBJFMPXGRIB-UHFFFAOYSA-N Acetamide Chemical compound CC(N)=O DLFVBJFMPXGRIB-UHFFFAOYSA-N 0.000 description 4
- 241001513093 Aspergillus awamori Species 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 101000672034 Bacillus sp. (strain GL1) Unsaturated glucuronyl hydrolase Proteins 0.000 description 4
- 241001362614 Crassa Species 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 108010029541 Laccase Proteins 0.000 description 4
- 102000004882 Lipase Human genes 0.000 description 4
- 108090001060 Lipase Proteins 0.000 description 4
- 239000004367 Lipase Substances 0.000 description 4
- 108010054377 Mannosidases Proteins 0.000 description 4
- 102000001696 Mannosidases Human genes 0.000 description 4
- 241000235395 Mucor Species 0.000 description 4
- 102000012479 Serine Proteases Human genes 0.000 description 4
- 241000700584 Simplexvirus Species 0.000 description 4
- 108010056079 Subtilisins Proteins 0.000 description 4
- 102000005158 Subtilisins Human genes 0.000 description 4
- 229930006000 Sucrose Natural products 0.000 description 4
- 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 4
- 241000218636 Thuja Species 0.000 description 4
- 102100036976 X-ray repair cross-complementing protein 6 Human genes 0.000 description 4
- 101710124907 X-ray repair cross-complementing protein 6 Proteins 0.000 description 4
- 108010061261 alpha-glucuronidase Proteins 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 108010089934 carbohydrase Proteins 0.000 description 4
- 150000001720 carbohydrates Chemical class 0.000 description 4
- 235000014633 carbohydrates Nutrition 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000012790 confirmation Methods 0.000 description 4
- 238000004132 cross linking Methods 0.000 description 4
- 108010092413 endoglucanase V Proteins 0.000 description 4
- 229940114124 ferulic acid Drugs 0.000 description 4
- 235000001785 ferulic acid Nutrition 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 108010025899 gelatin film Proteins 0.000 description 4
- 229920005610 lignin Polymers 0.000 description 4
- 235000019421 lipase Nutrition 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 235000015097 nutrients Nutrition 0.000 description 4
- 230000008488 polyadenylation Effects 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 230000006798 recombination Effects 0.000 description 4
- 238000005215 recombination Methods 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 238000009938 salting Methods 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 239000010907 stover Substances 0.000 description 4
- KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 4
- 239000005720 sucrose Substances 0.000 description 4
- 229910021654 trace metal Inorganic materials 0.000 description 4
- QURCVMIEKCOAJU-UHFFFAOYSA-N trans-isoferulic acid Natural products COC1=CC=C(C=CC(O)=O)C=C1O QURCVMIEKCOAJU-UHFFFAOYSA-N 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 3
- 229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 3
- 108010037870 Anthranilate Synthase Proteins 0.000 description 3
- 101000757144 Aspergillus niger Glucoamylase Proteins 0.000 description 3
- 241000221198 Basidiomycota Species 0.000 description 3
- 229920000018 Callose Polymers 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 3
- 241000146399 Ceriporiopsis Species 0.000 description 3
- 241001248634 Chaetomium thermophilum Species 0.000 description 3
- 108010022172 Chitinases Proteins 0.000 description 3
- 102000012286 Chitinases Human genes 0.000 description 3
- 241000123346 Chrysosporium Species 0.000 description 3
- 235000005979 Citrus limon Nutrition 0.000 description 3
- 244000131522 Citrus pyriformis Species 0.000 description 3
- 241000195493 Cryptophyta Species 0.000 description 3
- 108010025880 Cyclomaltodextrin glucanotransferase Proteins 0.000 description 3
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 3
- 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 3
- 241000223221 Fusarium oxysporum Species 0.000 description 3
- 241000221779 Fusarium sambucinum Species 0.000 description 3
- 229920001503 Glucan Polymers 0.000 description 3
- 102100027612 Kallikrein-11 Human genes 0.000 description 3
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 3
- 240000007594 Oryza sativa Species 0.000 description 3
- 235000007164 Oryza sativa Nutrition 0.000 description 3
- 241000228143 Penicillium Species 0.000 description 3
- 102000003992 Peroxidases Human genes 0.000 description 3
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 3
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 3
- 108091000080 Phosphotransferase Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 108020005091 Replication Origin Proteins 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 241001494489 Thielavia Species 0.000 description 3
- 102000006601 Thymidine Kinase Human genes 0.000 description 3
- 108020004440 Thymidine kinase Proteins 0.000 description 3
- 102000004357 Transferases Human genes 0.000 description 3
- 108090000992 Transferases Proteins 0.000 description 3
- 229920002000 Xyloglucan Polymers 0.000 description 3
- 150000001412 amines Chemical class 0.000 description 3
- 235000012538 ammonium bicarbonate Nutrition 0.000 description 3
- 239000001099 ammonium carbonate Substances 0.000 description 3
- 235000003704 aspartic acid Nutrition 0.000 description 3
- 229960005261 aspartic acid Drugs 0.000 description 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 3
- 239000001110 calcium chloride Substances 0.000 description 3
- 229910001628 calcium chloride Inorganic materials 0.000 description 3
- 230000001925 catabolic effect Effects 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 235000013339 cereals Nutrition 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 239000011248 coating agent Substances 0.000 description 3
- 238000000576 coating method Methods 0.000 description 3
- 230000009514 concussion Effects 0.000 description 3
- 235000009508 confectionery Nutrition 0.000 description 3
- 239000003431 cross linking reagent Substances 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 3
- 239000000975 dye Substances 0.000 description 3
- 229910052564 epsomite Inorganic materials 0.000 description 3
- 235000019253 formic acid Nutrition 0.000 description 3
- 238000007710 freezing Methods 0.000 description 3
- 230000008014 freezing Effects 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 229930182478 glucoside Natural products 0.000 description 3
- 150000008131 glucosides Chemical class 0.000 description 3
- 239000010977 jade Substances 0.000 description 3
- SQQMAOCOWKFBNP-UHFFFAOYSA-L manganese(II) sulfate Chemical compound [Mn+2].[O-]S([O-])(=O)=O SQQMAOCOWKFBNP-UHFFFAOYSA-L 0.000 description 3
- 229910000357 manganese(II) sulfate Inorganic materials 0.000 description 3
- 108040007629 peroxidase activity proteins Proteins 0.000 description 3
- 102000020233 phosphotransferase Human genes 0.000 description 3
- 229920003023 plastic Polymers 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 238000003259 recombinant expression Methods 0.000 description 3
- 235000009566 rice Nutrition 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 230000001954 sterilising effect Effects 0.000 description 3
- 238000004659 sterilization and disinfection Methods 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 239000012137 tryptone Substances 0.000 description 3
- TWNIBLMWSKIRAT-RWOPYEJCSA-N (1r,2s,3s,4s,5r)-6,8-dioxabicyclo[3.2.1]octane-2,3,4-triol Chemical compound O1[C@@]2([H])OC[C@]1([H])[C@@H](O)[C@H](O)[C@@H]2O TWNIBLMWSKIRAT-RWOPYEJCSA-N 0.000 description 2
- FJKROLUGYXJWQN-UHFFFAOYSA-N 4-hydroxybenzoic acid Chemical compound OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 2
- BTJIUGUIPKRLHP-UHFFFAOYSA-N 4-nitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-N 0.000 description 2
- 108010011619 6-Phytase Proteins 0.000 description 2
- 241001019659 Acremonium <Plectosphaerellaceae> Species 0.000 description 2
- 108700023418 Amidases Proteins 0.000 description 2
- 108090000915 Aminopeptidases Proteins 0.000 description 2
- 102000004400 Aminopeptidases Human genes 0.000 description 2
- 108700042778 Antimicrobial Peptides Proteins 0.000 description 2
- 102000044503 Antimicrobial Peptides Human genes 0.000 description 2
- 241000228193 Aspergillus clavatus Species 0.000 description 2
- 241001480052 Aspergillus japonicus Species 0.000 description 2
- 101000690713 Aspergillus niger Alpha-glucosidase Proteins 0.000 description 2
- 101000756530 Aspergillus niger Endo-1,4-beta-xylanase B Proteins 0.000 description 2
- 101900318521 Aspergillus oryzae Triosephosphate isomerase Proteins 0.000 description 2
- 241001465318 Aspergillus terreus Species 0.000 description 2
- 241000194108 Bacillus licheniformis Species 0.000 description 2
- 102100032487 Beta-mannosidase Human genes 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 2
- 108010006303 Carboxypeptidases Proteins 0.000 description 2
- 102000005367 Carboxypeptidases Human genes 0.000 description 2
- 102000016938 Catalase Human genes 0.000 description 2
- 108010053835 Catalase Proteins 0.000 description 2
- 108010031396 Catechol oxidase Proteins 0.000 description 2
- 102000030523 Catechol oxidase Human genes 0.000 description 2
- 241001515917 Chaetomium globosum Species 0.000 description 2
- 241000675108 Citrus tangerina Species 0.000 description 2
- 241000222511 Coprinus Species 0.000 description 2
- 244000251987 Coprinus macrorhizus Species 0.000 description 2
- 235000001673 Coprinus macrorhizus Nutrition 0.000 description 2
- 241000222356 Coriolus Species 0.000 description 2
- 241001337994 Cryptococcus <scale insect> Species 0.000 description 2
- 238000001712 DNA sequencing Methods 0.000 description 2
- 108010053770 Deoxyribonucleases Proteins 0.000 description 2
- 102000016911 Deoxyribonucleases Human genes 0.000 description 2
- AHCYMLUZIRLXAA-SHYZEUOFSA-N Deoxyuridine 5'-triphosphate Chemical compound O1[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C[C@@H]1N1C(=O)NC(=O)C=C1 AHCYMLUZIRLXAA-SHYZEUOFSA-N 0.000 description 2
- 108010014258 Elastin Proteins 0.000 description 2
- 102100033167 Elastin Human genes 0.000 description 2
- 241000588698 Erwinia Species 0.000 description 2
- 241000567163 Fusarium cerealis Species 0.000 description 2
- 241000223195 Fusarium graminearum Species 0.000 description 2
- 241000146406 Fusarium heterosporum Species 0.000 description 2
- 241000567178 Fusarium venenatum Species 0.000 description 2
- 108010093031 Galactosidases Proteins 0.000 description 2
- 102000002464 Galactosidases Human genes 0.000 description 2
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 2
- 108010015776 Glucose oxidase Proteins 0.000 description 2
- 239000004366 Glucose oxidase Substances 0.000 description 2
- 102000004366 Glucosidases Human genes 0.000 description 2
- 108010056771 Glucosidases Proteins 0.000 description 2
- 108010017544 Glucosylceramidase Proteins 0.000 description 2
- 102000004547 Glucosylceramidase Human genes 0.000 description 2
- 102000016354 Glucuronosyltransferase Human genes 0.000 description 2
- 108010092364 Glucuronosyltransferase Proteins 0.000 description 2
- 229920001706 Glucuronoxylan Polymers 0.000 description 2
- 241000223198 Humicola Species 0.000 description 2
- 101001035458 Humicola insolens Endoglucanase-5 Proteins 0.000 description 2
- 108090000856 Lyases Proteins 0.000 description 2
- 102000004317 Lyases Human genes 0.000 description 2
- 229920000168 Microcrystalline cellulose Polymers 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 241000221960 Neurospora Species 0.000 description 2
- 241000221961 Neurospora crassa Species 0.000 description 2
- QGGOCWIJGWDKHC-UHFFFAOYSA-N O4-Methyl-D-glucuronsaeure Natural products OC(=O)C(O)C(OC)C(O)C(O)C=O QGGOCWIJGWDKHC-UHFFFAOYSA-N 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 241001236817 Paecilomyces <Clavicipitaceae> Species 0.000 description 2
- 241000736122 Parastagonospora nodorum Species 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 102000002508 Peptide Elongation Factors Human genes 0.000 description 2
- 108010068204 Peptide Elongation Factors Proteins 0.000 description 2
- 241000222393 Phanerochaete chrysosporium Species 0.000 description 2
- 241000222350 Pleurotus Species 0.000 description 2
- 244000252132 Pleurotus eryngii Species 0.000 description 2
- 235000001681 Pleurotus eryngii Nutrition 0.000 description 2
- 229920001131 Pulp (paper) Polymers 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 241000222480 Schizophyllum Species 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 101100370749 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) trpC1 gene Proteins 0.000 description 2
- 241000187391 Streptomyces hygroscopicus Species 0.000 description 2
- 101710172711 Structural protein Proteins 0.000 description 2
- 101710135785 Subtilisin-like protease Proteins 0.000 description 2
- 102000004523 Sulfate Adenylyltransferase Human genes 0.000 description 2
- 108010022348 Sulfate adenylyltransferase Proteins 0.000 description 2
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 2
- 239000005864 Sulphur Substances 0.000 description 2
- 241000228341 Talaromyces Species 0.000 description 2
- 241001540751 Talaromyces ruber Species 0.000 description 2
- 241000228178 Thermoascus Species 0.000 description 2
- 241001149964 Tolypocladium Species 0.000 description 2
- 241000222354 Trametes Species 0.000 description 2
- 241000222355 Trametes versicolor Species 0.000 description 2
- 108091023040 Transcription factor Proteins 0.000 description 2
- 102000040945 Transcription factor Human genes 0.000 description 2
- 108060008539 Transglutaminase Proteins 0.000 description 2
- 241000223260 Trichoderma harzianum Species 0.000 description 2
- 241000223261 Trichoderma viride Species 0.000 description 2
- 101710152431 Trypsin-like protease Proteins 0.000 description 2
- 102000003425 Tyrosinase Human genes 0.000 description 2
- 108060008724 Tyrosinase Proteins 0.000 description 2
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 2
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- OUUUKJBTGQKJLX-UHFFFAOYSA-N acetic acid (4-nitrophenyl) acetate Chemical compound CC(O)=O.CC(=O)OC1=CC=C([N+]([O-])=O)C=C1 OUUUKJBTGQKJLX-UHFFFAOYSA-N 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- PYMYPHUHKUWMLA-VPENINKCSA-N aldehydo-D-xylose Chemical group OC[C@@H](O)[C@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-VPENINKCSA-N 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- AEMOLEFTQBMNLQ-WAXACMCWSA-N alpha-D-glucuronic acid Chemical compound O[C@H]1O[C@H](C(O)=O)[C@@H](O)[C@H](O)[C@H]1O AEMOLEFTQBMNLQ-WAXACMCWSA-N 0.000 description 2
- 102000005840 alpha-Galactosidase Human genes 0.000 description 2
- 108010030291 alpha-Galactosidase Proteins 0.000 description 2
- 102000005922 amidase Human genes 0.000 description 2
- RWZYAGGXGHYGMB-UHFFFAOYSA-N anthranilic acid Chemical compound NC1=CC=CC=C1C(O)=O RWZYAGGXGHYGMB-UHFFFAOYSA-N 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 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
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 2
- 102000005936 beta-Galactosidase Human genes 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 108010055059 beta-Mannosidase Proteins 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 238000009835 boiling Methods 0.000 description 2
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 2
- 239000003054 catalyst Substances 0.000 description 2
- 229910052927 chalcanthite Inorganic materials 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- 229960005091 chloramphenicol Drugs 0.000 description 2
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 235000019504 cigarettes Nutrition 0.000 description 2
- 108010005400 cutinase Proteins 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 239000005547 deoxyribonucleotide Substances 0.000 description 2
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 235000013399 edible fruits Nutrition 0.000 description 2
- 230000005611 electricity Effects 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 239000002657 fibrous material Substances 0.000 description 2
- 238000012239 gene modification Methods 0.000 description 2
- 229940116332 glucose oxidase Drugs 0.000 description 2
- 235000019420 glucose oxidase Nutrition 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 238000003306 harvesting Methods 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 101150029559 hph gene Proteins 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 238000011081 inoculation Methods 0.000 description 2
- 239000001573 invertase Substances 0.000 description 2
- 235000011073 invertase Nutrition 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical class O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 2
- 238000007422 luminescence assay Methods 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L magnesium chloride Substances [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 229910001629 magnesium chloride Inorganic materials 0.000 description 2
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 235000019813 microcrystalline cellulose Nutrition 0.000 description 2
- 239000008108 microcrystalline cellulose Substances 0.000 description 2
- 229940016286 microcrystalline cellulose Drugs 0.000 description 2
- 239000004570 mortar (masonry) Substances 0.000 description 2
- 239000010813 municipal solid waste Substances 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 231100000219 mutagenic Toxicity 0.000 description 2
- 230000003505 mutagenic effect Effects 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 239000002858 neurotransmitter agent Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 229920002114 octoxynol-9 Polymers 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 230000001590 oxidative effect Effects 0.000 description 2
- 239000010893 paper waste Substances 0.000 description 2
- 239000001814 pectin Substances 0.000 description 2
- 229920001277 pectin Polymers 0.000 description 2
- 235000010987 pectin Nutrition 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 238000000955 peptide mass fingerprinting Methods 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 108010082527 phosphinothricin N-acetyltransferase Proteins 0.000 description 2
- 229940085127 phytase Drugs 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- 239000003910 polypeptide antibiotic agent Substances 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 238000010791 quenching Methods 0.000 description 2
- 230000000171 quenching effect Effects 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 230000008439 repair process Effects 0.000 description 2
- 230000003252 repetitive effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000012723 sample buffer Substances 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000001488 sodium phosphate Substances 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- 239000012064 sodium phosphate buffer Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 229960000268 spectinomycin Drugs 0.000 description 2
- UNFWWIHTNXNPBV-WXKVUWSESA-N spectinomycin Chemical compound O([C@@H]1[C@@H](NC)[C@@H](O)[C@H]([C@@H]([C@H]1O1)O)NC)[C@]2(O)[C@H]1O[C@H](C)CC2=O UNFWWIHTNXNPBV-WXKVUWSESA-N 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 125000001424 substituent group Chemical group 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 230000009182 swimming Effects 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000004885 tandem mass spectrometry Methods 0.000 description 2
- OFVLGDICTFRJMM-WESIUVDSSA-N tetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O OFVLGDICTFRJMM-WESIUVDSSA-N 0.000 description 2
- 229930101283 tetracycline Natural products 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000012549 training Methods 0.000 description 2
- 102000003601 transglutaminase Human genes 0.000 description 2
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 2
- 101150016309 trpC gene Proteins 0.000 description 2
- 229960005356 urokinase Drugs 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 210000002268 wool Anatomy 0.000 description 2
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 2
- 229910000368 zinc sulfate Inorganic materials 0.000 description 2
- 239000011686 zinc sulphate Substances 0.000 description 2
- DWNBOPVKNPVNQG-LURJTMIESA-N (2s)-4-hydroxy-2-(propylamino)butanoic acid Chemical compound CCCN[C@H](C(O)=O)CCO DWNBOPVKNPVNQG-LURJTMIESA-N 0.000 description 1
- FYGDTMLNYKFZSV-WFYNLLPOSA-N (2s,3r,4s,5s,6r)-2-[(2r,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,3s,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1[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-WFYNLLPOSA-N 0.000 description 1
- QGGOCWIJGWDKHC-FSIIMWSLSA-N (2s,3s,4r,5r)-2,4,5-trihydroxy-3-methoxy-6-oxohexanoic acid Chemical compound OC(=O)[C@@H](O)[C@@H](OC)[C@H](O)[C@@H](O)C=O QGGOCWIJGWDKHC-FSIIMWSLSA-N 0.000 description 1
- HXBYBCASAVUYKF-GVYWOMJSSA-N (4r,5s,6r,7r)-4,5,6,7,8-pentahydroxyoctane-2,3-dione Chemical compound CC(=O)C(=O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO HXBYBCASAVUYKF-GVYWOMJSSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 229940090248 4-hydroxybenzoic acid Drugs 0.000 description 1
- BTJIUGUIPKRLHP-UHFFFAOYSA-M 4-nitrophenolate Chemical compound [O-]C1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-M 0.000 description 1
- MLJYKRYCCUGBBV-YTWAJWBKSA-N 4-nitrophenyl beta-D-xyloside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)CO[C@H]1OC1=CC=C([N+]([O-])=O)C=C1 MLJYKRYCCUGBBV-YTWAJWBKSA-N 0.000 description 1
- ISAVYTVYFVQUDY-UHFFFAOYSA-N 4-tert-Octylphenol Chemical compound CC(C)(C)CC(C)(C)C1=CC=C(O)C=C1 ISAVYTVYFVQUDY-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241000220433 Albizia Species 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 101710199313 Alpha-L-arabinofuranosidase Proteins 0.000 description 1
- 241000609240 Ambelania acida Species 0.000 description 1
- 241001494508 Arundo donax Species 0.000 description 1
- 102000004580 Aspartic Acid Proteases Human genes 0.000 description 1
- 241001507865 Aspergillus fischeri Species 0.000 description 1
- 241000892910 Aspergillus foetidus Species 0.000 description 1
- 241000122821 Aspergillus kawachii Species 0.000 description 1
- 101001065063 Aspergillus niger Feruloyl esterase A Proteins 0.000 description 1
- 101001049242 Aspergillus niger Feruloyl esterase B Proteins 0.000 description 1
- 241000223651 Aureobasidium Species 0.000 description 1
- 108010023063 Bacto-peptone Proteins 0.000 description 1
- 241000209128 Bambusa Species 0.000 description 1
- 235000017166 Bambusa arundinacea Nutrition 0.000 description 1
- 235000017491 Bambusa tulda Nutrition 0.000 description 1
- 229920002498 Beta-glucan Polymers 0.000 description 1
- 101710204694 Beta-xylosidase Proteins 0.000 description 1
- 235000009113 Betula papyrifera Nutrition 0.000 description 1
- 235000009109 Betula pendula Nutrition 0.000 description 1
- 244000089654 Betula populifolia Species 0.000 description 1
- 235000010928 Betula populifolia Nutrition 0.000 description 1
- 235000002992 Betula pubescens Nutrition 0.000 description 1
- 241000222490 Bjerkandera Species 0.000 description 1
- 241000222478 Bjerkandera adusta Species 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 244000025254 Cannabis sativa Species 0.000 description 1
- 108010051152 Carboxylesterase Proteins 0.000 description 1
- 102000013392 Carboxylesterase Human genes 0.000 description 1
- 241001466517 Ceriporiopsis aneirina Species 0.000 description 1
- 241001646018 Ceriporiopsis gilvescens Species 0.000 description 1
- 241001277875 Ceriporiopsis rivulosa Species 0.000 description 1
- 241000524302 Ceriporiopsis subrufa Species 0.000 description 1
- 241001657057 Chaetomium thermophilum var. coprophilum Species 0.000 description 1
- 229920002101 Chitin Polymers 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- 241000985909 Chrysosporium keratinophilum Species 0.000 description 1
- 241001674013 Chrysosporium lucknowense Species 0.000 description 1
- 241001556045 Chrysosporium merdarium Species 0.000 description 1
- 241000080524 Chrysosporium queenslandicum Species 0.000 description 1
- 241001674001 Chrysosporium tropicum Species 0.000 description 1
- 241000355696 Chrysosporium zonatum Species 0.000 description 1
- 241000259811 Cladorrhinum foecundissimum Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 241000002306 Collariella gracilis Species 0.000 description 1
- 241001290175 Coriolopsis trogii Species 0.000 description 1
- 229920000742 Cotton Polymers 0.000 description 1
- AEMOLEFTQBMNLQ-AQKNRBDQSA-N D-glucopyranuronic acid Chemical compound OC1O[C@H](C(O)=O)[C@@H](O)[C@H](O)[C@H]1O AEMOLEFTQBMNLQ-AQKNRBDQSA-N 0.000 description 1
- 125000002682 D-glucuronoyl group Chemical group O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C(=O)* 0.000 description 1
- LXJXRIRHZLFYRP-VKHMYHEASA-N D-glyceraldehyde 3-phosphate Chemical compound O=C[C@H](O)COP(O)(O)=O LXJXRIRHZLFYRP-VKHMYHEASA-N 0.000 description 1
- 125000000824 D-ribofuranosyl group Chemical group [H]OC([H])([H])[C@@]1([H])OC([H])(*)[C@]([H])(O[H])[C@]1([H])O[H] 0.000 description 1
- 125000000333 D-xylopyranosyl group Chemical group [H]O[C@]1([H])C([H])([H])OC([H])(*)[C@]([H])(O[H])[C@@]1([H])O[H] 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 241000522215 Dipteryx odorata Species 0.000 description 1
- 108010001817 Endo-1,4-beta Xylanases Proteins 0.000 description 1
- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 244000004281 Eucalyptus maculata Species 0.000 description 1
- 241000145614 Fusarium bactridioides Species 0.000 description 1
- 241000223194 Fusarium culmorum Species 0.000 description 1
- 101000759028 Fusarium oxysporum Trypsin Proteins 0.000 description 1
- 241001112697 Fusarium reticulatum Species 0.000 description 1
- 241001014439 Fusarium sarcochroum Species 0.000 description 1
- 241000223192 Fusarium sporotrichioides Species 0.000 description 1
- 241001465753 Fusarium torulosum Species 0.000 description 1
- 101150108358 GLAA gene Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 241000146398 Gelatoporia subvermispora Species 0.000 description 1
- 206010064571 Gene mutation Diseases 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- 108010060309 Glucuronidase Proteins 0.000 description 1
- 102000053187 Glucuronidase Human genes 0.000 description 1
- 241000222684 Grifola Species 0.000 description 1
- 101100295959 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) arcB gene Proteins 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 241000223200 Humicola grisea var. thermoidea Species 0.000 description 1
- 239000004354 Hydroxyethyl cellulose Substances 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 229910021578 Iron(III) chloride Inorganic materials 0.000 description 1
- 239000007836 KH2PO4 Substances 0.000 description 1
- SRBFZHDQGSBBOR-HWQSCIPKSA-N L-arabinopyranose Chemical compound O[C@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-HWQSCIPKSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 241000218652 Larix Species 0.000 description 1
- 235000005590 Larix decidua Nutrition 0.000 description 1
- 229920002097 Lichenin Polymers 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 241001344133 Magnaporthe Species 0.000 description 1
- 102100024295 Maltase-glucoamylase Human genes 0.000 description 1
- 241001184659 Melanocarpus albomyces Species 0.000 description 1
- 229920001410 Microfiber Polymers 0.000 description 1
- 241000878006 Miscanthus sinensis Species 0.000 description 1
- 241001074116 Miscanthus x giganteus Species 0.000 description 1
- 241000226677 Myceliophthora Species 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 101800000597 N-terminal peptide Proteins 0.000 description 1
- 102400000108 N-terminal peptide Human genes 0.000 description 1
- 229920002274 Nalgene Polymers 0.000 description 1
- 241000611009 Nematalosa come Species 0.000 description 1
- 241000233892 Neocallimastix Species 0.000 description 1
- 108090000913 Nitrate Reductases Proteins 0.000 description 1
- GRYLNZFGIOXLOG-UHFFFAOYSA-N Nitric acid Chemical compound O[N+]([O-])=O GRYLNZFGIOXLOG-UHFFFAOYSA-N 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 241000233654 Oomycetes Species 0.000 description 1
- 102000007981 Ornithine carbamoyltransferase Human genes 0.000 description 1
- 101710198224 Ornithine carbamoyltransferase, mitochondrial Proteins 0.000 description 1
- 238000010222 PCR analysis Methods 0.000 description 1
- 235000005035 Panax pseudoginseng ssp. pseudoginseng Nutrition 0.000 description 1
- 240000005373 Panax quinquefolius Species 0.000 description 1
- 235000003140 Panax quinquefolius Nutrition 0.000 description 1
- 241001520808 Panicum virgatum Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 241001507683 Penicillium aurantiogriseum Species 0.000 description 1
- 241001496963 Penicillium brasilianum Species 0.000 description 1
- 241000222385 Phanerochaete Species 0.000 description 1
- 244000046052 Phaseolus vulgaris Species 0.000 description 1
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 1
- 241000222395 Phlebia Species 0.000 description 1
- 241000222397 Phlebia radiata Species 0.000 description 1
- 102100027330 Phosphoribosylaminoimidazole carboxylase Human genes 0.000 description 1
- 108090000434 Phosphoribosylaminoimidazolesuccinocarboxamide synthases Proteins 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 235000014676 Phragmites communis Nutrition 0.000 description 1
- 235000015334 Phyllostachys viridis Nutrition 0.000 description 1
- 241000351396 Picea asperata Species 0.000 description 1
- 235000008331 Pinus X rigitaeda Nutrition 0.000 description 1
- 235000011613 Pinus brutia Nutrition 0.000 description 1
- 241000018646 Pinus brutia Species 0.000 description 1
- 241000235379 Piromyces Species 0.000 description 1
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 1
- 229920001214 Polysorbate 60 Polymers 0.000 description 1
- 241000168036 Populus alba Species 0.000 description 1
- 241000183024 Populus tremula Species 0.000 description 1
- 102100038946 Proprotein convertase subtilisin/kexin type 6 Human genes 0.000 description 1
- 101710148480 Putative beta-xylosidase Proteins 0.000 description 1
- 241000220324 Pyrus Species 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 240000000111 Saccharum officinarum Species 0.000 description 1
- 235000007201 Saccharum officinarum Nutrition 0.000 description 1
- 241000124033 Salix Species 0.000 description 1
- 241000222481 Schizophyllum commune Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 101100242848 Streptomyces hygroscopicus bar gene Proteins 0.000 description 1
- 241000030538 Thecla Species 0.000 description 1
- 241000228182 Thermoascus aurantiacus Species 0.000 description 1
- 241001313536 Thermothelomyces thermophila Species 0.000 description 1
- 241001495429 Thielavia terrestris Species 0.000 description 1
- 241000222357 Trametes hirsuta Species 0.000 description 1
- 241000217816 Trametes villosa Species 0.000 description 1
- 241000378866 Trichoderma koningii Species 0.000 description 1
- 241000223262 Trichoderma longibrachiatum Species 0.000 description 1
- 241000259813 Trichophaea saccata Species 0.000 description 1
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- 235000004240 Triticum spelta Nutrition 0.000 description 1
- 241000409279 Xerochrysium dermatitidis Species 0.000 description 1
- 229920002494 Zein Polymers 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- UGXQOOQUZRUVSS-ZZXKWVIFSA-N [5-[3,5-dihydroxy-2-(1,3,4-trihydroxy-5-oxopentan-2-yl)oxyoxan-4-yl]oxy-3,4-dihydroxyoxolan-2-yl]methyl (e)-3-(4-hydroxyphenyl)prop-2-enoate Chemical compound OC1C(OC(CO)C(O)C(O)C=O)OCC(O)C1OC1C(O)C(O)C(COC(=O)\C=C\C=2C=CC(O)=CC=2)O1 UGXQOOQUZRUVSS-ZZXKWVIFSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine group Chemical group [C@@H]1([C@H](O)[C@H](O)[C@@H](CO)O1)N1C=NC=2C(N)=NC=NC12 OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 108010028144 alpha-Glucosidases Proteins 0.000 description 1
- 125000000539 amino acid group Chemical group 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
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 229920000617 arabinoxylan Polymers 0.000 description 1
- 101150008194 argB gene Proteins 0.000 description 1
- 210000001367 artery Anatomy 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 239000010905 bagasse Substances 0.000 description 1
- 101150103518 bar gene Proteins 0.000 description 1
- 238000010364 biochemical engineering Methods 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 229920003090 carboxymethyl hydroxyethyl cellulose Polymers 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 101150052795 cbh-1 gene Proteins 0.000 description 1
- 101150114858 cbh2 gene Proteins 0.000 description 1
- 230000034303 cell budding Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 229940114081 cinnamate Drugs 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000005336 cracking Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000002242 deionisation method Methods 0.000 description 1
- 238000000326 densiometry Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 239000012470 diluted sample Substances 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 238000007599 discharging Methods 0.000 description 1
- 229940009662 edetate Drugs 0.000 description 1
- 229940124274 edetate disodium Drugs 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 108010000165 exo-1,3-alpha-glucanase Proteins 0.000 description 1
- 108010038658 exo-1,4-beta-D-xylosidase Proteins 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- KSEBMYQBYZTDHS-HWKANZROSA-N ferulic acid Chemical compound COC1=CC(\C=C\C(O)=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-N 0.000 description 1
- 108010041969 feruloyl esterase Proteins 0.000 description 1
- 238000007667 floating Methods 0.000 description 1
- 238000011010 flushing procedure Methods 0.000 description 1
- 230000004907 flux Effects 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 1
- 150000008195 galaktosides Chemical class 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000030279 gene silencing Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 235000008434 ginseng Nutrition 0.000 description 1
- 229940097042 glucuronate Drugs 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- XLYOFNOQVPJJNP-ZSJDYOACSA-N heavy water Substances [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 1
- 229920000140 heteropolymer Polymers 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 229940042795 hydrazides for tuberculosis treatment Drugs 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 235000019447 hydroxyethyl cellulose Nutrition 0.000 description 1
- 108010002685 hygromycin-B kinase Proteins 0.000 description 1
- 230000000091 immunopotentiator Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- 238000009655 industrial fermentation Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- RBTARNINKXHZNM-UHFFFAOYSA-K iron trichloride Chemical compound Cl[Fe](Cl)Cl RBTARNINKXHZNM-UHFFFAOYSA-K 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 210000002429 large intestine Anatomy 0.000 description 1
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 1
- 239000012263 liquid product Substances 0.000 description 1
- 101150039489 lysZ gene Proteins 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000000155 melt Substances 0.000 description 1
- 230000037353 metabolic pathway Effects 0.000 description 1
- 239000003658 microfiber Substances 0.000 description 1
- 238000002715 modification method Methods 0.000 description 1
- QXYJCZRRLLQGCR-UHFFFAOYSA-N molybdenum(IV) oxide Inorganic materials O=[Mo]=O QXYJCZRRLLQGCR-UHFFFAOYSA-N 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- TZBAVQKIEKDGFH-UHFFFAOYSA-N n-[2-(diethylamino)ethyl]-1-benzothiophene-2-carboxamide;hydrochloride Chemical compound [Cl-].C1=CC=C2SC(C(=O)NCC[NH+](CC)CC)=CC2=C1 TZBAVQKIEKDGFH-UHFFFAOYSA-N 0.000 description 1
- VGKONPUVOVVNSU-UHFFFAOYSA-N naphthalen-1-yl acetate Chemical compound C1=CC=C2C(OC(=O)C)=CC=CC2=C1 VGKONPUVOVVNSU-UHFFFAOYSA-N 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000007857 nested PCR Methods 0.000 description 1
- 101150095344 niaD gene Proteins 0.000 description 1
- 229910017604 nitric acid Inorganic materials 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000010355 oscillation Effects 0.000 description 1
- 238000006213 oxygenation reaction Methods 0.000 description 1
- 125000000636 p-nitrophenyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1*)[N+]([O-])=O 0.000 description 1
- 239000003973 paint Substances 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- LCCNCVORNKJIRZ-UHFFFAOYSA-N parathion Chemical compound CCOP(=S)(OCC)OC1=CC=C([N+]([O-])=O)C=C1 LCCNCVORNKJIRZ-UHFFFAOYSA-N 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 235000021017 pears Nutrition 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- 150000002978 peroxides Chemical class 0.000 description 1
- 108010031697 phosphoribosylaminoimidazole synthase Proteins 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000005375 photometry Methods 0.000 description 1
- 230000029553 photosynthesis Effects 0.000 description 1
- 238000010672 photosynthesis Methods 0.000 description 1
- 210000002706 plastid Anatomy 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000033458 reproduction Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000000779 smoke Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 238000010563 solid-state fermentation Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000010183 spectrum analysis Methods 0.000 description 1
- 235000013599 spices Nutrition 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001228 trophic effect Effects 0.000 description 1
- 230000001810 trypsinlike Effects 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 125000000969 xylosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)CO1)* 0.000 description 1
- 239000005019 zein Substances 0.000 description 1
- 229940093612 zein Drugs 0.000 description 1
- JLYXXMFPNIAWKQ-UHFFFAOYSA-N γ Benzene hexachloride Chemical compound ClC1C(Cl)C(Cl)C(Cl)C(Cl)C1Cl JLYXXMFPNIAWKQ-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
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/87—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation
-
- 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)
-
- 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)
- C12Y302/01091—Cellulose 1,4-beta-cellobiosidase (3.2.1.91)
-
- 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)
- C12Y302/0115—Oligoxyloglucan reducing-end-specific cellobiohydrolase (3.2.1.150)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Mycology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161526809P | 2011-08-24 | 2011-08-24 | |
| US61/526,809 | 2011-08-24 | ||
| CN201280052277.8A CN103890180A (zh) | 2011-08-24 | 2012-08-23 | 在丝状真菌宿主细胞中产生多种重组多肽的方法 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201280052277.8A Division CN103890180A (zh) | 2011-08-24 | 2012-08-23 | 在丝状真菌宿主细胞中产生多种重组多肽的方法 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN109136114A true CN109136114A (zh) | 2019-01-04 |
Family
ID=47358264
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201810953356.5A Pending CN109136114A (zh) | 2011-08-24 | 2012-08-23 | 在丝状真菌宿主细胞中产生多种重组多肽的方法 |
| CN201280052277.8A Pending CN103890180A (zh) | 2011-08-24 | 2012-08-23 | 在丝状真菌宿主细胞中产生多种重组多肽的方法 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201280052277.8A Pending CN103890180A (zh) | 2011-08-24 | 2012-08-23 | 在丝状真菌宿主细胞中产生多种重组多肽的方法 |
Country Status (7)
| Country | Link |
|---|---|
| US (3) | US9493790B2 (enExample) |
| EP (1) | EP2748322A2 (enExample) |
| CN (2) | CN109136114A (enExample) |
| AU (1) | AU2012298799B2 (enExample) |
| BR (1) | BR112014004190A2 (enExample) |
| IN (1) | IN2014CN02136A (enExample) |
| WO (1) | WO2013028912A2 (enExample) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114561303A (zh) * | 2022-02-14 | 2022-05-31 | 大连理工大学 | 一株分泌高性能纤维素酶的里氏木霉工程菌株及其应用 |
| CN117757643A (zh) * | 2024-01-12 | 2024-03-26 | 华东理工大学 | 一种分泌表达人溶菌酶的里氏木霉工程菌及其构建方法和应用 |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BR112014004190A2 (pt) * | 2011-08-24 | 2017-03-01 | Novozymes Inc | método para construir uma cepa fúngida filamentosa, cepa fúngida filamentosa, método para produzir múltiplos polipeptídeos recombinantes, e, construto em tandem |
| US9404101B2 (en) * | 2011-08-24 | 2016-08-02 | Novozymes, Inc. | Methods for obtaining positive transformants of a filamentous fungal host cell |
| EP2800809B1 (en) | 2012-01-05 | 2018-03-07 | Glykos Finland Oy | Protease deficient filamentous fungal cells and methods of use thereof |
| US9695454B2 (en) | 2012-05-23 | 2017-07-04 | Glykos Finland Oy | Production of fucosylated glycoproteins |
| KR20160035587A (ko) | 2013-07-10 | 2016-03-31 | 노파르티스 아게 | 복수개의 프로테아제 결핍 사상형 진균 세포들 및 그의 이용방법 |
| US20150147774A1 (en) * | 2013-11-22 | 2015-05-28 | National University Of Singapore | Expression construct for yeast and a method of using the construct |
| CN115975994A (zh) * | 2014-06-06 | 2023-04-18 | 诺维信公司 | 酶组合物及其用途 |
| CN108064266A (zh) | 2014-07-21 | 2018-05-22 | 格利科斯芬兰公司 | 在丝状真菌中具有哺乳动物样n-聚糖的糖蛋白的制备 |
| EP3198001B1 (en) | 2014-09-23 | 2021-08-11 | Novozymes A/S | Processes for producing ethanol and fermenting organisms |
| US10385352B2 (en) | 2015-03-09 | 2019-08-20 | Novozymes A/S | Methods of introducing multiple expression constructs into a eukaryotic cell |
| WO2017151957A1 (en) | 2016-03-02 | 2017-09-08 | Novozymes A/S | Cellobiohydrolase variants and polynucleotides encoding same |
| WO2018093752A1 (en) * | 2016-11-15 | 2018-05-24 | Danisco Us Inc. | Filamentous fungi with improved protein production |
| WO2018106792A1 (en) | 2016-12-06 | 2018-06-14 | Novozymes A/S | Improved processes for production of ethanol from xylose-containing cellulosic substrates using engineered yeast strains |
| US11091753B2 (en) | 2017-05-31 | 2021-08-17 | Novozymes A/S | Xylose fermenting yeast strains and processes thereof for ethanol production |
| CA3064042A1 (en) | 2017-06-02 | 2018-12-06 | Novozymes A/S | Improved yeast for ethanol production |
| CN109988714B (zh) * | 2017-12-29 | 2021-12-28 | 青岛蔚蓝生物集团有限公司 | 一种里氏木霉及其应用 |
| CA3089135A1 (en) | 2018-01-29 | 2019-08-01 | Novozymes A/S | Microorganisms with improved nitrogen utilization for ethanol production |
| CA3107110A1 (en) | 2018-07-25 | 2020-01-30 | Novozymes A/S | Enzyme-expressing yeast for ethanol production |
| CA3114783A1 (en) | 2018-10-08 | 2020-04-16 | Novozymes A/S | Enzyme-expressing yeast for ethanol production |
| CN113302305A (zh) * | 2018-12-12 | 2021-08-24 | 诺维信公司 | 提高丝状真菌细胞在多肽的产生方面的生产力的方法 |
| MX2021015821A (es) | 2019-07-26 | 2022-02-03 | Novozymes As | Microorganismos con transporte de nitrogeno mejorado para la produccion de etanol. |
| CN114127124A (zh) | 2019-08-06 | 2022-03-01 | 诺维信公司 | 用于提高酶表达的融合蛋白 |
| CN110724643B (zh) * | 2019-11-18 | 2022-07-15 | 河南省农业科学院植物保护研究所 | 一株具有防病促生功能的橘灰青霉及其菌剂和应用 |
| WO2021119304A1 (en) | 2019-12-10 | 2021-06-17 | Novozymes A/S | Microorganism for improved pentose fermentation |
| EP4208559A1 (en) | 2020-09-04 | 2023-07-12 | Novozymes A/S | Improved fermenting organism for ethanol production |
| MX2023014545A (es) | 2021-06-07 | 2024-03-01 | Novozymes As | Microorganismo diseñado para mejorar la fermentación del etanol. |
| CN115651933A (zh) * | 2022-06-06 | 2023-01-31 | 福州市皮肤病防治院 | 高效精准替换红色毛癣菌基因的方法 |
| CN120344672A (zh) | 2022-09-23 | 2025-07-18 | 诺维信公司 | 用于乙醇生产的改进发酵生物 |
| WO2025088155A1 (en) | 2023-10-25 | 2025-05-01 | Novozymes A/S | Improved fermenting organism for ethanol production |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007136865A2 (en) * | 2006-05-19 | 2007-11-29 | Glycofi, Inc | Recombinant vectors |
| WO2010039889A2 (en) * | 2008-09-30 | 2010-04-08 | Novozymes, Inc. | Methods for using positively and negatively selectable genes in a filamentous fungal cell |
| CN101970651A (zh) * | 2007-05-31 | 2011-02-09 | 诺维信股份有限公司 | 用于降解纤维素材料的组合物 |
Family Cites Families (115)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FI864473A7 (fi) * | 1985-11-20 | 1987-05-21 | Panlabs Inc | Yhdistetyt ilmaisukasetit fungaalitransformaatiota varten. |
| DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| US5989870A (en) | 1986-04-30 | 1999-11-23 | Rohm Enzyme Finland Oy | Method for cloning active promoters |
| US5776757A (en) | 1988-03-24 | 1998-07-07 | Novo Nordisk A/S | Fungal cellulase composition containing alkaline CMC-endoglucanase and essentially no cellobiohydrolase and method of making thereof |
| DK115890D0 (da) | 1990-05-09 | 1990-05-09 | Novo Nordisk As | Enzym |
| DE69133352T2 (de) | 1990-10-05 | 2004-11-04 | Genencor International, Inc., Palo Alto | Methoden zur behandlung baumwolle-enthaltender fasern mit zellulase |
| US5834286A (en) * | 1992-07-31 | 1998-11-10 | Rohm Enzyme Finland Oy | Recombinant cells that express phytate degrading enzymes in desired ratios |
| DE69433499T2 (de) | 1993-03-10 | 2004-12-02 | Novozymes A/S | Enzyme mit xylanaseaktivität aus aspergillus aculeatus |
| KR970703426A (ko) | 1994-06-03 | 1997-07-03 | 제임스 쉐한 | 정제된 Myceliophthora 락카제 및 그것을 암호화 하는 핵산(PURIFIED MYCELIOPHTHORA LACCASES AND NUCLEIC ACIDS ENCODING SAME) |
| EP0777737B1 (en) | 1994-06-30 | 2005-05-04 | Novozymes Biotech, Inc. | Non-toxic, non-toxigenic, non-pathogenic fusarium expression system and promoters and terminators for use therein |
| US6060305A (en) * | 1994-06-30 | 2000-05-09 | Novo Nordisk Biotech, Inc. | Non-toxic, non-toxigenic, non-pathogenic Fusarium expression system |
| US20030044956A1 (en) | 1995-08-23 | 2003-03-06 | Short Jay M. | Enzymes having carboxymethyl cellulase activity and methods of use thereof |
| DK0877801T3 (da) | 1996-01-19 | 2005-08-29 | Novozymes Biotech Inc | Morfologiske mutanter af trådsvampe |
| WO1998011203A1 (en) * | 1996-09-13 | 1998-03-19 | Novo Nordisk Biotech, Inc. | Cells having dna insertion mutations which produce altered amounts of a polypeptide |
| US6451063B1 (en) | 1996-09-25 | 2002-09-17 | Genencor International, Inc. | Cellulase for use in industrial processes |
| US6017870A (en) | 1996-10-09 | 2000-01-25 | Genencor International, Inc. | Purified cellulase and method of producing |
| US7883872B2 (en) | 1996-10-10 | 2011-02-08 | Dyadic International (Usa), Inc. | Construction of highly efficient cellulase compositions for enzymatic hydrolysis of cellulose |
| US5811381A (en) | 1996-10-10 | 1998-09-22 | Mark A. Emalfarb | Cellulase compositions and methods of use |
| US6265204B1 (en) * | 1997-01-17 | 2001-07-24 | Genencor International, Inc. | DNA sequences, vectors, and fusion polypeptides for secretion of polypeptides in filamentous fungi |
| JP2001512024A (ja) | 1997-07-31 | 2001-08-21 | デーエスエム・ナムローゼ・フェンノートシャップ | アスペルギルスのセルロース分解酵素 |
| US5871550A (en) | 1997-08-26 | 1999-02-16 | Genencor International, Inc. | Mutant Thermonospora spp. cellulase |
| ES2267200T3 (es) | 1997-11-19 | 2007-03-01 | Genencor International, Inc. | Celulasa producida por actinomycetes y metodo para producirla. |
| CA2315017C (en) | 1997-12-16 | 2011-10-11 | Genencor International, Inc. | Novel egiii-like enzymes, dna encoding such enzymes and methods for producing such enzymes |
| ES2143408B1 (es) * | 1998-04-02 | 2000-12-01 | Urquima Sa | Promotor y construcciones para expresion de proteinas recombinantes en hongos filamentosos. |
| AU4188099A (en) * | 1998-05-15 | 1999-12-06 | Novo Nordisk A/S | Methods for producing polypeptides in filamentous fungal mutant cells |
| AU4025700A (en) | 1999-03-22 | 2000-10-09 | Novo Nordisk Biotech, Inc. | Promoters for expressing genes in a fungal cell |
| CN1509330A (zh) | 2001-05-18 | 2004-06-30 | ŵ��ø�ɷ�����˾ | 具有纤维二糖酶活性的多肽和编码其的多核苷酸 |
| US6982159B2 (en) | 2001-09-21 | 2006-01-03 | Genencor International, Inc. | Trichoderma β-glucosidase |
| US7049125B2 (en) | 2001-12-18 | 2006-05-23 | Genencor International, Inc. | EGVIII endoglucanase and nucleic acids encoding the same |
| US7045332B2 (en) | 2001-12-18 | 2006-05-16 | Genencor International, Inc. | BGL4 β-glucosidase and nucleic acids encoding the same |
| US7005289B2 (en) | 2001-12-18 | 2006-02-28 | Genencor International, Inc. | BGL5 β-glucosidase and nucleic acids encoding the same |
| US7056721B2 (en) | 2001-12-18 | 2006-06-06 | Genencor International, Inc. | EGVI endoglucanase and nucleic acids encoding the same |
| US7045331B2 (en) | 2001-12-18 | 2006-05-16 | Genencor International, Inc. | EGVII endoglucanase and nucleic acids encoding the same |
| WO2004016760A2 (en) | 2002-08-16 | 2004-02-26 | Genencor International, Inc. | Novel variant hyprocrea jecorina cbh1 cellulases |
| US7582462B2 (en) | 2002-11-07 | 2009-09-01 | Danisco Us Inc., Genencor Division | BGL6 beta-glucosidase and nucleic acids encoding the same |
| US7407788B2 (en) | 2002-11-21 | 2008-08-05 | Danisco A/S, Genencor Division | BGL7 beta-glucosidase and nucleic acids encoding the same |
| CN1898381B (zh) | 2003-03-21 | 2013-07-17 | 金克克国际有限公司 | Cbh1同源物和cbh1纤维素酶变体 |
| WO2005001065A2 (en) | 2003-04-01 | 2005-01-06 | Genencor International, Inc. | Variant humicola grisea cbh1.1 |
| WO2004099228A2 (en) | 2003-05-02 | 2004-11-18 | Novozymes Inc. | Variants of beta-glucosidases |
| EP2261326B1 (en) | 2003-05-29 | 2017-03-29 | Danisco US Inc. | Novel Trichoderma genes |
| DK1682656T3 (da) | 2003-10-28 | 2013-11-18 | Novozymes Inc | Polypeptider med beta-glucosidaseaktivitet og polynukleotider, der koder for dem |
| EP2305703B1 (en) | 2004-01-30 | 2014-03-12 | Novozymes Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| ES2389442T3 (es) | 2004-02-06 | 2012-10-26 | Novozymes Inc. | Polipéptidos con actividad de aumento celulolítica y polinucleótidos que los codifican |
| US7960160B2 (en) * | 2004-02-12 | 2011-06-14 | Novozymes, Inc. | Polypeptides having xylanase activity from Aspergillus fumigatus |
| CA2560588A1 (en) | 2004-03-25 | 2005-10-06 | Genencor International, Inc. | Cellulase fusion protein and heterologous cellulase fusion construct encoding the same |
| US8097445B2 (en) | 2004-03-25 | 2012-01-17 | Danisco Us Inc. | Exo-endo cellulase fusion protein |
| ES2554467T3 (es) | 2004-12-30 | 2015-12-21 | Danisco Us Inc. | Variantes de celulasas CBH2 de Hypocrea jecorina |
| US7220565B2 (en) | 2005-01-06 | 2007-05-22 | Novozymes, Inc. | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
| AR053066A1 (es) | 2005-04-26 | 2007-04-18 | Novozymes As | Arabinofuranosidasas |
| PT1874927E (pt) | 2005-04-29 | 2014-04-23 | Ab Enzymes Oy | Celulases melhoradas |
| EP1928901B1 (en) | 2005-08-04 | 2011-06-15 | Novozymes, Inc. | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
| WO2007089290A2 (en) | 2005-09-30 | 2007-08-09 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
| DK1969123T3 (en) | 2005-12-22 | 2017-08-28 | Ab Enzymes Oy | Hitherto UNKNOWN ENZYMS |
| FI120045B (fi) | 2005-12-22 | 2009-06-15 | Roal Oy | Selluloosamateriaalin käsittely ja siinä käyttökelpoiset entsyymit |
| US8304212B2 (en) | 2006-07-10 | 2012-11-06 | Dyadic International, Inc. | Methods and compositions for degradation of lignocellulosic material |
| GB0614442D0 (en) * | 2006-07-20 | 2006-08-30 | Fluxome Sciences As | Metabolically engineered cells for the production of pinosylvin |
| BRPI0714870A2 (pt) | 2006-07-21 | 2013-05-28 | Novozymes Inc | mÉtodo para produzir um polipeptÍdeo secretado tendo atividade biolàgica, proteÍna de fusço isolada, polinucleotÍdeo isolado, construÇço de proteÍna de fusço, vetor de expressço, cÉlula hospedeira féngica, mÉtodos para degradar ou conventer um material celulàsico e para produzir uma substÂncia |
| WO2008073914A2 (en) * | 2006-12-10 | 2008-06-19 | Dyadic International Inc. | Expression and high-throughput screening of complex expressed dna libraries in filamentous fungi |
| CN101784659B (zh) | 2007-05-31 | 2016-05-18 | 诺维信股份有限公司 | 具有纤维素分解增强活性的多肽和编码它的多核苷酸 |
| US9453213B2 (en) | 2007-05-31 | 2016-09-27 | Novozymes, Inc. | Methods of increasing the cellulolytic enhancing activity of a polypeptide |
| DK2195424T3 (en) | 2007-09-28 | 2019-01-07 | Novozymes As | Polypeptides with cellobiohydrolase II activity and polynucleotides encoding them |
| US8034996B2 (en) | 2007-09-28 | 2011-10-11 | Novozymes A/S | Polypeptides having acetylxylan esterase activity and polynucleotides encoding same |
| BRPI0820552A2 (pt) | 2007-11-27 | 2014-10-14 | Novozymes As | Polipetídeo isolado, polinucleotídeo isolado, construção de ácido nucléico, vetor de expressão recombinante, célula hospedeira recombinante, métodos para produzir o polipeptídeo, para produzir uma proteína, e para degradar ou converter um material de biomassa, planta, parte vegetal ou célula vegetal transgêncica, método, composição, e. uso do polipeptídio. |
| WO2009073383A1 (en) | 2007-11-30 | 2009-06-11 | Novozymes A/S | Polypeptides having arabinofuranosidase activity and polynucleotides encoding same |
| BRPI0820102A2 (pt) | 2007-12-05 | 2017-05-23 | Novozymes As | polipeptídeo isolado, construção de ácido nucléico, célula hospedeira recombinante, métodos de produzir o polipeptídeo, de produzir um mutante de uma célula precursora, de inibir a expressão de um polipeptídeo tendo atividade de xilanase em uma célula, de produzir uma proteína e para degradar um material cotendo xilano, célula mutante, planta transgênica, parte de planta ou célula vegetal, e, molécula de rna inibidora de filamento duplo |
| DK2224822T3 (da) | 2007-12-06 | 2014-08-25 | Novozymes As | Polypeptider med acetylxylanesterase-aktivitet og polynukleotider, der koder for disse |
| CN101939420A (zh) | 2007-12-07 | 2011-01-05 | 诺维信公司 | 具有阿魏酸酯酶活性的多肽和编码该多肽的多核苷酸 |
| CA2709485A1 (en) | 2007-12-19 | 2009-07-09 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| EP2235049A2 (en) | 2007-12-19 | 2010-10-06 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| JP2011507525A (ja) | 2007-12-19 | 2011-03-10 | ノボザイムス アクティーゼルスカブ | セルロース分解増強活性を有するポリペプチドとこれをコードするポリヌクレオチド |
| CA2709371A1 (en) | 2007-12-19 | 2009-07-09 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| WO2009106488A1 (en) * | 2008-02-25 | 2009-09-03 | Novozymes A/S | Method for increasing expression yield of a protein of interest |
| BRPI0910965A2 (pt) | 2008-04-17 | 2016-01-05 | Novozymes As | polipeptídeo isolado, polinucleotídeos isolado e mutante, construto de ácido nucleico, vetor de expressão recombinante, célula hospedeira recombinante, métodos para produzir um polinucleotídeo e para produzir um polipeptídeo, planta transgênica, parte de planta ou célula de planta, método para degradar um material, e, composição |
| CA2732122A1 (en) | 2008-07-29 | 2010-02-04 | Novozymes A/S | Polypeptides having alpha-glucuronidase activity and polynucleotides encoding same |
| US8071335B2 (en) | 2008-07-31 | 2011-12-06 | Novozymes, Inc. | Polypeptides having acetylxylan esterase activity and polynucleotides encoding same |
| WO2010039840A1 (en) | 2008-09-30 | 2010-04-08 | Novozymes, Inc. | Methods for producing polypeptides in enzyme-deficient mutants of fusarium venenatum |
| EP2356136A1 (en) | 2008-11-10 | 2011-08-17 | Novozymes Inc. | Polypeptides having feruloyl esterase activity and polynucleotides encoding same |
| US8805427B2 (en) | 2008-11-14 | 2014-08-12 | Microsoft Corporation | Channel reuse with cognitive low interference signals |
| CN102300986A (zh) | 2008-12-04 | 2011-12-28 | 诺维信股份有限公司 | 具有纤维素分解增强活性的多肽和编码该多肽的多核苷酸 |
| US8609933B2 (en) | 2008-12-04 | 2013-12-17 | Novozymes, Inc. | Polypeptides having feruloyl esterase activity and polynucleotides encoding same |
| EP2391715A1 (en) | 2009-01-28 | 2011-12-07 | Novozymes Inc. | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
| DK2411511T3 (en) | 2009-03-24 | 2018-11-26 | Novozymes As | POLYPEPTIDES WITH ACETYLXYLANESTERASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
| CN102482680B (zh) | 2009-04-30 | 2014-09-10 | 诺维信股份有限公司 | 具有木聚糖酶活性的多肽和编码该多肽的多核苷酸 |
| WO2010138754A1 (en) | 2009-05-29 | 2010-12-02 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
| CN102482652B (zh) | 2009-06-02 | 2014-12-17 | 诺维信股份有限公司 | 具有纤维二糖水解酶活性的多肽和编码该多肽的多核苷酸 |
| CA2767169A1 (en) | 2009-07-07 | 2011-01-13 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| CN106085988A (zh) | 2009-09-17 | 2016-11-09 | 诺维信股份有限公司 | 具有纤维素分解增强活性的多肽及编码其的多核苷酸 |
| CN102712916B (zh) | 2009-09-18 | 2015-11-25 | 诺维信股份有限公司 | 具有β-葡糖苷酶活性的多肽和编码该多肽的多核苷酸 |
| CN102648276A (zh) | 2009-09-29 | 2012-08-22 | 诺维信股份有限公司 | 具有木聚糖酶活性的多肽和编码该多肽的多核苷酸 |
| EP2483295B1 (en) | 2009-09-29 | 2015-11-25 | Novozymes Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| EP2483402A1 (en) | 2009-09-30 | 2012-08-08 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| BR112012007375A2 (pt) | 2009-09-30 | 2016-11-22 | Novozymes As | polipeptídeo isolado, polinucleotídeo isolado, métodos para produzir um polipeptídeo, para produzir um mutante de uma célula precursora, para inibir a expressão de um polipeptídeo, para produzir uma proteína, para degradar ou converter um material celulósico, para produzir um produto de fermentação e para fermentar um material celulósico, planta transgênica, parte de planta ou célula de planta transformada, molécula de rna inibitória de filamento duplo, e, composição detergente |
| CN102597228A (zh) * | 2009-10-23 | 2012-07-18 | 诺维信股份有限公司 | 纤维二糖水解酶变体及编码其的多核苷酸 |
| BR112012006847A2 (pt) | 2009-10-29 | 2015-09-08 | Novozymes As | polipeptídeo polinucleotídeo, célula hospedeira recombinante, métodos para produzir o polipeptídeo para produzir um mutante de uma célula parental, para inibir a expressão de um polipeptídeo, para produzir uma proteína, para degradar ou converter um material celulósico, para produzir um produto de fermentação, para produzir um produto de fermentação e pra fermentar um material celulósico, planta transgênica, parte da planta ou célula da planta, molécula de rna inibitória de filamento duplo, e, composição. |
| BR112012008291A8 (pt) | 2009-11-06 | 2019-05-21 | Novozymes Inc | composição de enzima, célula hospedeira recombinante, e, métodos de produzir uma composição de enzima, para degradar ou converter um material celulósico, para produzir um produto de fermentação e de fermentar um material celulósico |
| CA2780198A1 (en) | 2009-11-06 | 2011-05-12 | Novozymes, Inc. | Polypeptides having xylanase activity and polynucleotides encoding same |
| DK2513290T3 (en) | 2009-12-18 | 2016-01-25 | Novozymes Inc | Methods for Preparation of Polypeptides in Trichoderma Mutants with Protease Deficiency |
| EP2371963A1 (en) * | 2010-03-29 | 2011-10-05 | Heinrich-Heine-Universität Düsseldorf | Protein production in filamentous fungi |
| EP2558566A4 (en) * | 2010-04-14 | 2013-10-02 | Penn State Res Found | TRANSGENIC HANDLING STRATEGIES OF FILAMENTOUS FUNGI |
| JP6061862B2 (ja) * | 2010-11-22 | 2017-01-18 | カーギル，インコーポレイティド | ３‐ヒドロキシプロピオン酸生産用の組成物及び方法 |
| US9387175B2 (en) * | 2011-08-12 | 2016-07-12 | Tohoku University | Agent for evading immune response |
| US9404101B2 (en) * | 2011-08-24 | 2016-08-02 | Novozymes, Inc. | Methods for obtaining positive transformants of a filamentous fungal host cell |
| BR112014004190A2 (pt) * | 2011-08-24 | 2017-03-01 | Novozymes Inc | método para construir uma cepa fúngida filamentosa, cepa fúngida filamentosa, método para produzir múltiplos polipeptídeos recombinantes, e, construto em tandem |
| WO2013067028A1 (en) * | 2011-10-31 | 2013-05-10 | Bp Corporation North America Inc. | Use of mammalian promoters in filamentous fungi |
| WO2013076280A1 (en) * | 2011-11-23 | 2013-05-30 | Dsm Ip Assets B.V. | Nucleic acid assembly system |
| WO2013111754A1 (ja) * | 2012-01-23 | 2013-08-01 | 旭硝子株式会社 | 発現ベクターおよび蛋白質の製造方法 |
| WO2014100612A1 (en) * | 2012-12-21 | 2014-06-26 | Novozymes, Inc. | Methods for producing heterologous polypeptides in mutants of trichoderma |
| DK2964760T3 (da) * | 2013-03-08 | 2021-07-26 | Novozymes Inc | Cellobiohydrolasevarianter og polynukleotider, der koder for dem |
| WO2014145768A2 (en) * | 2013-03-15 | 2014-09-18 | Bp Corporation North America Inc. | Use of non-fungal 5' utrs in filamentous fungi |
| EP2840139A1 (en) * | 2013-08-23 | 2015-02-25 | Wageningen Universiteit | Method for the single step introduction of a plurality of genes in microbial cells |
| CN115975994A (zh) * | 2014-06-06 | 2023-04-18 | 诺维信公司 | 酶组合物及其用途 |
| DK3183343T3 (da) * | 2014-08-20 | 2020-03-23 | Novozymes As | Rekombinase-medieret integration af et polynukleotidbibliotek |
| US10385352B2 (en) * | 2015-03-09 | 2019-08-20 | Novozymes A/S | Methods of introducing multiple expression constructs into a eukaryotic cell |
| US20200063166A1 (en) * | 2017-03-13 | 2020-02-27 | Dsm Ip Assets B.V. | Zinc binuclear cluster transcriptional regulator-deficient strain |
| WO2018226900A2 (en) * | 2017-06-06 | 2018-12-13 | Zymergen Inc. | A htp genomic engineering platform for improving fungal strains |
-
2012
- 2012-08-23 BR BR112014004190A patent/BR112014004190A2/pt not_active Application Discontinuation
- 2012-08-23 EP EP12801652.4A patent/EP2748322A2/en not_active Ceased
- 2012-08-23 US US14/238,691 patent/US9493790B2/en active Active
- 2012-08-23 IN IN2136CHN2014 patent/IN2014CN02136A/en unknown
- 2012-08-23 AU AU2012298799A patent/AU2012298799B2/en active Active
- 2012-08-23 CN CN201810953356.5A patent/CN109136114A/zh active Pending
- 2012-08-23 CN CN201280052277.8A patent/CN103890180A/zh active Pending
- 2012-08-23 WO PCT/US2012/052143 patent/WO2013028912A2/en not_active Ceased
-
2016
- 2016-09-29 US US15/280,706 patent/US10301610B2/en active Active
-
2019
- 2019-04-25 US US16/394,951 patent/US10822601B2/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007136865A2 (en) * | 2006-05-19 | 2007-11-29 | Glycofi, Inc | Recombinant vectors |
| CN101970651A (zh) * | 2007-05-31 | 2011-02-09 | 诺维信股份有限公司 | 用于降解纤维素材料的组合物 |
| WO2010039889A2 (en) * | 2008-09-30 | 2010-04-08 | Novozymes, Inc. | Methods for using positively and negatively selectable genes in a filamentous fungal cell |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114561303A (zh) * | 2022-02-14 | 2022-05-31 | 大连理工大学 | 一株分泌高性能纤维素酶的里氏木霉工程菌株及其应用 |
| CN114561303B (zh) * | 2022-02-14 | 2023-11-17 | 大连理工大学 | 一株分泌高性能纤维素酶的里氏木霉工程菌株及其应用 |
| CN117757643A (zh) * | 2024-01-12 | 2024-03-26 | 华东理工大学 | 一种分泌表达人溶菌酶的里氏木霉工程菌及其构建方法和应用 |
Also Published As
| Publication number | Publication date |
|---|---|
| AU2012298799B2 (en) | 2018-02-01 |
| CN103890180A (zh) | 2014-06-25 |
| US9493790B2 (en) | 2016-11-15 |
| US10822601B2 (en) | 2020-11-03 |
| BR112014004190A2 (pt) | 2017-03-01 |
| EP2748322A2 (en) | 2014-07-02 |
| WO2013028912A3 (en) | 2013-06-06 |
| WO2013028912A2 (en) | 2013-02-28 |
| AU2012298799A1 (en) | 2014-02-13 |
| IN2014CN02136A (enExample) | 2015-05-29 |
| US20190249161A1 (en) | 2019-08-15 |
| US20140212977A1 (en) | 2014-07-31 |
| US20170015986A1 (en) | 2017-01-19 |
| US10301610B2 (en) | 2019-05-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN109136114A (zh) | 在丝状真菌宿主细胞中产生多种重组多肽的方法 | |
| US11713476B2 (en) | Compositions for saccharification of cellulosic material | |
| AU2019200618B2 (en) | Cellulolytic enzyme compositions and uses thereof | |
| DK2802651T3 (en) | GH61 POLYPEPTIDE VARIATIONS AND POLYNUCLEOTIDES CODING THEM | |
| US10308967B2 (en) | Milling process | |
| DK2841567T3 (en) | GH61 polypeptide variants and polynucleotides encoding them | |
| WO2020123845A1 (en) | Methods for increasing the productivity of a filamentous fungal cell in the production of a polypeptide | |
| US20230183385A1 (en) | Wheat Milling Process and GH8 Xylanases | |
| US10647972B2 (en) | Methods for obtaining positive transformants of a filamentous fungal host cell | |
| WO2021148278A1 (en) | Mutants of a filamentous fungal cell having increased productivity in the production of a polypeptide |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| WD01 | Invention patent application deemed withdrawn after publication | ||
| WD01 | Invention patent application deemed withdrawn after publication |
Application publication date: 20190104 |