JP2011206058A - セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド - Google Patents
セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド Download PDFInfo
- Publication number
- JP2011206058A JP2011206058A JP2011124595A JP2011124595A JP2011206058A JP 2011206058 A JP2011206058 A JP 2011206058A JP 2011124595 A JP2011124595 A JP 2011124595A JP 2011124595 A JP2011124595 A JP 2011124595A JP 2011206058 A JP2011206058 A JP 2011206058A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- seq
- acid
- polynucleotide
- protein
- 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.)
- Granted
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 324
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 321
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 319
- 230000001461 cytolytic effect Effects 0.000 title claims abstract description 147
- 230000002708 enhancing effect Effects 0.000 title claims abstract description 91
- 108091033319 polynucleotide Proteins 0.000 title claims description 83
- 102000040430 polynucleotide Human genes 0.000 title claims description 83
- 239000002157 polynucleotide Substances 0.000 title claims description 83
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 183
- 238000000034 method Methods 0.000 claims abstract description 158
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 127
- 239000000463 material Substances 0.000 claims abstract description 77
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 50
- 244000005700 microbiome Species 0.000 claims abstract description 42
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 31
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 31
- 239000000126 substance Substances 0.000 claims abstract description 17
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 139
- 235000018102 proteins Nutrition 0.000 claims description 125
- 125000003729 nucleotide group Chemical group 0.000 claims description 117
- 239000002773 nucleotide Substances 0.000 claims description 114
- 102000004190 Enzymes Human genes 0.000 claims description 110
- 108090000790 Enzymes Proteins 0.000 claims description 110
- 229940088598 enzyme Drugs 0.000 claims description 108
- 238000000855 fermentation Methods 0.000 claims description 89
- 230000004151 fermentation Effects 0.000 claims description 86
- 235000001014 amino acid Nutrition 0.000 claims description 79
- 150000001413 amino acids Chemical group 0.000 claims description 74
- 241000196324 Embryophyta Species 0.000 claims description 71
- 229920002678 cellulose Polymers 0.000 claims description 68
- 239000001913 cellulose Substances 0.000 claims description 68
- 238000004519 manufacturing process Methods 0.000 claims description 62
- 230000014509 gene expression Effects 0.000 claims description 50
- 108091026890 Coding region Proteins 0.000 claims description 45
- 239000000203 mixture Substances 0.000 claims description 45
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 43
- 108090001060 Lipase Proteins 0.000 claims description 42
- 102000004882 Lipase Human genes 0.000 claims description 40
- 239000004367 Lipase Substances 0.000 claims description 39
- 235000019421 lipase Nutrition 0.000 claims description 39
- 108020004414 DNA Proteins 0.000 claims description 38
- 108090000371 Esterases Proteins 0.000 claims description 37
- 108091005804 Peptidases Proteins 0.000 claims description 36
- 239000004365 Protease Substances 0.000 claims description 30
- 108010059892 Cellulase Proteins 0.000 claims description 29
- 102000003992 Peroxidases Human genes 0.000 claims description 29
- 239000003599 detergent Substances 0.000 claims description 29
- 108010029541 Laccase Proteins 0.000 claims description 27
- -1 hydrogen monoxide Chemical class 0.000 claims description 26
- 150000007524 organic acids Chemical class 0.000 claims description 26
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 25
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 24
- 239000002299 complementary DNA Substances 0.000 claims description 24
- 239000011368 organic material Substances 0.000 claims description 24
- 102000015439 Phospholipases Human genes 0.000 claims description 23
- 108010064785 Phospholipases Proteins 0.000 claims description 23
- 238000006467 substitution reaction Methods 0.000 claims description 23
- 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 claims description 22
- 108040007629 peroxidase activity proteins Proteins 0.000 claims description 22
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 claims description 21
- 102000005575 Cellulases Human genes 0.000 claims description 21
- 108010084185 Cellulases Proteins 0.000 claims description 21
- 239000008103 glucose Substances 0.000 claims description 20
- 238000012258 culturing Methods 0.000 claims description 19
- 239000012634 fragment Substances 0.000 claims description 19
- 230000007062 hydrolysis Effects 0.000 claims description 18
- 238000006460 hydrolysis reaction Methods 0.000 claims description 18
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 claims description 17
- 239000013612 plasmid Substances 0.000 claims description 17
- 230000015556 catabolic process Effects 0.000 claims description 16
- 230000000295 complement effect Effects 0.000 claims description 16
- 238000006731 degradation reaction Methods 0.000 claims description 16
- 239000013604 expression vector Substances 0.000 claims description 16
- 230000001105 regulatory effect Effects 0.000 claims description 16
- 239000002253 acid Substances 0.000 claims description 15
- 108010005400 cutinase Proteins 0.000 claims description 15
- 108010002430 hemicellulase Proteins 0.000 claims description 15
- 108010008885 Cellulose 1,4-beta-Cellobiosidase Proteins 0.000 claims description 14
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 claims description 14
- 241000588724 Escherichia coli Species 0.000 claims description 14
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 claims description 14
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 13
- 238000012217 deletion Methods 0.000 claims description 13
- 230000037430 deletion Effects 0.000 claims description 13
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 12
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 12
- 235000000346 sugar Nutrition 0.000 claims description 12
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 claims description 11
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 claims description 11
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 claims description 11
- 235000005822 corn Nutrition 0.000 claims description 11
- 230000035772 mutation Effects 0.000 claims description 11
- 238000003780 insertion Methods 0.000 claims description 10
- 230000037431 insertion Effects 0.000 claims description 10
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 claims description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 9
- 230000009261 transgenic effect Effects 0.000 claims description 9
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 claims description 8
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 claims description 8
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Chemical compound C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 claims description 8
- 238000003259 recombinant expression Methods 0.000 claims description 8
- 229940059442 hemicellulase Drugs 0.000 claims description 7
- 150000002576 ketones Chemical class 0.000 claims description 7
- 239000004310 lactic acid Substances 0.000 claims description 7
- 235000014655 lactic acid Nutrition 0.000 claims description 7
- 239000002699 waste material Substances 0.000 claims description 7
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims description 6
- RGHNJXZEOKUKBD-SQOUGZDYSA-N D-gluconic acid Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O RGHNJXZEOKUKBD-SQOUGZDYSA-N 0.000 claims description 6
- VZCYOOQTPOCHFL-OWOJBTEDSA-N Fumaric acid Chemical compound OC(=O)\C=C\C(O)=O VZCYOOQTPOCHFL-OWOJBTEDSA-N 0.000 claims description 6
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 6
- OFOBLEOULBTSOW-UHFFFAOYSA-N Malonic acid Chemical compound OC(=O)CC(O)=O OFOBLEOULBTSOW-UHFFFAOYSA-N 0.000 claims description 6
- WNLRTRBMVRJNCN-UHFFFAOYSA-N adipic acid Chemical compound OC(=O)CCCCC(O)=O WNLRTRBMVRJNCN-UHFFFAOYSA-N 0.000 claims description 6
- 239000001257 hydrogen Substances 0.000 claims description 6
- 229910052739 hydrogen Inorganic materials 0.000 claims description 6
- HEBKCHPVOIAQTA-UHFFFAOYSA-N meso ribitol Natural products OCC(O)C(O)C(O)CO HEBKCHPVOIAQTA-UHFFFAOYSA-N 0.000 claims description 6
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 claims description 5
- 239000004471 Glycine Substances 0.000 claims description 5
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 5
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 5
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 5
- 239000004472 Lysine Substances 0.000 claims description 5
- KDYFGRWQOYBRFD-UHFFFAOYSA-N Succinic acid Natural products OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 claims description 5
- 235000019253 formic acid Nutrition 0.000 claims description 5
- 239000007789 gas Substances 0.000 claims description 5
- 239000004094 surface-active agent Substances 0.000 claims description 5
- DNIAPMSPPWPWGF-VKHMYHEASA-N (+)-propylene glycol Chemical compound C[C@H](O)CO DNIAPMSPPWPWGF-VKHMYHEASA-N 0.000 claims description 4
- YPFDHNVEDLHUCE-UHFFFAOYSA-N 1,3-propanediol Substances OCCCO YPFDHNVEDLHUCE-UHFFFAOYSA-N 0.000 claims description 4
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 claims description 4
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 claims description 4
- 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 claims description 4
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 claims description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 4
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 4
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 4
- 239000004473 Threonine Substances 0.000 claims description 4
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 claims description 4
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 claims description 4
- 235000003704 aspartic acid Nutrition 0.000 claims description 4
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims description 4
- 235000015165 citric acid Nutrition 0.000 claims description 4
- 229930182830 galactose Natural products 0.000 claims description 4
- 235000013922 glutamic acid Nutrition 0.000 claims description 4
- 239000004220 glutamic acid Substances 0.000 claims description 4
- 239000010893 paper waste Substances 0.000 claims description 4
- 239000010908 plant waste Substances 0.000 claims description 4
- 229920000166 polytrimethylene carbonate Polymers 0.000 claims description 4
- 235000019260 propionic acid Nutrition 0.000 claims description 4
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 claims description 4
- 239000000600 sorbitol Substances 0.000 claims description 4
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 claims description 4
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 claims description 3
- RTBFRGCFXZNCOE-UHFFFAOYSA-N 1-methylsulfonylpiperidin-4-one Chemical compound CS(=O)(=O)N1CCC(=O)CC1 RTBFRGCFXZNCOE-UHFFFAOYSA-N 0.000 claims description 3
- RXMWXENJQAINCC-DMTCNVIQSA-N 2,5-didehydro-D-gluconic acid Chemical compound OCC(=O)[C@@H](O)[C@H](O)C(=O)C(O)=O RXMWXENJQAINCC-DMTCNVIQSA-N 0.000 claims description 3
- RXMWXENJQAINCC-UHFFFAOYSA-N 2,5-diketo-D-gluconic acid Natural products OCC(=O)C(O)C(O)C(=O)C(O)=O RXMWXENJQAINCC-UHFFFAOYSA-N 0.000 claims description 3
- JAHNSTQSQJOJLO-UHFFFAOYSA-N 2-(3-fluorophenyl)-1h-imidazole Chemical compound FC1=CC=CC(C=2NC=CN=2)=C1 JAHNSTQSQJOJLO-UHFFFAOYSA-N 0.000 claims description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Natural products OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 claims description 3
- HEBKCHPVOIAQTA-QWWZWVQMSA-N D-arabinitol Chemical compound OC[C@@H](O)C(O)[C@H](O)CO HEBKCHPVOIAQTA-QWWZWVQMSA-N 0.000 claims description 3
- RGHNJXZEOKUKBD-UHFFFAOYSA-N D-gluconic acid Natural products OCC(O)C(O)C(O)C(O)C(O)=O RGHNJXZEOKUKBD-UHFFFAOYSA-N 0.000 claims description 3
- QXKAIJAYHKCRRA-UHFFFAOYSA-N D-lyxonic acid Natural products OCC(O)C(O)C(O)C(O)=O QXKAIJAYHKCRRA-UHFFFAOYSA-N 0.000 claims description 3
- QXKAIJAYHKCRRA-FLRLBIABSA-N D-xylonic acid Chemical compound OC[C@@H](O)[C@H](O)[C@@H](O)C(O)=O QXKAIJAYHKCRRA-FLRLBIABSA-N 0.000 claims description 3
- TVXBFESIOXBWNM-UHFFFAOYSA-N Xylitol Natural products OCCC(O)C(O)C(O)CCO TVXBFESIOXBWNM-UHFFFAOYSA-N 0.000 claims description 3
- 239000001361 adipic acid Substances 0.000 claims description 3
- 235000011037 adipic acid Nutrition 0.000 claims description 3
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 claims description 3
- JFCQEDHGNNZCLN-UHFFFAOYSA-N anhydrous glutaric acid Natural products OC(=O)CCCC(O)=O JFCQEDHGNNZCLN-UHFFFAOYSA-N 0.000 claims description 3
- 235000010323 ascorbic acid Nutrition 0.000 claims description 3
- 239000011668 ascorbic acid Substances 0.000 claims description 3
- 229960005070 ascorbic acid Drugs 0.000 claims description 3
- 239000001530 fumaric acid Substances 0.000 claims description 3
- 239000000174 gluconic acid Substances 0.000 claims description 3
- 235000012208 gluconic acid Nutrition 0.000 claims description 3
- 229950006191 gluconic acid Drugs 0.000 claims description 3
- TYQCGQRIZGCHNB-JLAZNSOCSA-N l-ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(O)=C(O)C1=O TYQCGQRIZGCHNB-JLAZNSOCSA-N 0.000 claims description 3
- 239000001630 malic acid Substances 0.000 claims description 3
- 235000011090 malic acid Nutrition 0.000 claims description 3
- LVHBHZANLOWSRM-UHFFFAOYSA-N methylenebutanedioic acid Natural products OC(=O)CC(=C)C(O)=O LVHBHZANLOWSRM-UHFFFAOYSA-N 0.000 claims description 3
- 239000000811 xylitol Substances 0.000 claims description 3
- HEBKCHPVOIAQTA-SCDXWVJYSA-N xylitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)CO HEBKCHPVOIAQTA-SCDXWVJYSA-N 0.000 claims description 3
- 235000010447 xylitol Nutrition 0.000 claims description 3
- 229960002675 xylitol Drugs 0.000 claims description 3
- DSLZVSRJTYRBFB-LLEIAEIESA-N D-glucaric acid Chemical compound OC(=O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O DSLZVSRJTYRBFB-LLEIAEIESA-N 0.000 claims description 2
- IAJILQKETJEXLJ-UHFFFAOYSA-N Galacturonsaeure Natural products O=CC(O)C(O)C(O)C(O)C(O)=O IAJILQKETJEXLJ-UHFFFAOYSA-N 0.000 claims description 2
- KDYFGRWQOYBRFD-NUQCWPJISA-N butanedioic acid Chemical compound O[14C](=O)CC[14C](O)=O KDYFGRWQOYBRFD-NUQCWPJISA-N 0.000 claims description 2
- 239000001569 carbon dioxide Substances 0.000 claims description 2
- 229910002092 carbon dioxide Inorganic materials 0.000 claims description 2
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims description 2
- 229940097043 glucuronic acid Drugs 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 2
- 241000209149 Zea Species 0.000 claims 2
- 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 claims 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 claims 1
- 239000013598 vector Substances 0.000 abstract description 39
- 210000004027 cell Anatomy 0.000 description 161
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 87
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 86
- 229940024606 amino acid Drugs 0.000 description 51
- 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 47
- 241000223218 Fusarium Species 0.000 description 47
- 230000000694 effects Effects 0.000 description 46
- 108091028043 Nucleic acid sequence Proteins 0.000 description 38
- 102000035195 Peptidases Human genes 0.000 description 34
- 230000002538 fungal effect Effects 0.000 description 32
- 125000003275 alpha amino acid group Chemical group 0.000 description 31
- 239000000047 product Substances 0.000 description 31
- 239000002609 medium Substances 0.000 description 30
- 238000002360 preparation method Methods 0.000 description 24
- 241000193830 Bacillus <bacterium> Species 0.000 description 23
- 241000228212 Aspergillus Species 0.000 description 22
- 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 22
- 229940072417 peroxidase Drugs 0.000 description 20
- 230000008569 process Effects 0.000 description 20
- 241000223198 Humicola Species 0.000 description 19
- 241000233866 Fungi Species 0.000 description 18
- 241000499912 Trichoderma reesei Species 0.000 description 18
- 230000001580 bacterial effect Effects 0.000 description 18
- 239000007788 liquid Substances 0.000 description 18
- 240000006439 Aspergillus oryzae Species 0.000 description 17
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 17
- 241001019659 Acremonium <Plectosphaerellaceae> Species 0.000 description 16
- 239000002028 Biomass Substances 0.000 description 16
- 239000000523 sample Substances 0.000 description 16
- 239000000758 substrate Substances 0.000 description 16
- 102000013142 Amylases Human genes 0.000 description 15
- 108010065511 Amylases Proteins 0.000 description 15
- 235000019418 amylase Nutrition 0.000 description 15
- 108010047754 beta-Glucosidase Proteins 0.000 description 15
- 102000006995 beta-Glucosidase Human genes 0.000 description 15
- 238000006243 chemical reaction Methods 0.000 description 15
- 230000012010 growth Effects 0.000 description 15
- 230000004048 modification Effects 0.000 description 15
- 238000012986 modification Methods 0.000 description 15
- 230000010076 replication Effects 0.000 description 15
- 229920002488 Hemicellulose Polymers 0.000 description 14
- 241000228245 Aspergillus niger Species 0.000 description 12
- 235000014469 Bacillus subtilis Nutrition 0.000 description 12
- 241001480714 Humicola insolens Species 0.000 description 12
- 238000009396 hybridization Methods 0.000 description 12
- 235000019419 proteases Nutrition 0.000 description 12
- 230000009466 transformation Effects 0.000 description 12
- 239000004382 Amylase Substances 0.000 description 11
- 241000894006 Bacteria Species 0.000 description 11
- 102000004157 Hydrolases Human genes 0.000 description 11
- 108090000604 Hydrolases Proteins 0.000 description 11
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 11
- 229940106157 cellulase Drugs 0.000 description 11
- 238000002703 mutagenesis Methods 0.000 description 11
- 231100000350 mutagenesis Toxicity 0.000 description 11
- 239000002853 nucleic acid probe Substances 0.000 description 11
- 238000013518 transcription Methods 0.000 description 11
- 230000035897 transcription Effects 0.000 description 11
- 230000014616 translation Effects 0.000 description 11
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 10
- 244000063299 Bacillus subtilis Species 0.000 description 10
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 10
- 241000223259 Trichoderma Species 0.000 description 10
- 240000008042 Zea mays Species 0.000 description 10
- 102000004316 Oxidoreductases Human genes 0.000 description 9
- 108090000854 Oxidoreductases Proteins 0.000 description 9
- 230000002378 acidificating effect Effects 0.000 description 9
- 125000000539 amino acid group Chemical group 0.000 description 9
- 230000000593 degrading effect Effects 0.000 description 9
- 239000008187 granular material Substances 0.000 description 9
- 229920005610 lignin Polymers 0.000 description 9
- 230000000813 microbial effect Effects 0.000 description 9
- 230000007935 neutral effect Effects 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 238000011282 treatment Methods 0.000 description 9
- 241000351920 Aspergillus nidulans Species 0.000 description 8
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 8
- 241000223221 Fusarium oxysporum Species 0.000 description 8
- 241000589516 Pseudomonas Species 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- 239000000654 additive Substances 0.000 description 8
- 235000014113 dietary fatty acids Nutrition 0.000 description 8
- 238000005516 engineering process Methods 0.000 description 8
- 230000002255 enzymatic effect Effects 0.000 description 8
- 239000000194 fatty acid Substances 0.000 description 8
- 229930195729 fatty acid Natural products 0.000 description 8
- 230000010354 integration Effects 0.000 description 8
- 230000002366 lipolytic effect Effects 0.000 description 8
- 108020004999 messenger RNA Proteins 0.000 description 8
- 238000002493 microarray Methods 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 241000894007 species Species 0.000 description 8
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 7
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 7
- 241000146406 Fusarium heterosporum Species 0.000 description 7
- 241000221779 Fusarium sambucinum Species 0.000 description 7
- 241000427940 Fusarium solani Species 0.000 description 7
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 7
- 229920001503 Glucan Polymers 0.000 description 7
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 7
- 241000235395 Mucor Species 0.000 description 7
- 241000235070 Saccharomyces Species 0.000 description 7
- 235000001006 Saccharomyces cerevisiae var diastaticus Nutrition 0.000 description 7
- 244000206963 Saccharomyces cerevisiae var. diastaticus Species 0.000 description 7
- 241000187747 Streptomyces Species 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 210000002421 cell wall Anatomy 0.000 description 7
- 238000007796 conventional method Methods 0.000 description 7
- 150000004665 fatty acids Chemical class 0.000 description 7
- 235000011187 glycerol Nutrition 0.000 description 7
- 235000015097 nutrients Nutrition 0.000 description 7
- 229920000642 polymer Polymers 0.000 description 7
- 150000004804 polysaccharides Chemical class 0.000 description 7
- 150000008163 sugars Chemical class 0.000 description 7
- 108010013043 Acetylesterase Proteins 0.000 description 6
- 241000796533 Arna Species 0.000 description 6
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 6
- 241000567178 Fusarium venenatum Species 0.000 description 6
- 241000221960 Neurospora Species 0.000 description 6
- 240000007594 Oryza sativa Species 0.000 description 6
- 235000007164 Oryza sativa Nutrition 0.000 description 6
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 6
- 241000228143 Penicillium Species 0.000 description 6
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 108010056079 Subtilisins Proteins 0.000 description 6
- 102000005158 Subtilisins Human genes 0.000 description 6
- 108010048241 acetamidase Proteins 0.000 description 6
- 230000000996 additive effect Effects 0.000 description 6
- 108090000637 alpha-Amylases Proteins 0.000 description 6
- 108010080434 cephalosporin-C deacetylase Proteins 0.000 description 6
- 230000008859 change Effects 0.000 description 6
- YARKTHNUMGKMGS-LQGKIZFRSA-N chembl3193980 Chemical compound COC1=C(O)C(OC)=CC(\C=N\N=C\C=2C=C(OC)C(O)=C(OC)C=2)=C1 YARKTHNUMGKMGS-LQGKIZFRSA-N 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 6
- 238000002955 isolation Methods 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 238000003199 nucleic acid amplification method Methods 0.000 description 6
- 230000008488 polyadenylation Effects 0.000 description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 6
- 235000009566 rice Nutrition 0.000 description 6
- 238000013519 translation Methods 0.000 description 6
- 241001513093 Aspergillus awamori Species 0.000 description 5
- 101000757144 Aspergillus niger Glucoamylase Proteins 0.000 description 5
- 241000194108 Bacillus licheniformis Species 0.000 description 5
- UGFAIRIUMAVXCW-UHFFFAOYSA-N Carbon monoxide Chemical compound [O+]#[C-] UGFAIRIUMAVXCW-UHFFFAOYSA-N 0.000 description 5
- 241000223195 Fusarium graminearum Species 0.000 description 5
- 102100031415 Hepatic triacylglycerol lipase Human genes 0.000 description 5
- 102100027612 Kallikrein-11 Human genes 0.000 description 5
- 125000003412 L-alanyl group Chemical group [H]N([H])[C@@](C([H])([H])[H])(C(=O)[*])[H] 0.000 description 5
- 108020002496 Lysophospholipase Proteins 0.000 description 5
- 108700020962 Peroxidase Proteins 0.000 description 5
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 5
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 5
- 241000209504 Poaceae Species 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 241000235403 Rhizomucor miehei Species 0.000 description 5
- 241000235527 Rhizopus Species 0.000 description 5
- 244000061456 Solanum tuberosum Species 0.000 description 5
- 235000002595 Solanum tuberosum Nutrition 0.000 description 5
- 241001494489 Thielavia Species 0.000 description 5
- 241000222354 Trametes Species 0.000 description 5
- 101710152431 Trypsin-like protease Proteins 0.000 description 5
- 108010093941 acetylxylan esterase Proteins 0.000 description 5
- 102000004139 alpha-Amylases Human genes 0.000 description 5
- 229940024171 alpha-amylase Drugs 0.000 description 5
- 229960000723 ampicillin Drugs 0.000 description 5
- 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 5
- 230000003321 amplification Effects 0.000 description 5
- 229910002091 carbon monoxide Inorganic materials 0.000 description 5
- 235000013339 cereals Nutrition 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 230000007071 enzymatic hydrolysis Effects 0.000 description 5
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 5
- 239000000446 fuel Substances 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 229930182478 glucoside Natural products 0.000 description 5
- 238000002744 homologous recombination Methods 0.000 description 5
- 230000006801 homologous recombination Effects 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 229920001282 polysaccharide Polymers 0.000 description 5
- 239000005017 polysaccharide Substances 0.000 description 5
- 239000000843 powder Substances 0.000 description 5
- 238000012545 processing Methods 0.000 description 5
- 230000002797 proteolythic effect Effects 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 239000013589 supplement Substances 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 241001225321 Aspergillus fumigatus Species 0.000 description 4
- 241000221198 Basidiomycota Species 0.000 description 4
- 229920002498 Beta-glucan Polymers 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 108010031396 Catechol oxidase Proteins 0.000 description 4
- 102000030523 Catechol oxidase Human genes 0.000 description 4
- 244000251987 Coprinus macrorhizus Species 0.000 description 4
- 241000222356 Coriolus Species 0.000 description 4
- 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 description 4
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- 229920000057 Mannan Polymers 0.000 description 4
- 102100036617 Monoacylglycerol lipase ABHD2 Human genes 0.000 description 4
- 241000226677 Myceliophthora Species 0.000 description 4
- 241001236817 Paecilomyces <Clavicipitaceae> Species 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 241000222640 Polyporus Species 0.000 description 4
- 241000589774 Pseudomonas sp. Species 0.000 description 4
- 244000184734 Pyrus japonica Species 0.000 description 4
- 241000235402 Rhizomucor Species 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 238000002105 Southern blotting Methods 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- 241000223257 Thermomyces Species 0.000 description 4
- 241001313536 Thermothelomyces thermophila Species 0.000 description 4
- 241000700605 Viruses Species 0.000 description 4
- 241000588902 Zymomonas mobilis Species 0.000 description 4
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 4
- 150000007513 acids Chemical class 0.000 description 4
- 229940025131 amylases Drugs 0.000 description 4
- 229940091771 aspergillus fumigatus Drugs 0.000 description 4
- 239000002585 base Substances 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 4
- 108010005774 beta-Galactosidase Proteins 0.000 description 4
- 102000005936 beta-Galactosidase Human genes 0.000 description 4
- 238000010364 biochemical engineering Methods 0.000 description 4
- 108010089934 carbohydrase Proteins 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 239000001768 carboxy methyl cellulose Substances 0.000 description 4
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 4
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 4
- 239000012876 carrier material Substances 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 230000002759 chromosomal effect Effects 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 230000002779 inactivation Effects 0.000 description 4
- 229910052500 inorganic mineral Inorganic materials 0.000 description 4
- 239000001573 invertase Substances 0.000 description 4
- 235000011073 invertase Nutrition 0.000 description 4
- 239000011707 mineral Substances 0.000 description 4
- 229910052757 nitrogen Inorganic materials 0.000 description 4
- 238000005457 optimization Methods 0.000 description 4
- 239000001814 pectin Substances 0.000 description 4
- 229920001277 pectin Polymers 0.000 description 4
- 235000010987 pectin Nutrition 0.000 description 4
- 239000008188 pellet Substances 0.000 description 4
- 230000037039 plant physiology Effects 0.000 description 4
- 238000003752 polymerase chain reaction Methods 0.000 description 4
- 210000001938 protoplast Anatomy 0.000 description 4
- 238000012552 review Methods 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 239000002002 slurry Substances 0.000 description 4
- 239000002689 soil Substances 0.000 description 4
- 238000010561 standard procedure Methods 0.000 description 4
- 239000002023 wood Substances 0.000 description 4
- 229920001221 xylan Polymers 0.000 description 4
- 150000004823 xylans Chemical class 0.000 description 4
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 3
- 108010011619 6-Phytase Proteins 0.000 description 3
- 241000590020 Achromobacter Species 0.000 description 3
- 102100034044 All-trans-retinol dehydrogenase [NAD(+)] ADH1B Human genes 0.000 description 3
- 101710193111 All-trans-retinol dehydrogenase [NAD(+)] ADH4 Proteins 0.000 description 3
- 102000004400 Aminopeptidases Human genes 0.000 description 3
- 108090000915 Aminopeptidases Proteins 0.000 description 3
- 108010037870 Anthranilate Synthase Proteins 0.000 description 3
- 241000223651 Aureobasidium Species 0.000 description 3
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 3
- 241000193422 Bacillus lentus Species 0.000 description 3
- 241000194107 Bacillus megaterium Species 0.000 description 3
- 108010006303 Carboxypeptidases Proteins 0.000 description 3
- 102000005367 Carboxypeptidases Human genes 0.000 description 3
- 108010053835 Catalase Proteins 0.000 description 3
- 102100035882 Catalase Human genes 0.000 description 3
- 241000146399 Ceriporiopsis Species 0.000 description 3
- 108010022172 Chitinases Proteins 0.000 description 3
- 102000012286 Chitinases Human genes 0.000 description 3
- 241000222511 Coprinus Species 0.000 description 3
- 108010053770 Deoxyribonucleases Proteins 0.000 description 3
- 102000016911 Deoxyribonucleases Human genes 0.000 description 3
- 241001112697 Fusarium reticulatum Species 0.000 description 3
- 102100022624 Glucoamylase Human genes 0.000 description 3
- 244000285963 Kluyveromyces fragilis Species 0.000 description 3
- 235000014663 Kluyveromyces fragilis Nutrition 0.000 description 3
- 125000000570 L-alpha-aspartyl group Chemical group [H]OC(=O)C([H])([H])[C@]([H])(N([H])[H])C(*)=O 0.000 description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 3
- 108010013563 Lipoprotein Lipase Proteins 0.000 description 3
- 102100024295 Maltase-glucoamylase Human genes 0.000 description 3
- 102000001696 Mannosidases Human genes 0.000 description 3
- 108010054377 Mannosidases Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 241001661345 Moesziomyces antarcticus Species 0.000 description 3
- 241000221961 Neurospora crassa Species 0.000 description 3
- 241000222393 Phanerochaete chrysosporium Species 0.000 description 3
- 244000046052 Phaseolus vulgaris Species 0.000 description 3
- 102100037883 Phospholipase B1, membrane-associated Human genes 0.000 description 3
- 241000235648 Pichia Species 0.000 description 3
- 240000005384 Rhizopus oryzae Species 0.000 description 3
- 241000223252 Rhodotorula Species 0.000 description 3
- 108010083644 Ribonucleases Proteins 0.000 description 3
- 102000006382 Ribonucleases Human genes 0.000 description 3
- 241000222480 Schizophyllum Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 108091081024 Start codon Proteins 0.000 description 3
- 108090000787 Subtilisin Proteins 0.000 description 3
- 241000228178 Thermoascus Species 0.000 description 3
- 108060008539 Transglutaminase Proteins 0.000 description 3
- 241000223261 Trichoderma viride Species 0.000 description 3
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 3
- 108700015934 Triose-phosphate isomerases Proteins 0.000 description 3
- 241000082085 Verticillium <Phyllachorales> Species 0.000 description 3
- 241000607632 Vibrio alginolyticus chemovar iophagus Species 0.000 description 3
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 3
- 108010030291 alpha-Galactosidase Proteins 0.000 description 3
- 102000005840 alpha-Galactosidase Human genes 0.000 description 3
- 108010028144 alpha-Glucosidases Proteins 0.000 description 3
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 3
- 108010055059 beta-Mannosidase Proteins 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 239000003054 catalyst Substances 0.000 description 3
- 230000003197 catalytic effect Effects 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- WBCMGDNFDRNGGZ-ACNVUDSMSA-N coumarate Natural products COC(=O)C1=CO[C@H](O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@H]3[C@@H]1C=C[C@]34OC(=O)C(=C4)[C@H](C)OC(=O)C=Cc5ccc(O)cc5 WBCMGDNFDRNGGZ-ACNVUDSMSA-N 0.000 description 3
- 150000002016 disaccharides Chemical class 0.000 description 3
- 230000007717 exclusion Effects 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 238000003306 harvesting Methods 0.000 description 3
- 229910001385 heavy metal Inorganic materials 0.000 description 3
- 239000005556 hormone Substances 0.000 description 3
- 229940088597 hormone Drugs 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 229940085127 phytase Drugs 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 229920005862 polyol Polymers 0.000 description 3
- 150000003077 polyols Chemical class 0.000 description 3
- 239000013615 primer Substances 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 150000005846 sugar alcohols Chemical class 0.000 description 3
- 230000002103 transcriptional effect Effects 0.000 description 3
- 102000003601 transglutaminase Human genes 0.000 description 3
- 229940088594 vitamin Drugs 0.000 description 3
- 229930003231 vitamin Natural products 0.000 description 3
- 235000013343 vitamin Nutrition 0.000 description 3
- 239000011782 vitamin Substances 0.000 description 3
- ALRHLSYJTWAHJZ-UHFFFAOYSA-N 3-hydroxypropionic acid Chemical compound OCCC(O)=O ALRHLSYJTWAHJZ-UHFFFAOYSA-N 0.000 description 2
- OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 2
- ALYNCZNDIQEVRV-UHFFFAOYSA-N 4-aminobenzoic acid Chemical compound NC1=CC=C(C(O)=O)C=C1 ALYNCZNDIQEVRV-UHFFFAOYSA-N 0.000 description 2
- RGIIXLVKXLFDLP-UHFFFAOYSA-N 5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene Chemical compound S1C(C#CC(OC(C)=O)COC(=O)C)=CC=C1C1=CC=CS1 RGIIXLVKXLFDLP-UHFFFAOYSA-N 0.000 description 2
- 241000235389 Absidia Species 0.000 description 2
- 241001438635 Acremonium brachypenium Species 0.000 description 2
- 229920002126 Acrylic acid copolymer Polymers 0.000 description 2
- 101710197633 Actin-1 Proteins 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 2
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 2
- 241000223600 Alternaria Species 0.000 description 2
- 241000609240 Ambelania acida Species 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 2
- 239000005695 Ammonium acetate Substances 0.000 description 2
- 101100163849 Arabidopsis thaliana ARS1 gene Proteins 0.000 description 2
- XKRFYHLGVUSROY-UHFFFAOYSA-N Argon Chemical compound [Ar] XKRFYHLGVUSROY-UHFFFAOYSA-N 0.000 description 2
- 241000222211 Arthromyces Species 0.000 description 2
- 108010017640 Aspartic Acid Proteases Proteins 0.000 description 2
- 102000035101 Aspartic proteases Human genes 0.000 description 2
- 108091005502 Aspartic proteases Proteins 0.000 description 2
- 241000892910 Aspergillus foetidus Species 0.000 description 2
- 101000690713 Aspergillus niger Alpha-glucosidase Proteins 0.000 description 2
- 108090000145 Bacillolysin Proteins 0.000 description 2
- 241000193752 Bacillus circulans Species 0.000 description 2
- 108010029675 Bacillus licheniformis alpha-amylase Proteins 0.000 description 2
- 241000194103 Bacillus pumilus Species 0.000 description 2
- 241000193388 Bacillus thuringiensis Species 0.000 description 2
- 108091005658 Basic proteases Proteins 0.000 description 2
- 102100032487 Beta-mannosidase Human genes 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 240000002791 Brassica napus Species 0.000 description 2
- 241000219193 Brassicaceae Species 0.000 description 2
- 241000193764 Brevibacillus brevis Species 0.000 description 2
- 241000206605 Brochothrix Species 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 241001508811 Clavispora Species 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 241001337994 Cryptococcus <scale insect> Species 0.000 description 2
- 229920000858 Cyclodextrin Polymers 0.000 description 2
- 102000018832 Cytochromes Human genes 0.000 description 2
- 101710088194 Dehydrogenase Proteins 0.000 description 2
- 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 2
- 241000580475 Embellisia Species 0.000 description 2
- 102000010911 Enzyme Precursors Human genes 0.000 description 2
- 108010062466 Enzyme Precursors Proteins 0.000 description 2
- PLUBXMRUUVWRLT-UHFFFAOYSA-N Ethyl methanesulfonate Chemical compound CCOS(C)(=O)=O PLUBXMRUUVWRLT-UHFFFAOYSA-N 0.000 description 2
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical group C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 2
- 102000048120 Galactokinases Human genes 0.000 description 2
- 108700023157 Galactokinases Proteins 0.000 description 2
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 2
- 101100369308 Geobacillus stearothermophilus nprS gene Proteins 0.000 description 2
- 101100080316 Geobacillus stearothermophilus nprT gene Proteins 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 2
- 206010020649 Hyperkeratosis Diseases 0.000 description 2
- 241000766694 Hyphozyma Species 0.000 description 2
- 102000004195 Isomerases Human genes 0.000 description 2
- 108090000769 Isomerases Proteins 0.000 description 2
- 241000235649 Kluyveromyces Species 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- 125000003440 L-leucyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C(C([H])([H])[H])([H])C([H])([H])[H] 0.000 description 2
- 125000002842 L-seryl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])O[H] 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 241000209510 Liliopsida Species 0.000 description 2
- 239000006142 Luria-Bertani Agar Substances 0.000 description 2
- 102000004317 Lyases Human genes 0.000 description 2
- 108090000856 Lyases Proteins 0.000 description 2
- VZUNGTLZRAYYDE-UHFFFAOYSA-N N-methyl-N'-nitro-N-nitrosoguanidine Chemical compound O=NN(C)C(=N)N[N+]([O-])=O VZUNGTLZRAYYDE-UHFFFAOYSA-N 0.000 description 2
- 238000005481 NMR spectroscopy Methods 0.000 description 2
- PVNIIMVLHYAWGP-UHFFFAOYSA-N Niacin Chemical compound OC(=O)C1=CC=CN=C1 PVNIIMVLHYAWGP-UHFFFAOYSA-N 0.000 description 2
- 244000061176 Nicotiana tabacum Species 0.000 description 2
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 2
- 241000233654 Oomycetes Species 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 241000222385 Phanerochaete Species 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- 241000222395 Phlebia Species 0.000 description 2
- 102000011420 Phospholipase D Human genes 0.000 description 2
- 108090000553 Phospholipase D Proteins 0.000 description 2
- 108010058864 Phospholipases A2 Proteins 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 241000235379 Piromyces Species 0.000 description 2
- 241000222350 Pleurotus Species 0.000 description 2
- 241000789035 Polyporus pinsitus Species 0.000 description 2
- 241000589540 Pseudomonas fluorescens Species 0.000 description 2
- 241000589755 Pseudomonas mendocina Species 0.000 description 2
- 241000589614 Pseudomonas stutzeri Species 0.000 description 2
- 241000577556 Pseudomonas wisconsinensis Species 0.000 description 2
- 241000222644 Pycnoporus <fungus> Species 0.000 description 2
- VYGQUTWHTHXGQB-FFHKNEKCSA-N Retinol Palmitate Chemical compound CCCCCCCCCCCCCCCC(=O)OC\C=C(/C)\C=C\C=C(/C)\C=C\C1=C(C)CCCC1(C)C VYGQUTWHTHXGQB-FFHKNEKCSA-N 0.000 description 2
- 241000813090 Rhizoctonia solani Species 0.000 description 2
- 241000223253 Rhodotorula glutinis Species 0.000 description 2
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 2
- 235000003534 Saccharomyces carlsbergensis Nutrition 0.000 description 2
- 241001123227 Saccharomyces pastorianus Species 0.000 description 2
- 241000235346 Schizosaccharomyces Species 0.000 description 2
- 101100097319 Schizosaccharomyces pombe (strain 972 / ATCC 24843) ala1 gene Proteins 0.000 description 2
- 241000221696 Sclerotinia sclerotiorum Species 0.000 description 2
- 241000906075 Simplicillium obclavatum Species 0.000 description 2
- 241000187398 Streptomyces lividans Species 0.000 description 2
- 241001468239 Streptomyces murinus Species 0.000 description 2
- RAHZWNYVWXNFOC-UHFFFAOYSA-N Sulphur dioxide Chemical compound O=S=O RAHZWNYVWXNFOC-UHFFFAOYSA-N 0.000 description 2
- 241000228341 Talaromyces Species 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- 241001149964 Tolypocladium Species 0.000 description 2
- 241000222645 Trametes cinnabarina Species 0.000 description 2
- 241000222357 Trametes hirsuta Species 0.000 description 2
- 241000222355 Trametes versicolor Species 0.000 description 2
- 102000004357 Transferases Human genes 0.000 description 2
- 108090000992 Transferases Proteins 0.000 description 2
- UYXTWWCETRIEDR-UHFFFAOYSA-N Tributyrin Chemical compound CCCC(=O)OCC(OC(=O)CCC)COC(=O)CCC UYXTWWCETRIEDR-UHFFFAOYSA-N 0.000 description 2
- 241000223260 Trichoderma harzianum Species 0.000 description 2
- 241000378866 Trichoderma koningii Species 0.000 description 2
- 235000021307 Triticum Nutrition 0.000 description 2
- 244000098338 Triticum aestivum Species 0.000 description 2
- 102000014384 Type C Phospholipases Human genes 0.000 description 2
- 108010079194 Type C Phospholipases Proteins 0.000 description 2
- 241000266300 Ulocladium Species 0.000 description 2
- 240000006677 Vicia faba Species 0.000 description 2
- 235000010749 Vicia faba Nutrition 0.000 description 2
- 229920002000 Xyloglucan Polymers 0.000 description 2
- 241000235013 Yarrowia Species 0.000 description 2
- 241000758405 Zoopagomycotina Species 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 238000000246 agarose gel electrophoresis Methods 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 238000012867 alanine scanning Methods 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 101150078331 ama-1 gene Proteins 0.000 description 2
- 235000019257 ammonium acetate Nutrition 0.000 description 2
- 229940043376 ammonium acetate Drugs 0.000 description 2
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 239000008346 aqueous phase Substances 0.000 description 2
- 102000028848 arylesterase Human genes 0.000 description 2
- 108010009043 arylesterase Proteins 0.000 description 2
- 210000003050 axon Anatomy 0.000 description 2
- 229940097012 bacillus thuringiensis Drugs 0.000 description 2
- 239000010905 bagasse Substances 0.000 description 2
- 235000013361 beverage Nutrition 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 238000004061 bleaching Methods 0.000 description 2
- 239000004327 boric acid Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000004422 calculation algorithm Methods 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000006860 carbon metabolism Effects 0.000 description 2
- 230000036978 cell physiology Effects 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000002962 chemical mutagen Substances 0.000 description 2
- 210000003763 chloroplast Anatomy 0.000 description 2
- 238000011098 chromatofocusing Methods 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 239000013256 coordination polymer Substances 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 239000008121 dextrose Substances 0.000 description 2
- 238000002050 diffraction method Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000004821 distillation Methods 0.000 description 2
- 238000010410 dusting Methods 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 235000013399 edible fruits Nutrition 0.000 description 2
- 230000005672 electromagnetic field Effects 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 108010092413 endoglucanase V Proteins 0.000 description 2
- 239000003797 essential amino acid Substances 0.000 description 2
- 235000020776 essential amino acid Nutrition 0.000 description 2
- 238000001704 evaporation Methods 0.000 description 2
- 230000008020 evaporation Effects 0.000 description 2
- 108010038658 exo-1,4-beta-D-xylosidase Proteins 0.000 description 2
- 238000004880 explosion Methods 0.000 description 2
- 239000004744 fabric Substances 0.000 description 2
- 150000002191 fatty alcohols Chemical class 0.000 description 2
- 108010041969 feruloyl esterase Proteins 0.000 description 2
- 239000007850 fluorescent dye Substances 0.000 description 2
- 239000006260 foam Substances 0.000 description 2
- OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- HYBBIBNJHNGZAN-UHFFFAOYSA-N furfural Chemical compound O=CC1=CC=CO1 HYBBIBNJHNGZAN-UHFFFAOYSA-N 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 108010061330 glucan 1,4-alpha-maltohydrolase Proteins 0.000 description 2
- 150000004676 glycans Polymers 0.000 description 2
- 125000003147 glycosyl group Chemical group 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 229910052737 gold Inorganic materials 0.000 description 2
- 239000010931 gold Substances 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 238000001155 isoelectric focusing Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 238000007834 ligase chain reaction Methods 0.000 description 2
- 239000002029 lignocellulosic biomass Substances 0.000 description 2
- 210000001161 mammalian embryo Anatomy 0.000 description 2
- 238000012269 metabolic engineering Methods 0.000 description 2
- 230000037353 metabolic pathway Effects 0.000 description 2
- 108010020132 microbial serine proteinases Proteins 0.000 description 2
- 229920000847 nonoxynol Polymers 0.000 description 2
- 235000006408 oxalic acid Nutrition 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000006072 paste Substances 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 150000003905 phosphatidylinositols Chemical class 0.000 description 2
- 150000003904 phospholipids Chemical class 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 238000005222 photoaffinity labeling Methods 0.000 description 2
- 239000001965 potato dextrose agar Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 238000007639 printing Methods 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 235000013772 propylene glycol Nutrition 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 101150054232 pyrG gene Proteins 0.000 description 2
- LXNHXLLTXMVWPM-UHFFFAOYSA-N pyridoxine Chemical compound CC1=NC=C(CO)C(CO)=C1O LXNHXLLTXMVWPM-UHFFFAOYSA-N 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000010839 reverse transcription Methods 0.000 description 2
- 238000005096 rolling process Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000012807 shake-flask culturing Methods 0.000 description 2
- 150000004760 silicates Chemical class 0.000 description 2
- 239000000344 soap Substances 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000001694 spray drying Methods 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000011550 stock solution Substances 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 235000011044 succinic acid Nutrition 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 229910021654 trace metal Inorganic materials 0.000 description 2
- 238000011426 transformation method Methods 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 244000298073 white hoary pea Species 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- TXXHDPDFNKHHGW-UHFFFAOYSA-N (2E,4E)-2,4-hexadienedioic acid Natural products OC(=O)C=CC=CC(O)=O TXXHDPDFNKHHGW-UHFFFAOYSA-N 0.000 description 1
- AXVIQHWRLSFEAC-KNYJJKDQSA-N (2r,3s,4s,5s)-2,3,4,5,6-pentahydroxy-7-oxooctanal Chemical compound CC(=O)C(O)[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O AXVIQHWRLSFEAC-KNYJJKDQSA-N 0.000 description 1
- OCUSNPIJIZCRSZ-ZTZWCFDHSA-N (2s)-2-amino-3-methylbutanoic acid;(2s)-2-amino-4-methylpentanoic acid;(2s,3s)-2-amino-3-methylpentanoic acid Chemical compound CC(C)[C@H](N)C(O)=O.CC[C@H](C)[C@H](N)C(O)=O.CC(C)C[C@H](N)C(O)=O OCUSNPIJIZCRSZ-ZTZWCFDHSA-N 0.000 description 1
- JQFLYFRHDIHZFZ-RXMQYKEDSA-N (2s)-3,3-dimethylpyrrolidine-2-carboxylic acid Chemical compound CC1(C)CCN[C@@H]1C(O)=O JQFLYFRHDIHZFZ-RXMQYKEDSA-N 0.000 description 1
- CNPSFBUUYIVHAP-AKGZTFGVSA-N (2s)-3-methylpyrrolidine-2-carboxylic acid Chemical compound CC1CCN[C@@H]1C(O)=O CNPSFBUUYIVHAP-AKGZTFGVSA-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
- CEKUJDXLIOIGRR-JVLMNHKTSA-N (2z,4z)-6-methoxy-6-oxohexa-2,4-dienoic acid Chemical compound COC(=O)\C=C/C=C\C(O)=O CEKUJDXLIOIGRR-JVLMNHKTSA-N 0.000 description 1
- QGKMIGUHVLGJBR-UHFFFAOYSA-M (4z)-1-(3-methylbutyl)-4-[[1-(3-methylbutyl)quinolin-1-ium-4-yl]methylidene]quinoline;iodide Chemical compound [I-].C12=CC=CC=C2N(CCC(C)C)C=CC1=CC1=CC=[N+](CCC(C)C)C2=CC=CC=C12 QGKMIGUHVLGJBR-UHFFFAOYSA-M 0.000 description 1
- CGMACWYGXJQZQW-NGAQKLERSA-N (9Z,21Z,33Z)-3,15,27-triamino-7,19,31-trihydroxy-10,22,34-trimethyl-1,13,25-trioxa-7,19,31-triazacyclohexatriaconta-9,21,33-triene-2,8,14,20,26,32-hexone Chemical compound C/C/1=C/C(=O)N(CCCC(C(=O)OCC/C(=C\C(=O)N(CCCC(C(=O)OCC/C(=C\C(=O)N(CCCC(C(=O)OCC1)N)O)/C)N)O)/C)N)O CGMACWYGXJQZQW-NGAQKLERSA-N 0.000 description 1
- GHOKWGTUZJEAQD-ZETCQYMHSA-N (D)-(+)-Pantothenic acid Chemical compound OCC(C)(C)[C@@H](O)C(=O)NCCC(O)=O GHOKWGTUZJEAQD-ZETCQYMHSA-N 0.000 description 1
- PORPENFLTBBHSG-MGBGTMOVSA-N 1,2-dihexadecanoyl-sn-glycerol-3-phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(O)=O)OC(=O)CCCCCCCCCCCCCCC PORPENFLTBBHSG-MGBGTMOVSA-N 0.000 description 1
- VUDQSRFCCHQIIU-UHFFFAOYSA-N 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one Chemical compound CCCCCC(=O)C1=C(O)C(Cl)=C(OC)C(Cl)=C1O VUDQSRFCCHQIIU-UHFFFAOYSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- OMGHIGVFLOPEHJ-UHFFFAOYSA-N 2,5-dihydro-1h-pyrrol-1-ium-2-carboxylate Chemical compound OC(=O)C1NCC=C1 OMGHIGVFLOPEHJ-UHFFFAOYSA-N 0.000 description 1
- 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 1
- FUOOLUPWFVMBKG-UHFFFAOYSA-N 2-Aminoisobutyric acid Chemical compound CC(C)(N)C(O)=O FUOOLUPWFVMBKG-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- OSBLTNPMIGYQGY-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid;boric acid Chemical compound OB(O)O.OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O OSBLTNPMIGYQGY-UHFFFAOYSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- CDUUKBXTEOFITR-BYPYZUCNSA-N 2-methyl-L-serine Chemical compound OC[C@@]([NH3+])(C)C([O-])=O CDUUKBXTEOFITR-BYPYZUCNSA-N 0.000 description 1
- VMUXSMXIQBNMGZ-UHFFFAOYSA-N 3,4-dihydrocoumarin Chemical compound C1=CC=C2OC(=O)CCC2=C1 VMUXSMXIQBNMGZ-UHFFFAOYSA-N 0.000 description 1
- IITIZHOBOIBGBW-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole Chemical compound C1=CC=C2N(CC)CSC2=C1 IITIZHOBOIBGBW-UHFFFAOYSA-N 0.000 description 1
- 108010000816 3-oxoadipate enol-lactonase Proteins 0.000 description 1
- XQJMXPAEFMWDOZ-UHFFFAOYSA-N 3exo-benzoyloxy-tropane Natural products CN1C(C2)CCC1CC2OC(=O)C1=CC=CC=C1 XQJMXPAEFMWDOZ-UHFFFAOYSA-N 0.000 description 1
- PNBJAWCXUSYQNY-UHFFFAOYSA-N 4-(2-thiophen-2-ylthiophen-3-yl)but-3-ynyl acetate Chemical compound C1=CSC(C=2SC=CC=2)=C1C#CCCOC(=O)C PNBJAWCXUSYQNY-UHFFFAOYSA-N 0.000 description 1
- BTJIUGUIPKRLHP-UHFFFAOYSA-N 4-nitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-N 0.000 description 1
- 108010015134 4-pyridoxolactonase Proteins 0.000 description 1
- 101710163881 5,6-dihydroxyindole-2-carboxylic acid oxidase Proteins 0.000 description 1
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 1
- 102000001762 6-phosphogluconolactonase Human genes 0.000 description 1
- 101150104118 ANS1 gene Proteins 0.000 description 1
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 102100033639 Acetylcholinesterase Human genes 0.000 description 1
- 108091005508 Acid proteases Proteins 0.000 description 1
- 241001438625 Acremonium dichromosporum Species 0.000 description 1
- 241000228209 Acremonium persicinum Species 0.000 description 1
- 241001019292 Acremonium pinkertoniae Species 0.000 description 1
- 101100510736 Actinidia chinensis var. chinensis LDOX gene Proteins 0.000 description 1
- 241000186046 Actinomyces Species 0.000 description 1
- 241000607534 Aeromonas Species 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 241000589155 Agrobacterium tumefaciens Species 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010053754 Aldehyde reductase Proteins 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 240000000643 Alnus japonica Species 0.000 description 1
- 241000266330 Alternaria chartarum Species 0.000 description 1
- 241000584609 Alternaria consortialis Species 0.000 description 1
- 108091029845 Aminoallyl nucleotide Proteins 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 241000534414 Anotopterus nikparini Species 0.000 description 1
- 241000219194 Arabidopsis Species 0.000 description 1
- 241000219195 Arabidopsis thaliana Species 0.000 description 1
- 101710152845 Arabinogalactan endo-beta-1,4-galactanase Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 235000011330 Armoracia rusticana Nutrition 0.000 description 1
- 241000235349 Ascomycota Species 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000636501 Asparagus aspergillus Species 0.000 description 1
- 102000004580 Aspartic Acid Proteases Human genes 0.000 description 1
- 101000961203 Aspergillus awamori Glucoamylase Proteins 0.000 description 1
- 241000228197 Aspergillus flavus Species 0.000 description 1
- 241001480052 Aspergillus japonicus Species 0.000 description 1
- 101100157016 Aspergillus niger (strain CBS 513.88 / FGSC A1513) xlnC gene Proteins 0.000 description 1
- 101900127796 Aspergillus oryzae Glucoamylase Proteins 0.000 description 1
- 101900318521 Aspergillus oryzae Triosephosphate isomerase Proteins 0.000 description 1
- 241000228251 Aspergillus phoenicis Species 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 241000223678 Aureobasidium pullulans Species 0.000 description 1
- 244000075850 Avena orientalis Species 0.000 description 1
- 235000007319 Avena orientalis Nutrition 0.000 description 1
- 241000193375 Bacillus alcalophilus Species 0.000 description 1
- 241000193749 Bacillus coagulans Species 0.000 description 1
- 101000695691 Bacillus licheniformis Beta-lactamase Proteins 0.000 description 1
- 108010023063 Bacto-peptone Proteins 0.000 description 1
- 241000223679 Beauveria Species 0.000 description 1
- 240000000511 Berberis pumila Species 0.000 description 1
- 241000219310 Beta vulgaris subsp. vulgaris Species 0.000 description 1
- 101710104295 Beta-1,4-xylanase Proteins 0.000 description 1
- 102100030981 Beta-alanine-activating enzyme Human genes 0.000 description 1
- 241000222490 Bjerkandera Species 0.000 description 1
- 241000222478 Bjerkandera adusta Species 0.000 description 1
- 241000222455 Boletus Species 0.000 description 1
- 241001465180 Botrytis Species 0.000 description 1
- 235000011293 Brassica napus Nutrition 0.000 description 1
- 235000011299 Brassica oleracea var botrytis Nutrition 0.000 description 1
- 240000003259 Brassica oleracea var. botrytis Species 0.000 description 1
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 1
- 241000722885 Brettanomyces Species 0.000 description 1
- 241000589513 Burkholderia cepacia Species 0.000 description 1
- 101100327917 Caenorhabditis elegans chup-1 gene Proteins 0.000 description 1
- 244000025254 Cannabis sativa Species 0.000 description 1
- 102100037633 Centrin-3 Human genes 0.000 description 1
- 241000135254 Cephalosporium sp. Species 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
- 241000462056 Cestraeus plicatilis Species 0.000 description 1
- 241001581558 Cheiraster antarcticus Species 0.000 description 1
- 229920002101 Chitin Polymers 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- 206010008631 Cholera Diseases 0.000 description 1
- 102000003914 Cholinesterases Human genes 0.000 description 1
- 108090000322 Cholinesterases Proteins 0.000 description 1
- 241000233652 Chytridiomycota Species 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 241000588923 Citrobacter Species 0.000 description 1
- 241000588919 Citrobacter freundii Species 0.000 description 1
- 241000222290 Cladosporium Species 0.000 description 1
- 241001508813 Clavispora lusitaniae Species 0.000 description 1
- 241000193454 Clostridium beijerinckii Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 241000222680 Collybia Species 0.000 description 1
- 101000981560 Comamonas testosteroni 2-pyrone-4,6-dicarbaxylate hydrolase Proteins 0.000 description 1
- 241001236836 Coprinopsis friesii Species 0.000 description 1
- 244000234623 Coprinus comatus Species 0.000 description 1
- 235000001673 Coprinus macrorhizus Nutrition 0.000 description 1
- 229920000832 Cutin Polymers 0.000 description 1
- 108010025880 Cyclomaltodextrin glucanotransferase Proteins 0.000 description 1
- 240000008990 Cyperus javanicus Species 0.000 description 1
- 108050008072 Cytochrome c oxidase subunit IV Proteins 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- AUNGANRZJHBGPY-UHFFFAOYSA-N D-Lyxoflavin Natural products OCC(O)C(O)C(O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-UHFFFAOYSA-N 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102000016559 DNA Primase Human genes 0.000 description 1
- 108010092681 DNA Primase Proteins 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 244000033273 Dahlia variabilis Species 0.000 description 1
- LIOOJQZRNLJKMU-UHFFFAOYSA-N Demethyl coniferin Natural products OCC=Cc1ccc(OC2OC(CO)C(O)C(O)C2O)c(O)c1 LIOOJQZRNLJKMU-UHFFFAOYSA-N 0.000 description 1
- 241000224495 Dictyostelium Species 0.000 description 1
- 241000168726 Dictyostelium discoideum Species 0.000 description 1
- 101100342470 Dictyostelium discoideum pkbA gene Proteins 0.000 description 1
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 241000935926 Diplodia Species 0.000 description 1
- 241000607473 Edwardsiella <enterobacteria> Species 0.000 description 1
- 241000607471 Edwardsiella tarda Species 0.000 description 1
- 108010001817 Endo-1,4-beta Xylanases Proteins 0.000 description 1
- 101710132690 Endo-1,4-beta-xylanase A Proteins 0.000 description 1
- 101710147028 Endo-beta-1,4-galactanase Proteins 0.000 description 1
- 241001246273 Endothia Species 0.000 description 1
- 241000588914 Enterobacter Species 0.000 description 1
- 241000588697 Enterobacter cloacae Species 0.000 description 1
- 241000588698 Erwinia Species 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 101100385973 Escherichia coli (strain K12) cycA gene Proteins 0.000 description 1
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 description 1
- 239000005977 Ethylene Substances 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 101710112457 Exoglucanase Proteins 0.000 description 1
- 241000123326 Fomes Species 0.000 description 1
- 244000307700 Fragaria vesca Species 0.000 description 1
- 235000016623 Fragaria vesca Nutrition 0.000 description 1
- 235000011363 Fragaria x ananassa Nutrition 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 241000223194 Fusarium culmorum Species 0.000 description 1
- 101150108358 GLAA gene Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 101100001650 Geobacillus stearothermophilus amyM gene Proteins 0.000 description 1
- 239000005980 Gibberellic acid Substances 0.000 description 1
- 241001019284 Gliomastix roseogrisea Species 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010055629 Glucosyltransferases Proteins 0.000 description 1
- 102000000340 Glucosyltransferases Human genes 0.000 description 1
- 108010060309 Glucuronidase Proteins 0.000 description 1
- 102000053187 Glucuronidase Human genes 0.000 description 1
- 102000009127 Glutaminase Human genes 0.000 description 1
- 108010073324 Glutaminase Proteins 0.000 description 1
- 108010068370 Glutens Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 108700023372 Glycosyltransferases Proteins 0.000 description 1
- 102000051366 Glycosyltransferases Human genes 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 101150009006 HIS3 gene Proteins 0.000 description 1
- 101100295959 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) arcB gene Proteins 0.000 description 1
- 101100246753 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) pyrF gene Proteins 0.000 description 1
- 101000854529 Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) Pentonolactonase XacC Proteins 0.000 description 1
- 244000286779 Hansenula anomala Species 0.000 description 1
- 235000014683 Hansenula anomala Nutrition 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000773364 Homo sapiens Beta-alanine-activating enzyme Proteins 0.000 description 1
- 101000880522 Homo sapiens Centrin-3 Proteins 0.000 description 1
- 101001128911 Homo sapiens Neutral cholesterol ester hydrolase 1 Proteins 0.000 description 1
- 101001010890 Homo sapiens S-formylglutathione hydrolase Proteins 0.000 description 1
- 241000291718 Hoplocampa brevis Species 0.000 description 1
- 240000005979 Hordeum vulgare Species 0.000 description 1
- 235000007340 Hordeum vulgare Nutrition 0.000 description 1
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 1
- 239000004354 Hydroxyethyl cellulose Substances 0.000 description 1
- 229920000663 Hydroxyethyl cellulose Polymers 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 241000222342 Irpex Species 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- 241000588915 Klebsiella aerogenes Species 0.000 description 1
- 241000588749 Klebsiella oxytoca Species 0.000 description 1
- 241001138401 Kluyveromyces lactis Species 0.000 description 1
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- 125000001176 L-lysyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C([H])([H])C([H])([H])C(N([H])[H])([H])[H] 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- HXEACLLIILLPRG-YFKPBYRVSA-N L-pipecolic acid Chemical compound [O-]C(=O)[C@@H]1CCCC[NH2+]1 HXEACLLIILLPRG-YFKPBYRVSA-N 0.000 description 1
- DZLNHFMRPBPULJ-VKHMYHEASA-N L-thioproline Chemical compound OC(=O)[C@@H]1CSCN1 DZLNHFMRPBPULJ-VKHMYHEASA-N 0.000 description 1
- 125000000769 L-threonyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])[C@](O[H])(C([H])([H])[H])[H] 0.000 description 1
- KKJQZEWNZXRJFG-UHFFFAOYSA-N L-trans-4-Methyl-2-pyrrolidinecarboxylic acid Chemical compound CC1CNC(C(O)=O)C1 KKJQZEWNZXRJFG-UHFFFAOYSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 125000003798 L-tyrosyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H] 0.000 description 1
- 125000003580 L-valyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(C([H])([H])[H])(C([H])([H])[H])[H] 0.000 description 1
- 241000235087 Lachancea kluyveri Species 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 241001134659 Lactobacillus curvatus Species 0.000 description 1
- 101710094902 Legumin Proteins 0.000 description 1
- 241000222418 Lentinus Species 0.000 description 1
- 241000222118 Leptoxyphium fumago Species 0.000 description 1
- 229920002097 Lichenin Polymers 0.000 description 1
- 101710098556 Lipase A Proteins 0.000 description 1
- 101710098554 Lipase B Proteins 0.000 description 1
- 102100022119 Lipoprotein lipase Human genes 0.000 description 1
- 235000007688 Lycopersicon esculentum Nutrition 0.000 description 1
- 102100026001 Lysosomal acid lipase/cholesteryl ester hydrolase Human genes 0.000 description 1
- 101710099648 Lysosomal acid lipase/cholesteryl ester hydrolase Proteins 0.000 description 1
- 101150068888 MET3 gene Proteins 0.000 description 1
- 241001344133 Magnaporthe Species 0.000 description 1
- 241001344131 Magnaporthe grisea Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241000123318 Meripilus giganteus Species 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 241000223201 Metarhizium Species 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 102000016397 Methyltransferase Human genes 0.000 description 1
- 229920001340 Microbial cellulose Polymers 0.000 description 1
- 241001287972 Microthecium Species 0.000 description 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 description 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 description 1
- TXXHDPDFNKHHGW-CCAGOZQPSA-N Muconic acid Natural products OC(=O)\C=C/C=C\C(O)=O TXXHDPDFNKHHGW-CCAGOZQPSA-N 0.000 description 1
- 241000907556 Mucor hiemalis Species 0.000 description 1
- 241001149951 Mucor mucedo Species 0.000 description 1
- 101000723939 Mus musculus Transcription factor HIVEP3 Proteins 0.000 description 1
- 241001674208 Mycothermus thermophilus Species 0.000 description 1
- 241000223251 Myrothecium Species 0.000 description 1
- 241000863420 Myxococcus Species 0.000 description 1
- 241001647006 Myxococcus virescens Species 0.000 description 1
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 1
- OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 description 1
- WHNWPMSKXPGLAX-UHFFFAOYSA-N N-Vinyl-2-pyrrolidone Chemical compound C=CN1CCCC1=O WHNWPMSKXPGLAX-UHFFFAOYSA-N 0.000 description 1
- 108010063089 N-acetylgalactosaminoglycan deacetylase Proteins 0.000 description 1
- 102100023315 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase Human genes 0.000 description 1
- 108010056664 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase Proteins 0.000 description 1
- QQXLDOJGLXJCSE-UHFFFAOYSA-N N-methylnortropinone Natural products C1C(=O)CC2CCC1N2C QQXLDOJGLXJCSE-UHFFFAOYSA-N 0.000 description 1
- 241000233892 Neocallimastix Species 0.000 description 1
- 101100022915 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cys-11 gene Proteins 0.000 description 1
- 102100032087 Neutral cholesterol ester hydrolase 1 Human genes 0.000 description 1
- 108091005507 Neutral proteases Proteins 0.000 description 1
- 102000035092 Neutral proteases Human genes 0.000 description 1
- 108090000913 Nitrate Reductases Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- IOVCWXUNBOPUCH-UHFFFAOYSA-N Nitrous acid Chemical compound ON=O IOVCWXUNBOPUCH-UHFFFAOYSA-N 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 240000001439 Opuntia Species 0.000 description 1
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 1
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 1
- 102000007981 Ornithine carbamoyltransferase Human genes 0.000 description 1
- 101710113020 Ornithine transcarbamylase, mitochondrial Proteins 0.000 description 1
- 102100037214 Orotidine 5'-phosphate decarboxylase Human genes 0.000 description 1
- 108010055012 Orotidine-5'-phosphate decarboxylase Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000235647 Pachysolen tannophilus Species 0.000 description 1
- 241000194109 Paenibacillus lautus Species 0.000 description 1
- 101100317617 Paenibacillus sp. (strain JDR-2) xynA1 gene Proteins 0.000 description 1
- 241001236144 Panaeolus Species 0.000 description 1
- 241000310787 Panaeolus papilionaceus Species 0.000 description 1
- 102100033357 Pancreatic lipase-related protein 2 Human genes 0.000 description 1
- 241000588912 Pantoea agglomerans Species 0.000 description 1
- 241000830138 Pediomelum mephiticum Species 0.000 description 1
- 241001507683 Penicillium aurantiogriseum Species 0.000 description 1
- 241001123663 Penicillium expansum Species 0.000 description 1
- 241000222397 Phlebia radiata Species 0.000 description 1
- 102000006448 Phospholipases A1 Human genes 0.000 description 1
- 102000006447 Phospholipases A2 Human genes 0.000 description 1
- 102000004861 Phosphoric Diester Hydrolases Human genes 0.000 description 1
- 108090001050 Phosphoric Diester Hydrolases Proteins 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical class OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- 235000010582 Pisum sativum Nutrition 0.000 description 1
- 240000004713 Pisum sativum Species 0.000 description 1
- 244000252132 Pleurotus eryngii Species 0.000 description 1
- 235000001681 Pleurotus eryngii Nutrition 0.000 description 1
- 206010035664 Pneumonia Diseases 0.000 description 1
- 241000221945 Podospora Species 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- 229920002504 Poly(2-vinylpyridine-N-oxide) Polymers 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 108010059820 Polygalacturonase Proteins 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 241000588769 Proteus <enterobacteria> Species 0.000 description 1
- 241000588768 Providencia Species 0.000 description 1
- 241000588778 Providencia stuartii Species 0.000 description 1
- 241001236760 Psathyrella Species 0.000 description 1
- 241000168225 Pseudomonas alcaligenes Species 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- 241000589776 Pseudomonas putida Species 0.000 description 1
- 241000383853 Pseudoplectania nigrella Species 0.000 description 1
- QIZDQFOVGFDBKW-DHBOJHSNSA-N Pseudotropine Natural products OC1C[C@@H]2[N+](C)[C@H](C1)CC2 QIZDQFOVGFDBKW-DHBOJHSNSA-N 0.000 description 1
- 108020004518 RNA Probes Proteins 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 239000003391 RNA probe Substances 0.000 description 1
- 108091030071 RNAI Proteins 0.000 description 1
- 102000018120 Recombinases Human genes 0.000 description 1
- 108010091086 Recombinases Proteins 0.000 description 1
- 108050007056 Regucalcin Proteins 0.000 description 1
- 102100030262 Regucalcin Human genes 0.000 description 1
- 102100031176 Retinoid isomerohydrolase Human genes 0.000 description 1
- 241001361634 Rhizoctonia Species 0.000 description 1
- 101000968489 Rhizomucor miehei Lipase Proteins 0.000 description 1
- 241000593344 Rhizopus microsporus Species 0.000 description 1
- 241000872726 Rhizopus pusillus Species 0.000 description 1
- 241000235546 Rhizopus stolonifer Species 0.000 description 1
- 241000191043 Rhodobacter sphaeroides Species 0.000 description 1
- 241000190950 Rhodopseudomonas palustris Species 0.000 description 1
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 1
- 241000221523 Rhodotorula toruloides Species 0.000 description 1
- 241000193448 Ruminiclostridium thermocellum Species 0.000 description 1
- 102100029991 S-formylglutathione hydrolase Human genes 0.000 description 1
- 101900354623 Saccharomyces cerevisiae Galactokinase Proteins 0.000 description 1
- 101900084120 Saccharomyces cerevisiae Triosephosphate isomerase Proteins 0.000 description 1
- 235000018368 Saccharomyces fragilis Nutrition 0.000 description 1
- 241001407717 Saccharomyces norbensis Species 0.000 description 1
- 241000582914 Saccharomyces uvarum Species 0.000 description 1
- 240000000111 Saccharum officinarum Species 0.000 description 1
- 235000007201 Saccharum officinarum Nutrition 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 241000190542 Sarocladium kiliense Species 0.000 description 1
- 241000235060 Scheffersomyces stipitis Species 0.000 description 1
- 101100022918 Schizosaccharomyces pombe (strain 972 / ATCC 24843) sua1 gene Proteins 0.000 description 1
- 241000221662 Sclerotinia Species 0.000 description 1
- 241001558929 Sclerotium <basidiomycota> Species 0.000 description 1
- 241000223255 Scytalidium Species 0.000 description 1
- 235000007238 Secale cereale Nutrition 0.000 description 1
- 244000082988 Secale cereale Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 241000607720 Serratia Species 0.000 description 1
- 241000607715 Serratia marcescens Species 0.000 description 1
- 241000607768 Shigella Species 0.000 description 1
- 241000607762 Shigella flexneri Species 0.000 description 1
- 102100021837 Sialate O-acetylesterase Human genes 0.000 description 1
- 101710146043 Sinapine esterase Proteins 0.000 description 1
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
- 240000003768 Solanum lycopersicum Species 0.000 description 1
- 240000003829 Sorghum propinquum Species 0.000 description 1
- 235000011684 Sorghum saccharatum Nutrition 0.000 description 1
- 241000732549 Sphaerius Species 0.000 description 1
- 101000981565 Sphingobium sp. (strain NBRC 103272 / SYK-6) 2-pyrone-4,6-dicarboxylate hydrolase Proteins 0.000 description 1
- 241000228391 Sporidiobolus pararoseus Species 0.000 description 1
- 241000222068 Sporobolomyces <Sporidiobolaceae> Species 0.000 description 1
- 101000693619 Starmerella bombicola Lactone esterase Proteins 0.000 description 1
- 241000122973 Stenotrophomonas maltophilia Species 0.000 description 1
- 108010055297 Sterol Esterase Proteins 0.000 description 1
- 102000000019 Sterol Esterase Human genes 0.000 description 1
- 244000057717 Streptococcus lactis Species 0.000 description 1
- 235000014897 Streptococcus lactis Nutrition 0.000 description 1
- 101100309436 Streptococcus mutans serotype c (strain ATCC 700610 / UA159) ftf gene Proteins 0.000 description 1
- 241000187432 Streptomyces coelicolor Species 0.000 description 1
- 101100370749 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) trpC1 gene Proteins 0.000 description 1
- 241000187391 Streptomyces hygroscopicus Species 0.000 description 1
- 241000187181 Streptomyces scabiei Species 0.000 description 1
- 241000187094 Streptomyces thermoviolaceus Species 0.000 description 1
- 208000037065 Subacute sclerosing leukoencephalitis Diseases 0.000 description 1
- 206010042297 Subacute sclerosing panencephalitis Diseases 0.000 description 1
- 235000021536 Sugar beet Nutrition 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 239000008049 TAE buffer Substances 0.000 description 1
- 239000008051 TBE buffer Substances 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 241000228182 Thermoascus aurantiacus Species 0.000 description 1
- JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
- 241001495429 Thielavia terrestris Species 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 241000217816 Trametes villosa Species 0.000 description 1
- 241000223238 Trichophyton Species 0.000 description 1
- 241000223229 Trichophyton rubrum Species 0.000 description 1
- 240000001274 Trichosanthes villosa Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108060008724 Tyrosinase Proteins 0.000 description 1
- 102000003425 Tyrosinase Human genes 0.000 description 1
- 101150050575 URA3 gene Proteins 0.000 description 1
- 108090000848 Ubiquitin Proteins 0.000 description 1
- 102000044159 Ubiquitin Human genes 0.000 description 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- 241000235015 Yarrowia lipolytica Species 0.000 description 1
- 241000607734 Yersinia <bacteria> Species 0.000 description 1
- 241000607447 Yersinia enterocolitica Species 0.000 description 1
- 235000016383 Zea mays subsp huehuetenangensis Nutrition 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
- 238000010521 absorption reaction Methods 0.000 description 1
- 235000010489 acacia gum Nutrition 0.000 description 1
- 239000001785 acacia senegal l. willd gum Substances 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 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 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 108010075015 actinomycin lactonase Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 108010045649 agarase Proteins 0.000 description 1
- 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 1
- 239000012670 alkaline solution Substances 0.000 description 1
- 150000004996 alkyl benzenes Chemical class 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 150000008051 alkyl sulfates Chemical class 0.000 description 1
- 125000005466 alkylenyl group Chemical group 0.000 description 1
- 108010034561 alpha-amino acid esterase Proteins 0.000 description 1
- 108010061261 alpha-glucuronidase Proteins 0.000 description 1
- CDUUKBXTEOFITR-UHFFFAOYSA-N alpha-methylserine Natural products OCC([NH3+])(C)C([O-])=O CDUUKBXTEOFITR-UHFFFAOYSA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 150000001414 amino alcohols Chemical class 0.000 description 1
- 108010073901 aminoacyl-tRNA hydrolase Proteins 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 239000000908 ammonium hydroxide Substances 0.000 description 1
- 238000012197 amplification kit Methods 0.000 description 1
- 230000003625 amylolytic effect Effects 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000433 anti-nutritional effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 101150009206 aprE gene Proteins 0.000 description 1
- 229920000617 arabinoxylan Polymers 0.000 description 1
- 101150008194 argB gene Proteins 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 229910052786 argon Inorganic materials 0.000 description 1
- 238000003491 array Methods 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- 229940054340 bacillus coagulans Drugs 0.000 description 1
- 101150103518 bar gene Proteins 0.000 description 1
- 239000007640 basal medium Substances 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 239000003659 bee venom Substances 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 229940077388 benzenesulfonate Drugs 0.000 description 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 1
- 125000000188 beta-D-glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 108010049297 beta-L-arabinosidase Proteins 0.000 description 1
- AFYNADDZULBEJA-UHFFFAOYSA-N bicinchoninic acid Chemical compound C1=CC=CC2=NC(C=3C=C(C4=CC=CC=C4N=3)C(=O)O)=CC(C(O)=O)=C21 AFYNADDZULBEJA-UHFFFAOYSA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 230000009141 biological interaction Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 238000013452 biotechnological production Methods 0.000 description 1
- 230000036983 biotransformation Effects 0.000 description 1
- 108010042769 bis(2-ethylhexyl)phthalate esterase Proteins 0.000 description 1
- 239000007844 bleaching agent Substances 0.000 description 1
- 238000005282 brightening Methods 0.000 description 1
- CDQSJQSWAWPGKG-UHFFFAOYSA-N butane-1,1-diol Chemical compound CCCC(O)O CDQSJQSWAWPGKG-UHFFFAOYSA-N 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 238000005251 capillar electrophoresis Methods 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 150000004649 carbonic acid derivatives Chemical class 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 101150052795 cbh-1 gene Proteins 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
- 239000006285 cell suspension Substances 0.000 description 1
- FYGDTMLNYKFZSV-ZWSAEMDYSA-N cellotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-ZWSAEMDYSA-N 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 108010025790 chlorophyllase Proteins 0.000 description 1
- 229940048961 cholinesterase Drugs 0.000 description 1
- 150000001860 citric acid derivatives Chemical class 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000003749 cleanliness Effects 0.000 description 1
- 239000005515 coenzyme Substances 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 239000008139 complexing agent Substances 0.000 description 1
- SFLMUHDGSQZDOW-FAOXUISGSA-N coniferin Chemical compound COC1=CC(\C=C\CO)=CC=C1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 SFLMUHDGSQZDOW-FAOXUISGSA-N 0.000 description 1
- LIOOJQZRNLJKMU-UXXRCYHCSA-N coniferin Natural products OCC=Cc1ccc(O[C@@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)c(O)c1 LIOOJQZRNLJKMU-UXXRCYHCSA-N 0.000 description 1
- SFLMUHDGSQZDOW-IBEHDNSVSA-N coniferoside Natural products COC1=CC(C=CCO)=CC=C1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 SFLMUHDGSQZDOW-IBEHDNSVSA-N 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000006059 cover glass Substances 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 101150005799 dagA gene Proteins 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 238000007405 data analysis Methods 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- NLNLACOJSWLNHE-DYNITIQCSA-N deoxylimonoic acid Chemical compound C=1([C@@H]2OC(=O)CC3=C([C@H](CC[C@]32C)[C@]23[C@H](CC(=O)OC2)OC(C)(C)[C@@H]3CC(O)=O)C)C=COC=1 NLNLACOJSWLNHE-DYNITIQCSA-N 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 150000001982 diacylglycerols Chemical class 0.000 description 1
- GSPKZYJPUDYKPI-UHFFFAOYSA-N diethoxy sulfate Chemical compound CCOOS(=O)(=O)OOCC GSPKZYJPUDYKPI-UHFFFAOYSA-N 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 1
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 1
- DMSHWWDRAYHEBS-UHFFFAOYSA-N dihydrocoumarin Natural products C1CC(=O)OC2=C1C=C(OC)C(OC)=C2 DMSHWWDRAYHEBS-UHFFFAOYSA-N 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 239000001177 diphosphate Substances 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical class [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 238000004851 dishwashing Methods 0.000 description 1
- NEKNNCABDXGBEN-UHFFFAOYSA-L disodium;4-(4-chloro-2-methylphenoxy)butanoate;4-(2,4-dichlorophenoxy)butanoate Chemical compound [Na+].[Na+].CC1=CC(Cl)=CC=C1OCCCC([O-])=O.[O-]C(=O)CCCOC1=CC=C(Cl)C=C1Cl NEKNNCABDXGBEN-UHFFFAOYSA-L 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- GMSCBRSQMRDRCD-UHFFFAOYSA-N dodecyl 2-methylprop-2-enoate Chemical compound CCCCCCCCCCCCOC(=O)C(C)=C GMSCBRSQMRDRCD-UHFFFAOYSA-N 0.000 description 1
- 230000035622 drinking Effects 0.000 description 1
- 238000002003 electron diffraction Methods 0.000 description 1
- 210000002257 embryonic structure Anatomy 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 108010091371 endoglucanase 1 Proteins 0.000 description 1
- 108010091384 endoglucanase 2 Proteins 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 210000002615 epidermis Anatomy 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- 239000000262 estrogen Substances 0.000 description 1
- 229940011871 estrogen Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- IKUQEFGEUOOPGY-UHFFFAOYSA-N euoniside Natural products COC1=CC=2C=CC(=O)OC=2C(OC)=C1OC1OC(CO)C(O)C(O)C1O IKUQEFGEUOOPGY-UHFFFAOYSA-N 0.000 description 1
- 108010000165 exo-1,3-alpha-glucanase Proteins 0.000 description 1
- 108010093305 exopolygalacturonase Proteins 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000002979 fabric softener Substances 0.000 description 1
- 235000019387 fatty acid methyl ester Nutrition 0.000 description 1
- 108010063260 fatty acyl ethyl ester synthase Proteins 0.000 description 1
- 150000002190 fatty acyls Chemical group 0.000 description 1
- 238000012262 fermentative production Methods 0.000 description 1
- 235000021001 fermented dairy product Nutrition 0.000 description 1
- 229940114123 ferulate Drugs 0.000 description 1
- KSEBMYQBYZTDHS-HWKANZROSA-M ferulate Chemical compound COC1=CC(\C=C\C([O-])=O)=CC=C1O KSEBMYQBYZTDHS-HWKANZROSA-M 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 108010011505 fluorescein-avidin Proteins 0.000 description 1
- 229960000304 folic acid Drugs 0.000 description 1
- 235000019152 folic acid Nutrition 0.000 description 1
- 239000011724 folic acid Substances 0.000 description 1
- KFIFDKLIFPYSAZ-UHFFFAOYSA-N formyloxy(phenyl)borinic acid Chemical compound O=COB(O)C1=CC=CC=C1 KFIFDKLIFPYSAZ-UHFFFAOYSA-N 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 239000000417 fungicide Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000012224 gene deletion Methods 0.000 description 1
- 230000009368 gene silencing by RNA Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000035784 germination Effects 0.000 description 1
- IXORZMNAPKEEDV-UHFFFAOYSA-N gibberellic acid GA3 Natural products OC(=O)C1C2(C3)CC(=C)C3(O)CCC2C2(C=CC3O)C1C3(C)C(=O)O2 IXORZMNAPKEEDV-UHFFFAOYSA-N 0.000 description 1
- IXORZMNAPKEEDV-OBDJNFEBSA-N gibberellin A3 Chemical compound C([C@@]1(O)C(=C)C[C@@]2(C1)[C@H]1C(O)=O)C[C@H]2[C@]2(C=C[C@@H]3O)[C@H]1[C@]3(C)C(=O)O2 IXORZMNAPKEEDV-OBDJNFEBSA-N 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229960002442 glucosamine Drugs 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- MNQZXJOMYWMBOU-UHFFFAOYSA-N glyceraldehyde Chemical compound OCC(O)C=O MNQZXJOMYWMBOU-UHFFFAOYSA-N 0.000 description 1
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 1
- 210000005255 gram-positive cell Anatomy 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 229940093915 gynecological organic acid Drugs 0.000 description 1
- 125000001475 halogen functional group Chemical group 0.000 description 1
- 238000010438 heat treatment Methods 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
- 150000002431 hydrogen Chemical class 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 239000003752 hydrotrope Substances 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 108010008510 hydroxybutyrate-dimer hydrolase Proteins 0.000 description 1
- 235000019447 hydroxyethyl cellulose Nutrition 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 108010002685 hygromycin-B kinase Proteins 0.000 description 1
- 150000003949 imides Chemical class 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 229910017053 inorganic salt Inorganic materials 0.000 description 1
- 229960000367 inositol Drugs 0.000 description 1
- CDAISMWEOUEBRE-GPIVLXJGSA-N inositol Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O CDAISMWEOUEBRE-GPIVLXJGSA-N 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- GCHPUFAZSONQIV-UHFFFAOYSA-N isovaline Chemical compound CCC(C)(N)C(O)=O GCHPUFAZSONQIV-UHFFFAOYSA-N 0.000 description 1
- 108010080576 juvenile hormone esterase Proteins 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 229940031154 kluyveromyces marxianus Drugs 0.000 description 1
- HXEACLLIILLPRG-RXMQYKEDSA-N l-pipecolic acid Natural products OC(=O)[C@H]1CCCCN1 HXEACLLIILLPRG-RXMQYKEDSA-N 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 239000010985 leather Substances 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000021374 legumes Nutrition 0.000 description 1
- 239000012978 lignocellulosic material Substances 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- YFVGRULMIQXYNE-UHFFFAOYSA-M lithium;dodecyl sulfate Chemical compound [Li+].CCCCCCCCCCCCOS([O-])(=O)=O YFVGRULMIQXYNE-UHFFFAOYSA-M 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 101150039489 lysZ gene Proteins 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 235000009973 maize Nutrition 0.000 description 1
- VZCYOOQTPOCHFL-UPHRSURJSA-N maleic acid Chemical compound OC(=O)\C=C/C(O)=O VZCYOOQTPOCHFL-UPHRSURJSA-N 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 238000013178 mathematical model Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 238000010208 microarray analysis Methods 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 238000003801 milling Methods 0.000 description 1
- 210000003470 mitochondria Anatomy 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229940045641 monobasic sodium phosphate Drugs 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 1
- 235000019799 monosodium phosphate Nutrition 0.000 description 1
- 239000004570 mortar (masonry) Substances 0.000 description 1
- 239000003471 mutagenic agent Substances 0.000 description 1
- 239000006199 nebulizer Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 101150095344 niaD gene Proteins 0.000 description 1
- 235000001968 nicotinic acid Nutrition 0.000 description 1
- 229960003512 nicotinic acid Drugs 0.000 description 1
- 239000011664 nicotinic acid Substances 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- SNQQPOLDUKLAAF-UHFFFAOYSA-N nonylphenol Chemical class CCCCCCCCCC1=CC=CC=C1O SNQQPOLDUKLAAF-UHFFFAOYSA-N 0.000 description 1
- 101150105920 npr gene Proteins 0.000 description 1
- 101150017837 nprM gene Proteins 0.000 description 1
- 239000012038 nucleophile Substances 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 235000014593 oils and fats Nutrition 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- AHLBNYSZXLDEJQ-FWEHEUNISA-N orlistat Chemical compound CCCCCCCCCCC[C@H](OC(=O)[C@H](CC(C)C)NC=O)C[C@@H]1OC(=O)[C@H]1CCCCCC AHLBNYSZXLDEJQ-FWEHEUNISA-N 0.000 description 1
- 229960003104 ornithine Drugs 0.000 description 1
- 108090000021 oryzin Proteins 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 108010001073 oxyhemoglobin oxidase Proteins 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 229940014662 pantothenate Drugs 0.000 description 1
- 235000019161 pantothenic acid Nutrition 0.000 description 1
- 239000011713 pantothenic acid Substances 0.000 description 1
- 108020004410 pectinesterase Proteins 0.000 description 1
- 101150019841 penP gene Proteins 0.000 description 1
- 150000002972 pentoses Chemical class 0.000 description 1
- 210000002824 peroxisome Anatomy 0.000 description 1
- 150000004965 peroxy acids Chemical class 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- JTJMJGYZQZDUJJ-UHFFFAOYSA-N phencyclidine Chemical compound C1CCCCN1C1(C=2C=CC=CC=2)CCCCC1 JTJMJGYZQZDUJJ-UHFFFAOYSA-N 0.000 description 1
- OSCBARYHPZZEIS-UHFFFAOYSA-N phenoxyboronic acid Chemical class OB(O)OC1=CC=CC=C1 OSCBARYHPZZEIS-UHFFFAOYSA-N 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000002644 phorbol ester Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- 108010082527 phosphinothricin N-acetyltransferase Proteins 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 239000003375 plant hormone Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920002006 poly(N-vinylimidazole) polymer Polymers 0.000 description 1
- 229920000196 poly(lauryl methacrylate) Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920005646 polycarboxylate Polymers 0.000 description 1
- 229920002643 polyglutamic acid Polymers 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 108060006613 prolamin Proteins 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000020978 protein processing Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 101150108007 prs gene Proteins 0.000 description 1
- 101150086435 prs1 gene Proteins 0.000 description 1
- 101150070305 prsA gene Proteins 0.000 description 1
- 235000008160 pyridoxine Nutrition 0.000 description 1
- 239000011677 pyridoxine Substances 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000000985 reactive dye Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 108010054126 retinoid isomerohydrolase Proteins 0.000 description 1
- 235000019172 retinyl palmitate Nutrition 0.000 description 1
- 239000011769 retinyl palmitate Substances 0.000 description 1
- 229940108325 retinyl palmitate Drugs 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 235000019192 riboflavin Nutrition 0.000 description 1
- 229960002477 riboflavin Drugs 0.000 description 1
- 239000002151 riboflavin Substances 0.000 description 1
- 101150025220 sacB gene Proteins 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- CDAISMWEOUEBRE-UHFFFAOYSA-N scyllo-inosotol Natural products OC1C(O)C(O)C(O)C(O)C1O CDAISMWEOUEBRE-UHFFFAOYSA-N 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 108010015572 sialate O-acetylesterase Proteins 0.000 description 1
- 235000021309 simple sugar Nutrition 0.000 description 1
- RYMZZMVNJRMUDD-HGQWONQESA-N simvastatin Chemical compound C([C@H]1[C@@H](C)C=CC2=C[C@H](C)C[C@@H]([C@H]12)OC(=O)C(C)(C)CC)C[C@@H]1C[C@@H](O)CC(=O)O1 RYMZZMVNJRMUDD-HGQWONQESA-N 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 239000003998 snake venom Substances 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
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
- FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
- 229940048086 sodium pyrophosphate Drugs 0.000 description 1
- AHXBFYVJAJSQKV-UHFFFAOYSA-M sodium;3-(cyclohexylamino)propane-1-sulfonic acid;hydroxide Chemical compound [OH-].[Na+].OS(=O)(=O)CCCNC1CCCCC1 AHXBFYVJAJSQKV-UHFFFAOYSA-M 0.000 description 1
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 1
- 238000010563 solid-state fermentation Methods 0.000 description 1
- 239000000021 stimulant Substances 0.000 description 1
- 239000010902 straw Substances 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 1
- 239000001384 succinic acid Substances 0.000 description 1
- 235000021092 sugar substitutes Nutrition 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 150000003457 sulfones Chemical class 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 108010038851 tannase Proteins 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- FRPJTGXMTIIFIT-UHFFFAOYSA-N tetraacetylethylenediamine Chemical compound CC(=O)C(N)(C(C)=O)C(N)(C(C)=O)C(C)=O FRPJTGXMTIIFIT-UHFFFAOYSA-N 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 235000019818 tetrasodium diphosphate Nutrition 0.000 description 1
- 239000001577 tetrasodium phosphonato phosphate Substances 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000005809 transesterification reaction Methods 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- 125000005457 triglyceride group Chemical group 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- CYHOMWAPJJPNMW-JIGDXULJSA-N tropine Chemical compound C1[C@@H](O)C[C@H]2CC[C@@H]1N2C CYHOMWAPJJPNMW-JIGDXULJSA-N 0.000 description 1
- 101150016309 trpC gene Proteins 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- WFKWXMTUELFFGS-UHFFFAOYSA-N tungsten Chemical compound [W] WFKWXMTUELFFGS-UHFFFAOYSA-N 0.000 description 1
- 229910052721 tungsten Inorganic materials 0.000 description 1
- 239000010937 tungsten Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000000870 ultraviolet spectroscopy Methods 0.000 description 1
- 241001148471 unidentified anaerobic bacterium Species 0.000 description 1
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 1
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 1
- 108010086346 uronolactonase Proteins 0.000 description 1
- 210000003934 vacuole Anatomy 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 239000000052 vinegar Substances 0.000 description 1
- 235000021419 vinegar Nutrition 0.000 description 1
- 235000019155 vitamin A Nutrition 0.000 description 1
- 239000011719 vitamin A Substances 0.000 description 1
- 235000019156 vitamin B Nutrition 0.000 description 1
- 239000011720 vitamin B Substances 0.000 description 1
- 235000019154 vitamin C Nutrition 0.000 description 1
- 239000011718 vitamin C Substances 0.000 description 1
- 235000019166 vitamin D Nutrition 0.000 description 1
- 239000011710 vitamin D Substances 0.000 description 1
- 235000019165 vitamin E Nutrition 0.000 description 1
- 239000011709 vitamin E Substances 0.000 description 1
- 229940011671 vitamin b6 Drugs 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
- 108010062040 wax-ester hydrolase Proteins 0.000 description 1
- 101150091506 xynA gene Proteins 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000004711 α-olefin Substances 0.000 description 1
Images
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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/37—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from fungi
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
-
- 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
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8243—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine
- C12N15/8245—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine involving modified carbohydrate or sugar alcohol metabolism, e.g. starch biosynthesis
- C12N15/8246—Non-starch polysaccharides, e.g. cellulose, fructans, levans
-
- 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
- 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
- C12N9/244—Endo-1,3(4)-beta-glucanase (3.2.1.6)
-
- 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
- C12N9/2445—Beta-glucosidase (3.2.1.21)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/02—Monosaccharides
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
- C12P7/04—Preparation of oxygen-containing organic compounds containing a hydroxy group acyclic
- C12P7/06—Ethanol, i.e. non-beverage
- C12P7/08—Ethanol, i.e. non-beverage produced as by-product or from waste or cellulosic material substrate
- C12P7/10—Ethanol, i.e. non-beverage produced as by-product or from waste or cellulosic material substrate substrate containing cellulosic material
-
- 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)
- C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
-
- 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)
- C12Y302/01006—Endo-1,3(4)-beta-glucanase (3.2.1.6)
-
- 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)
- C12Y302/01021—Beta-glucosidase (3.2.1.21)
-
- 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)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
- Y02E50/00—Technologies for the production of fuel of non-fossil origin
- Y02E50/10—Biofuels, e.g. bio-diesel
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- Nutrition Science (AREA)
- Biophysics (AREA)
- General Chemical & Material Sciences (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Cell Biology (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Gastroenterology & Hepatology (AREA)
- Mycology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Detergent Compositions (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
【解決手段】セルロース分解増強活性を有する単離されたポリペプチド、及び前記ポリペプチドをコードする単離された核酸、および、前記核酸を含んで成る、核酸構造体、ベクター及び宿主細胞。前記ポリペプチドの生成方法及び有効量のセルロース分解タンパク質と有効量の前記ポリペプチドの存在下でセルロース材料を糖化し、糖化されたセルロース材料を、1又は複数の発酵微生物と共に発酵し、有機物質を回収することを含んで成る、有機物質の生成方法。
【選択図】なし
Description
本発明は、セルロース分解増強活性を有する単離されたポリペプチド、及び前記ポリペプチドをコードする単離されたポリヌクレオチドに関する。本発明はまた、前記ポリヌクレオチドを含んで成る、核酸構造体、ベクター及び宿主細胞、及び前記ポリペプチドの生成及び使用方法にも関する。
セルロースは、β−1,4−結合により共有結合される単純糖グルコースのポリマーである。多くの微生物は、β−結合されたグルカンを加水分解する酵素を生成する。それらの酵素は、エンドグルカナーゼ、セロビオビドロラーゼ、及びβ−グルコシダーゼを包含する。エンドグルカナーゼは、セルロースポリマーをランダム位置で消化し、それを、セロビオヒドロラーゼによる攻撃に開放する。セロビオヒドロラーゼは、セルロースポリマーの末端からセロビオースの分子を連続的に開放する。セロビオースは、グルコースの水溶性β−1,4−結合されたダイマーである。β−グルコシダーゼは、セロビオースをグルコースに加水分解する。
セルロース分解増強活性を有する単離されたポリペプチド、及び前記ポリペプチドをコードする単離された核酸配列を、セルロース性供給原料の転換性を改良するために供給することが、本発明の目的である。
本発明は、
(a)配列番号2のアミノ酸23〜250と少なくとも70%の同一性を有するアミノ酸配列を有するポリペプチド;
(b)(i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、少なくとも中位の緊縮条件下でハイブリダイズする核酸配列によりコードされるポリペプチド;及び
(c)配列番号2のアミノ酸23〜250の1又は複数のアミノ酸の保存性置換、欠失及び/又は挿入を含んで成る変異体から成る群から選択された、セルロース分解増強活性を有する単離されたポリペプチドに関する。
(a)配列番号2のアミノ酸23〜250と少なくとも70%の同一性を有するアミノ酸配列を有するポリペプチドをコードするポリヌクレオチド;
(b)配列番号1のヌクレオチド67〜805と少なくとも70%の同一性を有するポリヌクレオチド;及び
(c)(i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、少なくとも中位の緊縮条件下でハイブリダイズするポリヌクレオチドから成る群から選択された、セルロース分解増強活性を有するポリペプチドをコードする単離されたポリヌクレオチドにも関する。
本発明はまた、(a)セルロース分解増強活性を有するポリペプチドをコードするポリヌクレオチドを含んで成る核酸構造体を含んで成る組換え宿主細胞を、前記ポリペプチドの生成の助けと成る条件下で培養し;そして(b)前記ポリペプチドを回収することを含んで成る方法にも関する。
本発明はまた、セルロース材料を分解するか又は転換するための方法にも関し、ここで前記セルロース材料を、有効量のセルロース分解タンパク質により、セルロース分解増強活性を有する、有効量のポリペプチドの存在下で処理し、ここで前記セルロース分解増強活性を有するポリペプチドの存在が、セルロース分解増強活性を有するポリペプチドの不在に比較して、セルロース材料の分解を高める。
(a)セルロース材料を、有効量のセルロース分解タンパク質により、セルロース分解増強活性を有する、有効量のポリペプチドの存在下で糖化し、ここで前記セルロース分解増強活性を有するポリペプチドの存在が、セルロース分解増強活性を有するポリペプチドの不在に比較して、セルロース材料の分解を高め;
(b)段階(a)の糖化されたセルロース材料を、1又は複数の発酵微生物と共に発酵し;そして
(c)前記酵素から有機物質を回収することを含んで成る、有機物質の生成方法にも関する。
セルロース分解増強活性:この用語“セルロース分解増強活性”とは、セルロース分解活性を有するタンパク質による、セルロース材料の加水分解を増強する生物学的活性として、本明細書において定義され得る。本発明のためには、セルロース分解増強活性は、セルロース分解増強活性を有さない等しい合計タンパク質負荷による対照加水分解に比較して(5.01〜7.5mgのセルロース分解タンパク質/PCS中、1gのセルロース)、次の条件下でセルロース分解タンパク質によるセルロース材料の加水分解からの還元糖の上昇を測定することにより決定される: PCS中、1gのセルロース当たり0.01〜2.5mgのセルロース分解増強活性の存在又は不在下での、50℃で5〜7日間の、PCS中、1gのセルロース当たり5.0mgのセルロース分解タンパク質。好ましい態様においては、この後、Tr/AoBGと呼ばれ、そしてNovozymes A/S, Bagsvoerd, Denmarkから得られた、アスペルギラス・オリザエ(WO02/095014)号からのβ−グルコシダーゼを発現するトリコダーマ・レセイの発酵に由来する、セルラーゼタンパク質負荷のセルラーゼ調製物が、セルロース分解活性の源として使用される。
ここで、用語“実質的に純粋なポリペプチド”は、用語“単離されたポリペプチド”及び“単離された形のポリペプチド”と類似語である。
本発明のためには、2種のアミノ酸配列間の同一性の程度は、Paracel BioView Workbench ソフトウエアー(Paracel, Pasadena, CA)及びblosum62を用いて、blastpアルゴリズム(Higgins, 1989, CABIOS 5: 151- 153)により決定され得る。ギャップペナルティー、存在:11及び延長:1が、対様アリグメントパラメーターとして使用された。
コード配列:本明細書において使用される場合、用語“コード配列”とは、そのタンパク質生成物のアミノ酸配列を直接的に特定するヌクレオチド配列を包含する。コード配列の境界は一般的に、ATG開始コドン、又は他の開始コドン、例えばGTG及びTTGにより通常、開始し、そしてTAA、TAG及びTGAにより終結する読み取り枠により決定される。コード配列は、DNA、cDNA及び組換えヌクレオチドを包含する。
発現ベクター:本発明においては、用語“発現ベクター”とは、本発明のポリペプチドをコードするポリヌクレオチドを含んで成り、そしてその発現を提供する追加のヌクレオチドに作用可能に結合される、線状又は環状のDNA分子を包含する。
修飾:用語“修飾”とは、配列番号2のアミノ酸23〜250を含んで成るか、又はそれらから成るポリペプチド、又はそれらの相同配列のいずれかの化学的修飾、及び前記ポリペプチドをコードするDNAの遺伝子操作を、本明細書においては意味する。修飾は、1又は複数のアミノ酸の置換、欠失及び/又は挿入、及び1又は複数のアミノ酸側鎖の置換であり得る。
セルロース分解増強活性を有するポリペプチド:
第1の観点においては、本発明は、配列番号2(すなわち、成熟ポリペプチド)のアミノ酸23〜250に対して、少なくとも70%、好ましくは少なくとも75%、より好ましくは少なくとも80%、より好ましくは少なくとも85%、さらに好ましくは少なくとも90%、最も好ましくは少なくとも95%、及びさらに最も好ましくは少なくとも97%、98%又は99%の程度を有するアミノ酸配列を有する単離されたポリペプチド(セルロース分解増強活性を有する)(この後、“相同ポリペプチドと称する)に関する。好ましい観点においては、相同ポリペプチドは、配列番号2のアミノ酸23〜250とは、10個までのアミノ酸、好ましくは5個までのアミノ酸、より好ましくは4個までのアミノ酸、さらにより好ましくは3個までのアミノ酸、最も好ましくは2個までのアミノ酸、及びさらに最も好ましくは1個までのアミノ酸で異なるアミノ酸配列を有する。
本発明のポリペプチドは、いずれかの属の微生物から得られる。本発明のためには、用語“〜から得られる”とは、所定の源に関して本明細書において使用される場合、ヌクレオチド配列によりコードされるポリペプチドが前記源により、又は前記源からのヌクレオチド配列によりコードされるポリペプチドが前記源により、又は前記源からのヌクレオチド配列が、挿入されている株により生成されることを意味する。好ましい観点においては、所定の減から得られるポリペプチドは、細胞内分泌される。
前述の種に関しては、本発明は完全及び不完全状態の両者、及び他の分類学的同等物、例えばアナモルフを、それらが知られている種の名称にかかわらず、包含することが理解されるであろう。当業者は適切な同等物の正体を容易に理解するであろう。
本発明はまた、本発明のポリペプチドをコードするヌクレオチド配列を有する単離されたポリヌクレオチドにも関する。
本発明はまた、適切な宿主細胞におけるコード配列の発現を、制御配列と適合できる条件下で指図する、1又は複数の制御配列に作用可能に結合される本発明の単離されたポリヌクレオチドを含んで成る核酸構造体に関する。
本発明のポリペプチドをコードする単離されたポリヌクレオチドは、ポリペプチドの発現を提供するために種々の手段で操作され得る。ベクター中へのその挿入の前、ポリヌクレオチドの操作は、発現ベクターに依存して、所望されるか又は必要とされる。組換えDNA方法を用いてポリヌクレオチドを修飾するための技法は、当業界において良く知られている。
糸状菌宿主細胞のための好ましいリーダーは、アスペルギラス・オリザエTAKAアミラーゼ、アスペルギラス・ニジュランストリオースリン酸イソメラーゼについての遺伝子から得られる。
酵母宿主細胞のための有用なポリアデニル化配列は、Guo and Sherman, 1995, Molecular Cellular Biology 15: 5983-5990により記載されている。
酵母宿主細胞のための有用なシグナルペプチドは、サッカロミセス・セレビシアエα−因子及びサッカロミセル・セレビシアエインバーターゼについての遺伝子から得られる。他の有用なシグナルペプチドコード領域は、Romanos など., 1992, 前記により記載される。
本発明はまた、本発明のポリヌクレオチド、プロモーター、及び転写及び翻訳停止シグナルを含んで成る組換え発現ベクターにも関する。上記の種々の核酸及び制御配列は、1又は複数の便利な制限部位でポリペプチドをコードするヌクレオチド配列の挿入又は置換を可能にするためにそれらの部位を含むことができる組換え発現ベクターを生成するために一緒に連結され得る。他方では、本発明のポリヌクレオチド配列は、前記配列又は前記配列を含んで成る核酸構造体を、発現のための適切なベクター中に挿入することによって発現され得る。発現ベクターを創造する場合、そのコード配列はベクターに位置し、その結果、コード配列は発現のための適切な制御配列により作用可能に連結される。
酵母宿主細胞への使用のための複製の起点の例は、複製の2ミクロン起点、すなわちARS1, ARS4, ARS1及びCEN3の組み合わせ、及びARS4及びCEN6の組み合わせである。
本発明の組換え発現ベクターを構成するために上記要素を連結するために使用される方法は、当業者に良く知られている(例えば、Sambrookなど., 1989, 前記を参照のこと)。
本発明はまた、ポリペプチドの組換え生成において都合良く使用される、本発明のポリヌクレオチドを含んで成る組換え宿主にも関する。本発明のポリヌクレオチドを含んでなるベクターは、そのベクターが染色体組み込み体として、又は前記のような自己複製染色体外ベクターとして維持されるように、宿主細胞中に導入される。用語“宿主細胞”とは、複製の間に生じる突然変異のために、親細胞と同一ではない親細胞のいずれかの子孫を包含する。宿主細胞の選択は、ポリペプチドをコードする遺伝子及びその源に、かなりの程度依存するであろう。
宿主細胞は、単細胞微生物、例えば原核生物、又は単細胞微生物、真核生物であり得る。
好ましい態様においては、宿主細胞は菌類細胞である“菌類”とは、本明細書において使用される場合、門アスコミコタ(Ascomycota)、バシジオミコタ(Basidiomycota)、キトリジオミコタ(Chytridiomycota)及びヅイゴミコタ(Zygomycota)(Hawksworth など., Ainsworth and Bisby’s Dictionary of the Fungi, 8th edition, 1995, CAB International, University Press, Cambridge, UKにより定義される)、及びオーミコタ(Oomycota)(Hawksworth など., 1995, 前記、171ページに引用される)、並びに栄養胞子菌(Hawksworh など., 1995, 前記)を包含する。
本発明はまた、(a)その野生型において、ポリペプチドを生成できる細胞を、ポリペプチドの生成の助けに成る条件かで培養し;そして(b)ポリペプチドを回収することを含んで成る、本発明のポリペプチドを生成するための方法にも関する。好ましくは、前記細胞は、サーモアスカス属、及びより好ましくは、サーモアスカス・アウレウニアタスである。
本発明はまた、(a)ポリペプチドの生成の助けとなる条件下で宿主細胞を培養し、ここで前記宿主細胞は配列番号1の成熟ポリペプチドコード領域に少なくとも1つの突然変異を有する変異体ヌクレオチド配列を含んで成り、そして前記変異体ヌクレオチド配列は配列番号2のアミノ酸23〜250から成るポリペプチドをコードし;そして(b)前記ポリペプチドを回収することを含んで成る、本発明のポリペプチドの生成方法にも関する。
得られるポリペプチドは、当業界において知られている方法により回収され得る。例えば、ポリペプチドは、従来の方法、例えば遠心分離、濾過、抽出、噴霧−乾燥、蒸発又は沈殿(但し、それらだけには限定されない)により、栄養培地から回収され得る。
本発明はまた、ポリペプチドを、回収可能な量で発現し、そして生成するために、本発明のセルロース分解増強活性を有するポリペプチドをコードする核酸配列により形質転換されている、トランスジェニック植物、植物部分又は植物細胞にも関する。ポリペプチドは、植物又は植物部分から回収され得る。他方では、組換えポリペプチドを含む植物又は植物部分が、食品又は飼料の品質を改良するために、例えば、栄養価値、味のよさ及び流動性質を改良するために、又は抗栄養因子を破壊するために使用され得る。
双子葉植物の例は、タバコ、マメ科植物、たとえばハウチワマメ、ジャガイモ、テンサイ、エンドウ、豆及び大豆、並びにアブラナ科(ブラシカセアエ科(Brassicaceae))、たとえばカリフラワー、ナタネ及び密接に関連するモデル生物アラビドプシス・タリアナ(Arabidopsis Thaliana)である。
本発明のポリペプチドを発現するトランスジェニック植物又は植物細胞は、当業界において知られている方法に従って構成され得る。手短には、植物又は植物細胞は、本発明のポリペプチドをコードする1又は複数の発現構造体を植物宿主ゲノム又はクロロプラストゲノム中に組み込み、そしてその得られる修飾された植物又は植物細胞をトランスジェニック植物又は植物細胞に生長せしめることによって構成される。
核酸構造体は、当業界において知られている従来の技法、たとえばアグロバクテリウム−介在性形質転換、ウィルス−介在性形質転換、マイクロインジェクション、粒子衝撃、バイオリスティク形質転換、及びエレクトロポレーションに従って、植物ゲノム中に組込まれる(Gasser など., Science, 244, 1293; Potrykus, Bio/tech. 8,535,1990; Shimamoto など., Natune, 338, 274, 1989)。
本発明はまた、同じ条件下で培養される場合、親細胞よりもポリペプチドを少なく生成する変異体細胞をもたらす、本発明のポリペプチドをコードする、ポリヌクレオチド配列又はその一部を破壊し、又は欠失することを含んで成る、親細胞の変異体細胞を生成するための方法にも関する。
そのような剤が使用される場合、突然変異誘発は典型的には、選択の突然変異誘発の存在下で、適切な条件下で、突然変異誘発されるベき親細胞をインキュベートし、そして低められた又は発現のない遺伝子を示す変異体細胞をスクリーニングし、そして/又は選択することによって行われる。
前記組み合わされたpH及び温度処理は好ましくは、所望する効果を達成するための十分な時間、4〜5の範囲のpH及び80〜90℃の範囲の温度で行われる。
興味ある生成物の培養及び精製のために使用される方法は、当業界において知られている方法により行われ得る。
もう1つの観点においては、本発明は、本発明の方法により生成される、セルロース分解増強活性を実質的に有さないタンパク質生成物に関する。
本発明はまた、本発明のポリペプチドを含んで成る組成物にも関する。好ましくは、組成物は、そのようなポリペプチドにおいて富化される。用語“富化される”とは、組成物のセルロース分解増強活性が、例えば、少なくとも1.1の富化因子、高められることを示す。
本発明のポリペプチド組成物の好ましい使用の例は下記に与えられる。本発明のポリペプチド組成物の用量、及び組成物が使用される他の条件は、当業界において知られている方法に基づいて決定され得る。
本発明はまた、前記セルロース材料を、有効量のセルロース分解タンパク質により、セルロース分解増強活性を有する、有効量のポリペプチドの存在下で処理し、ここで前記セルロース分解増強活性を有するポリペプチドの存在が、セルロース分解増強活性を有するポリペプチドの不在に比較して、セルロース材料の分解を高める、セルロース材料を分解するか又は転換するための方法にも関する。
用語“エンドグルカナーゼ”とは、セルロース、セルロース誘導体(例えば、カルボキシメチルセルロース及びヒドロキシエチルセルロース)、リケニン、混合されたβ−1,3−グルカン、例えば穀物β−D−グルカン又はキシログルカンにおけるβ−1,4結合、及び、セルロース成分を含む他の植物材料における1,4−β−D−グルコシド結合のエンドヒドロシスを触媒するエンド−1,4−(1,3;1,4)−β−D−グルカン4−グルカノヒドロラーゼ活性は、Ghose, 1987, Pure and Appl. Chem. 59: 257-268の方法に従って、カルボキシメチルセルロース(CMC)加水分解を用いて決定される。
好ましい観点においては、gセルロース分解タンパク質の当たり、セルロース分解増強活性を有するポリペプチドの量は、gセルロースタンパク質当たり、約0.005〜約1.0g、好ましくは約0.01〜約1.0g、より好ましくは約0.15〜約0.75g、より好ましくは約0.15〜約0.5g、より好ましくは約0.1〜約0.5g、さらにより好ましくは約0.1〜約0.5g、及び最も好ましくは約0.05〜約0.2gである。
上記に記載される生成物はまた、本明細書において記載のように、他の有機物質を生成するために使用され得ることは、当業界において良く知られている。
エタノール生成に関しては、発酵に続いて、マッシュが蒸留され、エタノールが抽出される。本発明に従って得られるエタノールは、例えば燃料エタノール、飲料エタノール、すなわち飲用スピリット、又は産業用エタノールとして使用され得る。
本発明の方法においては、追加の酵素が、発酵の前、又は間、例えば発酵微生物の増殖の間又は後、添加され得る。
ヘミセルロースの酵素加水分解は、広範囲の種類の菌類及び細菌により行われ得る。セルロース分解に類似するヘミセルロース加水分解は、多くの酵素の共同作用を必要とする。
セルロースの生物転換のために使用され得るエステラーゼは、アセチルエステラーゼ、例えばアセチルガラクタンエステラーゼ、アセチルマンナンエステラーゼ、及びアセチルキシランエステラーゼ、及びリグニングルコシド結合を加水分解するエステラーゼ、例えばクマル酸エステラーゼ及びフェルラ酸エステラーゼを包含する。
リパーゼは好ましくは、約1〜約400LU/g DS, 好ましくは約1〜約10LU/g DS及びより好ましくは約1〜約5LU/g DSの量で添加される。
ホスホリパーゼの有効量は、約0.01〜約400Lu/g DS、好ましくは約0.1〜約100Lu/g DS、及びより好ましくは約1〜約50LU/g DSである。ホスホリパーゼの量のさらなる最適化は、この後、当業界において知られている標準方法を用いて得られる。
本発明のもう1つの好ましい観点においては、少なくとも1つの界面活性剤及び少なくとも1つの炭水化物生成酵素が、少なくとも1つのプロテアーゼと組合して使用される。プロテアーゼは、遊離アミノ窒素(FAN)を生成するためのタンパク質を消化するために使用され得る。そのような遊離アミノ酸は、酵母のための栄養物として機能し、それにより、酵母の増殖及び従って、エタノールの生成を増強する。
好ましくは、プロテアーゼは、Handbook of Proteolytic Enzymes, Edited by A. J. Barrett, N. D. Rawlings and J. F. Woessner, Academic Press, San Diego, 1998, Chapter 270に記載のように、アスパラギン酸プロテアーゼである。アスパラギン酸プロテアーゼの適切な例は、Berka など., 1990, Gene 96: 313; Berka など., 1993, Gene 125: 195-198; 及び Gomi など., 1993, Biosci. Biotech. Biochem. 57: 1095-1100により開示されるそれらを包含する。
ペルオキシダーゼ活性を有する他の化合物は、いずれかのペルオキシダーゼ(EC1. 11. 1. 7)又はペルオキシダーゼ活性を示す、それらから誘導されたペルオキシダーゼ活性を有するいずれかのフラグメントであり得る。
好ましくは、ペルオキシダーゼは、植物(例えば、ホースラディシュ又は大豆ペルオキシダーゼ)、又は微生物、例えば菌類又は細菌により生成される。
いくつかの好ましい菌類は、アクチノミセス網の株、例えばストレプトミセス・スフェロイデス(Streptomyces spheroids)(ATTC23965)、ストレプトミセス・サーモビオラセウス(Streptomyces thermoviolaceus)(IFO12382)、又はストレプトベルチシラム・ベルチシリウムssp. ベルチシリク(Streptoverticillum verticillium ssp. verticillium)を包含する。
ペルオキシダーゼはまた、ペルオキシダーゼをコードするDNA配列、及びペルオキシダーゼをコードするDNA配列の発現のためのDNA配列を担持する組換えDNAベクターにより形質転換された宿主細胞を、ペルオキシダーゼの発現を可能にする条件下で、培養培地において培養し、そして増殖物からペルオキシダーゼを回収することを含んで成る方法により生成されるペルオキシダーゼでもあり得る。
本発明においては、ペルオキシダーゼ活性を有する化合物は、ペルオキシダーゼ酵素、及びチトクロム、ヘモグロビン又はペルオキシダーゼ酵素由来のペルオキシダーゼ活性フラグメントを含んで成る。
本発明においては、ラッカーゼ及びラッカーゼ関連酵素は、EC1. 10. 3. 2として分類されるいずれかのラッカーゼ酸素、EC1. 10. 3. 1として分類されるいずれかのカテコールオキシダーゼ酵素、EC1. 3. 3. 5として分類されるいずれかのピリルビンオキシダーゼ酵素、又はEC1. 14. 18. 1として分類されるいずれかのものフェノールモノオキシゲナーゼ酵素を包含する。
菌類からの適切な例は、次の株から得られるラッカーゼを包含する:アスペルギラス(Aspergillus)、ニューロスポラ(Neurospora)、例えばN. クラサ(N. crassa)、ポドスポラ(Podospora)、ボトリチス(Botrytis)、コリビア(Collybia)、ホメス(Fomes)、レンチヌス(Lentinus)、プレウロタス(Pleurotus)、トラメテス(Trametes)、例えばT. ビロサ(T. villosa)、及びT. ベルシコロル(T. versicolor)、リゾオクトニア(Rhizooctonia)、例えばR. ソラニ(R. solani)、コプリヌス(Coprins)、例えばC. ニネレウス(C. cinereus)、C. コマタス(C. comatus)、C. フリエシル(C. friesii)、及びC. プリカチリス(C. plicatilis)、プサチレラ(Psathyrella)、例えばP. コンデレアナ(P. condelleana)、パナエオラス(Panaeolus)、例えばP. パピロナセウス(P. papilionaceus)、マイセリオプソラ(Myceliophthora)、例えばM. サーモフィラ(M. thermophila)、シタリジウム(Schytalidium)、例えばS. サーモフィラム(S. thermophilum)、ポリポラス(Polyporus)、例えばP. ピンシタス(P. pinsitus)、ピシノポラス(Pycnoporus)、例えばP. シンナバリマス(P. cinnabarinus)、フレビア(Phlebia)、例えばP. ラジタ(P. radita)(WO92/01046号)又はコリオラス(Coriolus)、例えばC. ヒルスタス(C. hirsutus)(日本特許第2−238885号)。
コプリンス(Coprins)、マイセリオプソラ(Myceliophthora)、ポリポラス(Polyporus)、ピシノポラス(Pycnoporus)、シタリジウム(Scytalidium)又はリゾクトニア(Rhizoctonia)から得られるラッカーゼが好ましくは;特に、コプリヌス・シネレウス(Coprins cinereus)、マイセリオプソラ・サーモフィラ(Myceliophthora thermophila)、ポリポラス・ピンシタス(Polyporus pinsitus)、ピンノポラス・シンナパリヌス(Pycnoporus cinnabarinus)、シタリジウム・サーモフィラム(Scytalidium thermophilum)又はリゾクトニア・ソラニ(Rhizoctonia solani)から得られるラッカーゼが好ましい。
セルロース分解増強活性を有する本発明のポリペプチドは、洗剤組成物に添加され得、そして従って、洗剤組成物の成分になることができる。
本発明の洗剤組成物は、手動又は機械洗濯用洗剤組成物、例えば染色された布の前処理のために適切な洗濯用添加剤組成物及びすすぎ用布ソフトナー組成物として配合され得、又は一般的な家庭用硬質表面洗浄操作における使用のための洗剤組成物として配合され得、又は手動又は機械皿洗い操作のために配合され得る。
一般的に、選択された酵素の性質は、選択された洗剤と適合できるべきであり(すなわち、他の酵素及び非酵素の成分、等とのpH−最適適合性)、そして酵素は効果的な量で存在すべきである。
市販のセルラーゼは、CelluzymeTM 及びCarezymeTM (Novo Nordisk A/S), ClazinaseTM 及びPuradex HATM (Genencor International Inc.) 及びKAC−500 (B)TM (Kao Corporation) を包含する。
好ましい市販のリパーゼ酵素は、LipolaseTM 及びLipolase UltraTM (Novo Nordisk A/S) を包含する。
市販のアミラーゼは、DuramylTM, TermamaylTM, FungamylTM 及びBAMTM (Novo Nordisk A/S), RapidaseTM 及びPurastarTM (Genencor International Inc.)である。
市販のペルオキシダーゼは、GuardzymeTM (Novo Nordisk A/S) を包含する。
洗剤組成物は、非イオン性、例えば半−極性及び/又はアニオン性及び/又はカチオン性及び/又は両性イオンであり得る1又は複数の界面活性剤を含んで成る。界面活性剤は典型的には、0.1〜60重量%のレベルで存在する。
洗剤は、1又は複数のポリマーを含んで成る。例としては、カルボキシメチルセルロース、ポリ(ビニルピロリドン)、ポリ(エチレングリコール)、ポリ(ビニルアルコール)、ポリ(ビニルピリジン−N−オキシド)、ポリ(ビニルイミダゾール)、ポリカルボキシレート(例えばポリアクリレート、マレイン酸/アクリル酸コポリマー及びラウリルメタクリレート/アクリル酸コポリマーを含んで成る。
本発明の洗剤組成物の酵素は、従来の安定剤、例えばポリオール、例えばプロピレングリコール又はグリセロール、糖又は糖アルコール、乳酸、硼酸又は硼酸誘導体、例えば芳香族硼酸エステル又はフェニル硼素酸誘導体、例えば4−ホルミルフェニル硼素酸を用いて安定化され得、そして前記組成物は、例えばWO92/19709号及びWO92/19708号に記載のようにして配合され得る。
洗剤組成物においては、いずれかの酵素、特に本発明の酵素は、洗浄液体1L当たり0.01−100mgの酵素タンパク質、好ましくは洗浄液体1L当たり0.05−5mgの酵素タンパク質、特に洗浄液体1L当たり0.1−1mgの酵素タンパク質に対応する量で添加され得ることが、現在企画される。
セルロース分解増強活性を有する本発明のポリペプチドはまた、WO97/07202号(引例として本明細書組み込まれる)に開示される洗剤配合物に導入され得る。
一般的に、いずれかの植物細胞壁材料の処理は、セルロース分解増強活性を有する本発明のポリペプチドを補足することにより増強され得る。
シグナルペプチド:
本発明はまた、培養培地中へのタンパク質の分泌を可能にする、配列番号2のアミノ酸1〜22から成るシグナルペプチドをコードする、配列番号1のヌクレオチド1〜66から成る核酸配列に作用可能に連結されるタンパク質をコードする、前記核酸配列に対して外来性の遺伝子を含んで成る核酸構造体にも関する。
本発明はまた、(a)そのような組換え宿主細胞を、タンパク質の生成のために適切な条件で培養し;そして(b)タンパク質を回収することを含んで成るタンパク質の生成方法にも関する。
前記核酸配列は、他の制御配列と共に、外来性遺伝子に作用可能に連結され得る。そのような他の制御配列は、前記の通りである。
本発明はさらに、次の例により記載されるが、但しそれは本発明を制限するものではない。
緩衝液及び基質として使用される化物物質は、少なくとも試薬品種の市販の製品であった。
株:
サーモアスカス・アウランチアカス(Thermoaseus aurantiacus)株NN044936 T002-5を、セルロース分解増強活性を有するファミリーGH61ポリペプチドの源として使用した。アスペルギラス・オリザエJaL250株(WO99/61651号)を、セルロース分解増強活性を有するサーモアスカス・アウランチアカスポリペプチドの発現のために使用した。
サーモアスカス・アウランチアカスの通常のプレート及び増殖のための固体ジャガイモデキストロース培地を、1L当たり39gのジャガイモデキストロース糖(Difco BD Biosciences, Franklin Lakes, NJ)から構成した。サーモアスカス・アウランチアカス培養物の増殖のための液体培地を、1L当たり、24gのジャガイモデキストロースブイヨンから構成した。
3%グルコースと共に200mlのNNCYP培地(pH5.0)を含む、500mlのそらせ版付フラスコを、PDA上で増強されたサーモアスカス・アウランチアカスのプレートからの寒天プラグにより接種した。培養物を、170rpmで振盪しながら、45℃で一晩、増殖した。菌糸体を、Whatman #1 フィルター (Whatman Inc., Clifton NJ)を通しての濾過により集め、そして液体窒素下で凍結した。凍結された菌糸体を、冷却された乳鉢において粉末に粉砕し、そしてスキリューカップ管に分配した。粉末を、0.5%のドデシル硫酸リチウム及び0.5mMのGDTAを含む、50mMのCAPS−NaOH緩衝液40mlに懸濁した。
ローリングサークル型増幅(RCA)及び生成物希釈のためのロボット方法を、Biomek FX ロボット (Beckman Coulter, Brea, CA)上での使用のために開発した。TempliPhi DNA Sequencing Template Amplification キット(Amersham Biosciences Corp. , Piscataway, NJ)を、RCAのために使用し、そして製造業者のプロトコールを、ロボット方法において追跡した。
すべての発酵を、5.2%(w/v)グルコース又は5.2%セルロースのいずれかの炭素源によりバッチ供給された2LのApplikon発酵器において行なった。基本培地はNNCYPであり、そしてセルロース培地はまた、初期細胞増殖を促進するために0.4%グルコースを含んだ。pHは、水酸化アンモニウム又はリン酸の添加により、発酵の間、調節された。発酵を、42℃、pH5で、約120時間、行った。菌糸体のサンプルを、5回の接種後、1日目に収穫した。菌糸体サンプルをすばやく、MiraclothTM (Calbiochem, San Diego, CA)を通して濾過により培養地から分離し、そして次に、液体窒素において凍結し、そして-80℃で貯蔵した。
サーモアスカス・アウランチアカスサンプルからの低RNA収率は、マイクロアレイハイブリダイゼーションのための十分な量のRNAを生成するために線状増幅方法(aRNA増幅)の使用を必要した。RNAを増幅し、そしてアミノアリル MessageAmpTm ARNA キット (Ambion, Inc., Austin, TX)を用いて、その製造業者の説明書に従って蛍光ラベルした。
発現ベクターpAILo1を、NA2-tp:プロモーター、アスペルギラス・ニガーアミログルコシダーゼターミネーター配列(AMGターミネーター)及びアスペルギラス・ニジュランスアセトアミダーゼ遺伝子(amdS)を含んで成るpBANe6(アメリカ特許第6,461,837号)を修飾することにより構成した。pBANe6の修飾を、特定部位の突然変異誘発により、amdS選択マーカーからの位置2051, 2722及び3397bpでの3種のNcoI制限部位をまず排除することにより行った。すべての変化は、amdS遺伝子生成物の実際のタンパク質配列を末変化まま残す“サイレント”であるよう企画された。
AMDS3NcoMut (2050):
5'-GTGCCCCATGATACGCCTCCGG-3' (配列番号3)
AMDS2NcoMut (2721):
5'-GAGTCGTATTTCCAAGGCTCCTGACC-3' (配列番号4)
AMDS1 NcoMut (3396):
5'-GGAGGCCATGAAGTGGACCAACGG-3' (配列番号5)。
5’− CACCGTGAAAGCCATGCTCTTTCCTTCGTGTAGAAGACCAGACAG−3’(配列番号6)
アスペルギラス・ニガーアミログルコシダーゼ(AMG)ターミネーター配列を突然変異誘発するための下方プライマー:
5’− CTGGTCTTCTACACGAAGGAAAGAGCATGGCTTTCACGGTGTCTG−3’(配列番号7)。
アスペルギラス・ニガーアミラーゼプロモーター(NA2−tpi)を突然変異誘発するための上方プライマー:
5’− CTATATACACAACTGGATTTACCATGGGCCCGCGGCCGCAGATC−3’(配列番号8)
アスペルギラス・ニガーアミラーゼプロモーター(NA2−tpi)を突然変異誘発するための下方プライマー:
5’− GATCTGCGGCCGCGGGCCCATGGTAAATCCAGTTGTGTATATAG−3’(配列番号9)。
下記に示される2種の合成オリゴヌクレオチドプライマーを、ゲノムクローン番号3からの推定上のファミリーGH61Aをコードするサーモアスカス・アウレンチアカス遺伝子をPCR増幅するために企画した。InFusion Cloning キット(BD Biosciences, Palo Alto, CA)を用いて、制限消化又は連結の必要性を伴わないで、発現ベクターpAILo2中にフラグメントを直接的にクローン化した。
5’− CACAACTGGATTTACCATGTCCTTTTCCAAG−3’(配列番号10)
逆方向プライマー:
5’− AGTCACCTCTAGTTATTAACCAGTATACAG−3’(配列番号11)。
太字の文字は、コード配列を表す。残りの配列は、pAILo2の挿入部位に対して相同である。
サーモアスカス・アウレンチアカスGH61Aゲノムクローン15のDNA配列決定を、バージョン3.1Big Dyeターミネーター化学及びdGTP化学(Applied Biosystems, Inc., Foster City, CA)及びプライマーウォーキング方法を用いて、Applied Biosystems Model 3700 Automated DNA Sequencerにより行った。ヌクレオチド配列をアセンブリーし、そしてVector NTI 8 SuiteソフトウェアーパッケージのContigExpress成分 (Informa, Inc., Frederick, MD)を用いて比較した。
アスペルギラス・オリザエJaL250プロトプラストを、Christensen など., 1988, BiolTechnology 6 : 1419-1422の方法に従って調製した。約1.5μgのpDZA2を用いて、アスペルギラス・オリザエJaL250を形質転換した。プラスミドpAILo2を対照として用いた。
pDZA2によるアスペルギラス・オリザエJaL250の形質転換が約11の形質転換体を生成した。10個の形質転換体を、個々のPDAプレートに単離した。
トウモロコシの茎を、希硫酸を用いて、U. S. Department of Energy National Renewable Energy Laboratory (NREL)で前処理した。次の条件を、前処理のために使用した:190℃での0.048gの硫酸/g乾燥バイオマス及び25%(w/w)乾燥固形物、約1分。NRELに従って、前処理されたトウモロコシの茎(PCR)における水不溶性固形物は、52%セルロース、3.6%ヘミセルロース及び29.8%リグニンを含んだ。
転換率(%)=RS(mg/ml)*100*162/(セルロース(mg/ml)*180)=RS(mg/ml)*100/(セルロース(mg/ml)*1.111)
この等式においては、RSは、グルコース同等物において測定された、溶液における還元糖の濃度(mg/ml)であり、そして因子1.111は、グルコースへのセルロースの転換においての重量増加を表す。
次の生物学的材料を、Agriculture Research Service Patent Culture Collection, Northern Regional Research Center (NRRL),1815 University Street, Peoria, Illinois に、ブタペスト条件に基づいて寄託し、そして次の受託番号を付与された:
寄託物:E. coli 株pDZA2-7
受託番号:NRRL B-30704
寄託日:2004年1月30日
種々の文献が本明細書に引用されており、それらの開示は引用により本明細書に組み込まれている。
Claims (66)
- (a)配列番号2のアミノ酸23〜250と少なくとも70%の同一性を有するアミノ酸配列を有するポリペプチド;
(b)(i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、少なくとも低い緊縮条件下でハイブリダイズするポリヌクレオチドによりコードされるポリペプチド;及び
(c)配列番号2のアミノ酸23〜250の1又は複数のアミノ酸の保存性置換、欠失及び/又は挿入を含んで成る変異体から成る群から選択された、セルロース分解増強活性を有する単離されたポリペプチド。 - 配列番号2のアミノ酸23〜250と、少なくとも70%の同一性を有するアミノ酸を有する請求項1記載のポリペプチド。
- 配列番号2のアミノ酸23〜250と、少なくとも75%の同一性を有するアミノ酸を有する請求項2記載のポリペプチド。
- 配列番号2のアミノ酸23〜250と、少なくとも80%の同一性を有するアミノ酸を有する請求項3記載のポリペプチド。
- 配列番号2のアミノ酸23〜250と、少なくとも90%の同一性を有するアミノ酸を有する請求項4記載のポリペプチド。
- 配列番号2のアミノ酸23〜250と、少なくとも95%の同一性を有するアミノ酸を有する請求項5記載のポリペプチド。
- 配列番号2のアミノ酸23〜250と、少なくとも97%の同一性を有するアミノ酸を有する請求項6記載のポリペプチド。
- 配列番号2のアミノ酸配列を含んで成る請求項1〜7のいずれか1項記載のポリペプチド。
- 配列番号2、又はセルロース分解増強活性を有するそのフラグメントから成る請求項1〜8のいずれか1項記載のポリペプチド。
- 配列番号2から成る請求項9記載のポリペプチド。
- 配列番号2のアミノ酸23〜250から成る請求項9記載のポリペプチド。
- (i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、少なくとも中位の緊縮条件下でハイブリダイズするポリヌクレオチドによりコードされる請求項1記載のポリペプチド。
- (i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、少なくとも中位の高い緊縮条件下でハイブリダイズするポリヌクレオチドによりコードされる請求項1記載のポリペプチド。
- (i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、少なくとも高い緊縮条件下でハイブリダイズするポリヌクレオチドによりコードされる請求項1記載のポリペプチド。
- 前記ポリペプチドが、配列番号2のアミノ酸23〜250の1又は複数のアミノ酸の保存性置換、欠失及び/又は挿入を含んで成る変異体である請求項1記載のポリペプチド。
- E. コリNRRL B-30704に含まれるプラスミドpDZA2-7に含まれるポリヌクレオチドによりコードされる請求項1記載のポリペプチド。
- 請求項1〜16のいずれか1項記載のポリペプチドをコードするヌクレオチド配列を含んで成る単離されたポリヌクレオチド。
- 配列番号1の成熟ポリペプチドコード配列に少なくとも1つの突然変異を有し、ここで前記変異体ヌクレオチド配列が配列番号2のアミノ酸23〜250から成るポリペプチドをコードする請求項17記載の単離されたポリヌクレオチド。
- 発現宿主におけるポリペプチドの生成を指図する1又は複数の制御配列に作用可能に結合される、請求項17又は18記載のポリヌクレオチドを含んで成る核酸構造体。
- 請求項18記載の核酸構造体を含んで成る組換え発現ベクター。
- 請求項18記載の核酸構造体を含んで成る組換え宿主細胞。
- 請求項1〜16のいずれか1項記載のポリペプチドの生成方法であって、(a)その野生型において、前記ポリペプチドの生成の助けと成る条件下でそのポリペプチドを生成できる細胞を培養し;そして(b)前記ポリペプチドを回収することを含んで成る方法。
- 請求項1〜16のいずれか1項記載のポリペプチドの生成方法であって、(a)前記ポリペプチドをコードするヌクレオチド配列を含んで成る核酸構造体を含んで成る宿主細胞を、前記ポリペプチドの生成の助けと成る条件下で培養し;そして(b)前記ポリペプチドを回収することを含んで成る方法。
- 親細胞よりもポリペプチドを少なく生成する変異体をもたらす、請求項1〜16のいずれか1項記載のポリペプチドをコードするヌクレオチド配列を破壊するか又は欠失することを含んで成る、親細胞の変異体の生成方法。
- 請求項24記載の方法により生成される変異体細胞。
- 生来の又は異種タンパク質をコードする遺伝子をさらに含んで成る請求項24記載の変異体。
- (a) 請求項26記載の変異体細胞を、タンパク質の生成の助けと成る条件下で培養し;そして(b)前記タンパク質を回収することを含んで成る、タンパク質の生成方法。
- (a)(i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、DNA集団とを、少なくとも中位の緊縮条件下でハイブリダイズし;そしてセルロース分解増強活性を有するポリペプチドをコードする、ハイブリダイズするポリヌクレオチドを単離することにより得られる単離されたポリヌクレオチド。
- (a)(i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、DNA集団とを、少なくとも中位の高い緊縮条件下でハイブリダイズし;そしてセルロース分解増強活性を有するポリペプチドをコードする、ハイブリダイズするポリヌクレオチドを単離することにより得られる、請求項28記載の単離されたポリヌクレオチド。
- (a)(i)配列番号1のヌクレオチド67〜805、(ii)配列番号1のヌクレオチド67〜805に含まれるcDNA配列、又は(iii)前記(i)もしくは(ii)の相補的鎖と、DNA集団とを、少なくとも高い緊縮条件下でハイブリダイズし;そしてセルロース分解増強活性を有するポリペプチドをコードする、ハイブリダイズするポリヌクレオチドを単離することにより得られる、請求項29記載の単離されたポリヌクレオチド。
- 変異体ヌクレオチド配列を有するポリヌクレオチドの生成方法であって、(a)配列番号1の成熟ポリペプチドコード配列中に少なくとも1つの突然変異を導入し、ここで前記変異体ヌクレオチド配列は配列番号2のアミノ酸23〜250から成るポリペプチドをコードし;そして(b)前記変異体ヌクレオチド配列を含んで成るポリヌクレオチドを回収することを含んで成る方法。
- 請求項31記載の方法により生成される変異体ポリヌクレオチド。
- ポリペプチドの生成方法であって、(a)前記ポリペプチドをコードする請求項32記載の変異体ポリヌクレオチドを含んで成る細胞を、前記ポリペプチドの生成の助けになる条件下で培養し、;そして(b)前記ポリペプチドを回収することを含んで成る方法。
- 配列番号1のヌクレオチド1〜66から成るシグナルペプチドをコードするヌクレオチド配列に作用可能に結合されるタンパク質をコードする、前記ヌクレオチド配列に対して外来性の遺伝子を含んで成る核酸構造体。
- 請求項34記載の核酸構造体を含んで成る組換え発現ベクター。
- 請求項34記載の核酸構造体を含んで成る組換え宿主細胞。
- (a) 請求項36記載の組換え宿主細胞を、タンパク質の生成の助けと成る条件下で培養し;そして(b)前記タンパク質を回収することを含んで成る、タンパク質の生成方法。
- 請求項1〜16のいずれかの1項記載のポリペプチドの生成方法であって、(a)本発明のセルロース分解増強活性を有するポリペプチドをコードするポリヌクレオチドを含んで成るトランスジェニック植物又は植物細胞を、前記ポリペプチドの生成の助けになる条件下で培養し;そして(b)前記ポリペプチドを回収することを含んで成る方法。
- 請求項1記載のポリペプチドをコードするポリヌクレオチドにより形質転換されている、トランスジェニック植物、植物部分又は植物細胞。
- 請求項1〜16のいずれか1項記載のセルロース分解増強活性を有するポリペプチド、セルロース分解活性、及び界面活性剤を含んで成る洗剤組成物。
- セルロース材料を分解するか又は転換するための方法であって、前記セルロース材料を、有効量のセルロース分解タンパク質により、請求項1〜16のいずれか1項記載のセルロース分解増強活性を有する、有効量のポリペプチドの存在下で処理し、ここで前記セルロース分解増強活性を有するポリペプチドの存在が、セルロース分解増強活性を有するポリペプチドの不在に比較して、セルロース材料の分解を高める方法。
- 前記セルロース材料が、草葉性物質、農作物残留物、山林残留物、都市のごみ、古紙、及び紙パルプ工場残留物から成る群から選択される請求項41記載の方法。
- 前記セルロース材料がトウモロコシ茎である請求項41記載の方法。
- 前記1又は複数のセルロース分解酵素が、セルラーゼ、エンドグルカナーゼ、セロビオヒドロラーゼ及びβ−グルコシダーゼから成る群から選択される請求項41記載の方法。
- ヘミセルラーゼ、エステラーゼ、プロテアーゼ、ラッカーゼ又はペルオキシダーゼから成る群から選択された、有効量の1又は複数の酵素により、前記セルロース材料を処理することをさらに含んで成る請求項41記載の方法。
- 前記材料が、前処理工程である請求項41記載の方法。
- 前記方法が、同時糖化及び発酵工程(SSF)における段階である請求項41記載の方法。
- 前記方法が、ハイブリッド加水分解及び発酵工程(HHF)における段階である請求項41記載の方法。
- 分解されたセルロース材料を回収することをさらに含んで成る請求項41記載の方法。
- 前記分解されたセルロース材料が、糖である請求項49記載の方法。
- 前記糖が、グルコース、キシロース、マンノース、ガラクトース及びアラビノースから成る群から選択される請求項50記載の方法。
- 前記セルロース分解タンパク質及び/又は前記セルロース分解増強活性を有するポリペプチドが、細胞を含むか又は含まない発酵ブイヨンの形で存在する請求項41記載の方法。
- (a)セルロース材料を、有効量のセルロース分解タンパク質により、請求項8記載のセルロース分解増強活性を有する、有効量のポリペプチドの存在下で糖化し、ここで前記セルロース分解増強活性を有するポリペプチドの存在が、セルロース分解増強活性を有するポリペプチドの不在に比較して、セルロース材料の分解を高め;
(b)段階(a)の糖化されたセルロース材料を、1又は複数の発酵微生物と共に発酵し;そして
(c)前記酵素から有機物質を回収することを含んで成る、有機物質の生成方法。 - 前記セルロース材料が、草葉性物質、農作物残留物、山林残留物、都市のごみ、古紙、及び紙パルプ工場残留物から成る群から選択される請求項53記載の方法。
- 前記セルロース材料がトウモロコシ茎である請求項53記載の方法。
- 前記1又は複数のセルロース分解酵素が、セルラーゼ、エンドグルカナーゼ、セロビオヒドロラーゼ及びβ−グルコシダーゼから成る群から選択される請求項53記載の方法。
- ヘミセルラーゼ、エステラーゼ、プロテアーゼ、ラッカーゼ又はペルオキシダーゼから成る群から選択された、有効量の1又は複数の酵素により、前記セルロース材料を処理することをさらに含んで成る請求項53記載の方法。
- 前記エステラーゼが、リパーゼ、ホスホリパーゼ、クチナーゼ又はそれらの混合物である請求項57記載の方法。
- 前記段階(a)及び(b)が、同時糖化及び発酵において同時に行われる請求項53記載の方法。
- 前記有機物質が、アルコール、有機酸、ケトン、アミノ酸又はガスである請求項53記載の方法。
- 前記アルコールが、アラビニトール、ブタノール、エタノール、グリセロール、メタノール、1,3−プロパンジオール、ソルビトール又はキシリトールである請求項60記載の方法。
- 前記有機酸が、酢酸、アセトン酸、アジピン酸、アスコルビン酸、クエン酸、2,5−ジケト−D−グルコン酸、ギ酸、フマル酸、グルカル酸、グルコン酸、グルクロン酸、グルタル酸、3-ヒドロキシプロピオン酸、イタコン酸、乳酸、リンゴ酸、マロン酸、蓚酸、プロピオン酸、蟻酸、又はキシロン酸である請求項60記載の方法。
- 前記ケトンが、アセトンである請求項60記載の方法。
- 前記アミノ酸が、アスパラギン酸、グルタミン酸、グリシン、リシン、セリン又はトレオニンである請求項60記載の方法。
- 前記ガスが、メタン、水素、二酸化炭素、又は一酸化水素である請求項60記載の方法。
- 前記セルロース分解タンパク質、及び/又はセルロース分解増強活性を有するポリペプチドが、細胞を有するか又は有さない発酵ブイヨンの形で存在する請求項53記載の方法。
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US54261404P | 2004-02-06 | 2004-02-06 | |
US60/542,614 | 2004-02-06 |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2006552324A Division JP5015610B2 (ja) | 2004-02-06 | 2005-02-04 | セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2011206058A true JP2011206058A (ja) | 2011-10-20 |
JP5221710B2 JP5221710B2 (ja) | 2013-06-26 |
Family
ID=34837563
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2006552324A Expired - Fee Related JP5015610B2 (ja) | 2004-02-06 | 2005-02-04 | セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド |
JP2011124595A Active JP5221710B2 (ja) | 2004-02-06 | 2011-06-02 | セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド |
Family Applications Before (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2006552324A Expired - Fee Related JP5015610B2 (ja) | 2004-02-06 | 2005-02-04 | セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド |
Country Status (10)
Country | Link |
---|---|
US (2) | US7271244B2 (ja) |
EP (1) | EP1733033B1 (ja) |
JP (2) | JP5015610B2 (ja) |
CN (2) | CN103667215A (ja) |
BR (1) | BRPI0507431B1 (ja) |
CA (1) | CA2554784C (ja) |
DK (1) | DK1733033T3 (ja) |
ES (1) | ES2389442T3 (ja) |
MX (1) | MXPA06008745A (ja) |
WO (1) | WO2005074656A2 (ja) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2015037389A (ja) * | 2013-08-19 | 2015-02-26 | 独立行政法人産業技術総合研究所 | 脂質分解酵素及び非イオン性界面活性剤添加によるリグノセルロース系バイオマスからの酵素糖化反応および同時糖化発酵の改善方法 |
Families Citing this family (297)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
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 |
KR100618495B1 (ko) * | 1998-10-06 | 2006-08-31 | 마크 아론 에말파브 | 섬유상의 진균성 숙주 영역에서의 형질전환 시스템:크리소스포륨속에서 |
US7537826B2 (en) * | 1999-06-22 | 2009-05-26 | Xyleco, Inc. | Cellulosic and lignocellulosic materials and compositions and composites made therefrom |
EP1709163B1 (en) * | 2004-01-16 | 2010-11-24 | Novozymes, Inc. | Methods for degrading lignocellulosic materials |
EP1733033B1 (en) * | 2004-02-06 | 2012-06-20 | Novozymes Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
WO2005100582A2 (en) * | 2004-03-25 | 2005-10-27 | Novozymes Inc. | Methods for degrading or converting plant cell wall polysaccharides |
US7708214B2 (en) | 2005-08-24 | 2010-05-04 | Xyleco, Inc. | Fibrous materials and composites |
US20150328347A1 (en) | 2005-03-24 | 2015-11-19 | Xyleco, Inc. | Fibrous materials and composites |
AU2006337184B2 (en) * | 2005-09-30 | 2012-08-16 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
FI120045B (fi) | 2005-12-22 | 2009-06-15 | Roal Oy | Selluloosamateriaalin käsittely ja siinä käyttökelpoiset entsyymit |
US8239083B2 (en) * | 2006-01-18 | 2012-08-07 | I-Guide Robotics, Inc. | Robotic vehicle controller |
CA2640429C (en) * | 2006-01-27 | 2014-04-01 | University Of Massachusetts | Systems and methods for producing biofuels and related materials |
ES2368608T3 (es) | 2006-03-20 | 2011-11-18 | Novozymes, Inc. | Polipéptidos con actividad endoglucanasa y polinucleótidos codifcando los polipéptidos. |
BRPI0710217A2 (pt) | 2006-03-30 | 2011-08-02 | Novozymes Inc | polipeptìdeo, polinucleotìdeo, construção de ácido nucleico, vetor de expressão recombinante, célula hospedeira recombinante, métodos para produzir o polipeptìdeo, para produzir um mutante a partir de uma célula precursora, para produzir uma proteìna, para produzir um polinucleotìdeo, para degradar ou converter um material celulósico, para produzir uma substáncia e para inibir a expressão de um polinucleotìdeo em uma célula, célula mutante, planta transgênica, parte de planta ou célula de planta, e, molécula de rna de filamento duplo |
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 |
PL2082054T5 (pl) † | 2006-11-13 | 2019-03-29 | Danisco Inc | Sposób poprawy uzysku procesów konwersji celulozy |
US9862956B2 (en) | 2006-12-10 | 2018-01-09 | Danisco Us Inc. | Expression and high-throughput screening of complex expressed DNA libraries in filamentous fungi |
US8680252B2 (en) | 2006-12-10 | 2014-03-25 | Dyadic International (Usa), Inc. | Expression and high-throughput screening of complex expressed DNA libraries in filamentous fungi |
CN101652381B (zh) * | 2007-01-30 | 2014-04-09 | 维莱尼姆公司 | 用于处理木质纤维素的酶、编码它们的核酸及其制备和应用方法 |
DK2140016T3 (da) * | 2007-04-24 | 2012-11-12 | Novozymes North America Inc | Detoksificering af forbehandlede lignocelluloseholdige materialer |
WO2008140749A2 (en) * | 2007-05-10 | 2008-11-20 | Novozymes, Inc. | Compositions and methods for enhancing the degradation or conversion of cellulose-containing material |
US8044264B2 (en) | 2007-05-31 | 2011-10-25 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
CA2689910A1 (en) | 2007-05-31 | 2008-12-11 | Novozymes, Inc. | Compositions for degrading cellulosic material |
JP2010528624A (ja) * | 2007-05-31 | 2010-08-26 | ノボザイムス,インコーポレイティド | セルロース物質分解のための組成物 |
US20100333223A1 (en) * | 2007-06-22 | 2010-12-30 | Cornell Research Foundation, Inc | Carbohydrate binding plant hydrolases which alter plant cell walls |
WO2009003167A1 (en) * | 2007-06-27 | 2008-12-31 | Novozymes A/S | Methods for producing fermentation products |
EP2188381B1 (en) * | 2007-08-30 | 2011-12-14 | Iogen Energy Corporation | Enzymatic hydrolysis of lignocellulosic feedstocks using accessory enzymes |
US9695549B2 (en) | 2007-09-03 | 2017-07-04 | Norozymes Als | Detoxifying and recycling of washing solution used in pretreatment of lignocellulose-containing materials |
CA2736661A1 (en) | 2007-09-07 | 2009-03-12 | Dyadic International, Inc. | Novel fungal enzymes |
US20090246844A1 (en) * | 2007-10-26 | 2009-10-01 | Arbor Fuel Inc. | Methods for the production of ethanol |
EP2215242A2 (en) * | 2007-11-01 | 2010-08-11 | Novozymes Inc. | Methods of reducing the inhibitory effect of a tannin of the enzymatic hydrolysis of cellulosic material |
BRPI0819896B1 (pt) * | 2007-12-12 | 2019-03-19 | Novozymes A/S | Processo para converter um material vegetal derivado de um aracaceae sp. contendo manana em um álcool |
CN101952304A (zh) * | 2007-12-19 | 2011-01-19 | 诺维信公司 | 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 |
WO2009085868A1 (en) * | 2007-12-19 | 2009-07-09 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
CA2709490A1 (en) | 2007-12-19 | 2009-07-09 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
CN101981199A (zh) * | 2008-02-27 | 2011-02-23 | 奎特罗斯公司 | 通过两种微生物的顺序作用将植物材料转化为燃料和化学产品的方法 |
BRPI0908564A2 (pt) * | 2008-03-06 | 2019-09-24 | Novozymes As | polipeptídeo e polinucleotídeo isolados, construção de ácido nucleico, célula hospedeira recombinante, métodos para produzir o polipeptídeo, para produzir um mutante de uma célula precursora, para inibir a expressão de um polipeptídeo, 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, e, molécula de rna inibidor de filamento duplo |
NZ587525A (en) * | 2008-03-06 | 2012-02-24 | Novozymes As | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
CN101981200A (zh) | 2008-03-27 | 2011-02-23 | 诺维信公司 | 从含木素纤维素材料产生发酵产物 |
WO2009121058A1 (en) * | 2008-03-28 | 2009-10-01 | Novozymes A/S | Producing fermentation products in the presence of trehalase |
US20090286294A1 (en) * | 2008-04-04 | 2009-11-19 | University Of Massachusetts | Methods and Compositions for Improving the Production of Fuels in Microorganisms |
DE102008024084A1 (de) * | 2008-05-17 | 2009-11-19 | Clariant International Ltd. | Wasch- und Reinigungsmittel |
WO2009152362A2 (en) * | 2008-06-11 | 2009-12-17 | University Of Massachusetts | Methods and compositions for regulating sporulation |
WO2010014631A2 (en) * | 2008-07-28 | 2010-02-04 | University Of Massachusetts | Methods and compositions for improving the production of products in microorganisms |
BRPI0916598A2 (pt) * | 2008-07-28 | 2017-05-30 | Qteros Inc | métodos e composições para aumentar a produção de produtos em micro-organismos |
KR100983672B1 (ko) | 2008-09-16 | 2010-09-24 | 서울과학기술대학교산학협력단 | 당화 및 발효의 동시 공정을 통한 음식물쓰레기로부터의 바이오 에탄올 제조 장치 및 방법 |
US20110165617A1 (en) | 2008-09-30 | 2011-07-07 | Novozymes North America, Inc. | Enzymatic Hydrolysis Of Pretreated Lignocellulose-Containing Material With Distillers Dried Grains |
CA2745760A1 (en) | 2008-12-04 | 2010-06-10 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
EP2379732A2 (en) * | 2008-12-19 | 2011-10-26 | Novozymes Inc. | Methods for increasing enzymatic hydrolysis of cellulosic material in the presence of a peroxidase |
WO2010080527A1 (en) | 2008-12-19 | 2010-07-15 | Novozymes, Inc. | Methods for determining cellulolytic enhancing activity of a polypeptide |
EP2379712B1 (en) * | 2008-12-19 | 2017-02-22 | Novozymes Inc. | Methods for increasing hydrolysis of cellulosic material in the presence of cellobiose dehydrogenase |
CN102325889A (zh) * | 2008-12-19 | 2012-01-18 | 诺维信股份有限公司 | 增加纤维素材料水解的方法 |
WO2010078391A2 (en) | 2008-12-30 | 2010-07-08 | Novozymes North America, Inc. | Improvement of enzymatic hydrolysis of pretreated lignocellulose-containing material with dissolved air flotation sludge |
WO2010078392A2 (en) | 2008-12-31 | 2010-07-08 | Novozymes North America, Inc. | Processes of producing fermentation products |
AR075136A1 (es) | 2009-01-16 | 2011-03-09 | Danisco | Generacion enzimatica de oligosacaridos a partir de cereales o de flujos secundarios de cereales |
DK2387330T3 (en) | 2009-01-16 | 2018-02-05 | Dupont Nutrition Biosci Aps | ENZYMATIC GENERATION OF FUNCTIONAL LIPIDS OUT OF CORN CHLIDE EXTRACT |
US8604277B2 (en) | 2009-01-28 | 2013-12-10 | Novozymes, Inc. | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
WO2010088463A2 (en) | 2009-01-30 | 2010-08-05 | Novozymes, Inc. | Polypeptides having expansin activity and polynucleotides encoding same |
US20100086981A1 (en) * | 2009-06-29 | 2010-04-08 | Qteros, Inc. | Compositions and methods for improved saccharification of biomass |
CN102421302A (zh) | 2009-03-31 | 2012-04-18 | 丹尼斯科公司 | 防止植物细胞壁材料溶解过程中提取物变暗和恶臭形成 |
BRPI1013829A2 (pt) * | 2009-04-20 | 2019-09-24 | Qteros Inc | composições e métodos para fermentação de biomassa |
EP2432889A4 (en) * | 2009-05-18 | 2013-09-11 | Poet Res Inc | SYSTEM FOR TREATING BIOMASS TO FACILITATE ETHANOL PRODUCTION |
CA2763031A1 (en) * | 2009-05-29 | 2010-12-02 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
US8278507B2 (en) | 2009-06-02 | 2012-10-02 | Novozymes, Inc. | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
CN102471759A (zh) | 2009-06-30 | 2012-05-23 | 诺维信公司 | 生物质水解方法 |
EP2451957B1 (en) * | 2009-07-07 | 2017-11-15 | Novozymes Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
EP2451961A1 (en) | 2009-07-07 | 2012-05-16 | Novozymes A/S | Process for treating a substrate with an enzyme |
MX2012000322A (es) | 2009-07-17 | 2012-02-08 | Novozymes As | Metodo de analisis del decaimiento de la celulosa en la hidrolisis del material celulosico. |
DK2478096T3 (en) | 2009-09-17 | 2017-08-28 | Novozymes Inc | POLYPEPTIDES WITH CELLULOLYTIC IMPROVING ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
EP2478095A1 (en) | 2009-09-18 | 2012-07-25 | Novozymes Inc. | Polypeptides having beta-glucosidase activity and polynucleotides encoding same |
DK2480660T5 (da) | 2009-09-23 | 2020-11-09 | Danisco Us Inc | Hidtil ukendte glycosylhydrolaseenzymer og anvendelser heraf |
BR112012006982B1 (pt) | 2009-09-29 | 2021-12-21 | Novozymes, Inc. | Célula hospedeira microbiana transgênica, 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, para fermentar um material celulósico, construções de ácido nucleico, vetor de expressão, polipeptídeo isolado tendo atividade intensificadora celulolítica, polinucleotídeo isolado que codifica o mesmo, e, composição detergente |
WO2011041405A1 (en) | 2009-09-29 | 2011-04-07 | Novozymes, Inc. | Polypeptides having xylanase activity and polynucleotides encoding same |
EP2483296B1 (en) | 2009-09-30 | 2015-07-29 | Novozymes Inc. | Polypeptides derived from thermoascus crustaceus having cellulolytic enhancing activity and polynucleotides encoding same |
WO2011039319A1 (en) | 2009-09-30 | 2011-04-07 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
WO2011059740A1 (en) * | 2009-10-29 | 2011-05-19 | Novozymes, Inc. | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
WO2011057086A1 (en) | 2009-11-06 | 2011-05-12 | Novozymes, Inc. | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
EP2496692B1 (en) | 2009-11-06 | 2016-03-16 | Novozymes, Inc. | Polypeptides having xylanase activity and polynucleotides encoding same |
CA2780179A1 (en) | 2009-11-06 | 2011-05-12 | Novozymes, Inc. | Compositions for saccharification of cellulosic material |
US20130023028A1 (en) | 2009-12-03 | 2013-01-24 | Novozymes South Asia Pvt. Ltd. | Variants Of A Polypeptide With Lipolytic Activity and Improved Stability |
WO2011081658A2 (en) * | 2009-12-15 | 2011-07-07 | Qteros, Inc. | Methods and compositions for producing chemical products from c. phytofermentants |
WO2011080155A2 (en) | 2009-12-21 | 2011-07-07 | Novozymes A/S | Method for producing fermentation products from lignocellulose-containing material |
US20120270277A1 (en) | 2009-12-21 | 2012-10-25 | Coftco Corporation | Biomass Hydrolysis Process |
MX2012007224A (es) | 2009-12-23 | 2012-07-30 | Danisco Us Inc | Metodos para mejorar la eficacia de las reacciones de sacarificacion y fermentacion simultaneas. |
WO2011080267A2 (en) | 2009-12-29 | 2011-07-07 | Novozymes A/S | Polypetides having detergency enhancing effect |
FI122937B (fi) | 2009-12-30 | 2012-09-14 | Roal Oy | Menetelmä selluloosamateriaalin käsittelemiseksi sekä tässä käyttökelpoiset CBH II/Cel6A entsyymit |
US20130040354A1 (en) | 2010-01-29 | 2013-02-14 | Novozymes A/S | Biogas Production Process With Enzymatic Pre-Treatment |
CN102781587A (zh) | 2010-03-01 | 2012-11-14 | 诺维信公司 | 粘压测定 |
GB2478791A (en) * | 2010-03-19 | 2011-09-21 | Qteros Inc | Ethanol production by genetically-modified bacteria |
ES2636216T3 (es) | 2010-03-30 | 2017-10-05 | Novozymes North America, Inc. | Procesos de producción de un producto de fermentación |
BR112012020503A2 (pt) | 2010-03-31 | 2015-09-15 | Novozymes Inc | variante isolado de celobioidrolase precursor, polipeptídeo isolado, construção de ácido nucleico, vetor de expressão, célula hospedeira, método de produzir um variante de celobioidrolas precursor, métodos para obter o variante, para degradar variante de celobioidrolase precursor, métodos para obter o variante, para degradar ou converter um material celulósico, poara produzir um produto de fermentação e de fermentar um material celulósico, e, composição de enzima. |
BR112012024959A2 (pt) * | 2010-03-31 | 2015-09-22 | Meiji Seika Pharma Co Ltd | novo gene de celulose |
DK2588604T3 (en) | 2010-06-30 | 2016-09-26 | Novozymes Inc | Polypeptides having beta-glucosidase activity and polynucleotides encoding them |
DK2591119T4 (da) | 2010-07-07 | 2022-12-12 | Novozymes North America Inc | Fermenteringsproces |
WO2012012590A2 (en) | 2010-07-23 | 2012-01-26 | Novozymes A/S | Processes for producing fermentation products |
EP2598629B1 (en) | 2010-07-30 | 2020-04-08 | Cleanvantage LLC | Aspergillus containing beta-glucosidase, beta-glucosidases and nucleic acids encoding the same |
BR112013002377B1 (pt) | 2010-08-06 | 2020-12-29 | Novozymes A/S | método para degradar ou hidrolisar um polissacarídeo, para produzir sacarídeos solúveis e para produzir uma substância orgânica, e, processo para produzir um produto de fermentação |
EP2603594B1 (en) | 2010-08-12 | 2018-04-25 | Novozymes, Inc. | Compositions comprising a polypeptide having cellulolytic enhancing activity and a bicyclic compound and uses thereof |
US9458483B2 (en) | 2010-08-12 | 2016-10-04 | Novozymes, Inc. | Compositions comprising a polypeptide having cellulolytic enhancing activity and a bicyclic compound and uses thereof |
ES2623288T3 (es) * | 2010-08-20 | 2017-07-10 | Codexis, Inc. | Uso de proteínas de la familia de glicólido hidrolasa 61 en el procesamiento de celulosa |
WO2012030844A1 (en) | 2010-08-30 | 2012-03-08 | Novozymes A/S | Polypeptides having endoglucanase activity and polynucleotides encoding same |
WO2012030811A1 (en) | 2010-08-30 | 2012-03-08 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
EP3470514A1 (en) * | 2010-08-30 | 2019-04-17 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
US20130212746A1 (en) | 2010-08-30 | 2013-08-15 | Novoyzmes A/S | Polypeptides Having Hemicellulolytic Activity And Polynucleotides Encoding Same |
US8624082B2 (en) | 2010-08-30 | 2014-01-07 | Novozymes A/S | Polypeptides having xylanase activity and polynucleotides encoding same |
EP2611901B1 (en) | 2010-08-30 | 2016-05-11 | Novozymes A/S | Polypeptides having beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity and polynucleotides encoding same |
ES2594528T3 (es) | 2010-09-30 | 2016-12-20 | Novozymes, Inc. | Variantes de polipéptidos con actividad de mejora celulolítica y polinucleótidos que las codifican |
MX2013003237A (es) * | 2010-09-30 | 2013-05-30 | Novozymes Inc | Variantes de polipeptidos que tienen actividad potenciadora celulolitica y polinucleotidos que codifican a los mismos. |
BR112013004256A2 (pt) | 2010-10-01 | 2016-08-02 | Novozymes Inc | variante de beta-glicosidase,polinucleotídeo isolado, célula hospedeira recombinante, métodos para produzir uma variante, para degradar um material celulósico, para produzir um produto de fermentação, e para fermentar um material celulósico, e, formulação de caldo total ou composição de cultura de células. |
AU2011315580B2 (en) | 2010-10-13 | 2015-05-07 | Novozymes A/S | Preparation of baked product from dough |
US20130260423A1 (en) | 2010-10-26 | 2013-10-03 | Novozymes North America, Inc. | Methods of Saccharifying Sugar Cane Trash |
BR112013010008B1 (pt) | 2010-11-02 | 2020-09-08 | Novozymes, Inc. | Métodos para degradar e para fermentar um material celulósico, e para produzir um produto de fermentação |
US9212354B2 (en) | 2010-11-04 | 2015-12-15 | Novozymes Inc. | Polypeptides having cellobiohydrolase activitiy and polynucleotides encoding same |
DK2638153T3 (en) * | 2010-11-12 | 2017-10-16 | Novozymes Inc | POLYPEPTIDES WITH ENDOGLUCANASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
DK2640833T3 (en) * | 2010-11-18 | 2016-11-28 | Novozymes Inc | Chimeric polypeptides having cellulolytic enhancing ACTIVITY AND POLYNUCLEOTIDES ENCODING THEM |
US8927235B2 (en) | 2010-12-06 | 2015-01-06 | Novozymes A/S | Methods of hydrolyzing oligomers in hemicellulosic liquor |
EP2661499A1 (en) | 2011-01-04 | 2013-11-13 | Novozymes A/S | Process for producing biogas from pectin and lignocellulose containing material |
WO2012103322A1 (en) | 2011-01-26 | 2012-08-02 | Novozymes A/S | Polypeptides having endoglucanase activity and polynucleotides encoding same |
CN103517985B (zh) | 2011-01-26 | 2016-12-07 | 诺维信公司 | 具有纤维二糖水解酶活性的多肽及编码该多肽的多核苷酸 |
WO2012103288A1 (en) | 2011-01-26 | 2012-08-02 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
WO2012103350A1 (en) | 2011-01-26 | 2012-08-02 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
EP2668268B1 (en) | 2011-01-26 | 2017-05-31 | Novozymes A/S | Polypeptides having cellobiohydrolase activity and polynucleotides encoding same |
WO2012104239A1 (en) * | 2011-01-31 | 2012-08-09 | Dsm Ip Assets B.V. | Mutant cellobiohydrolase |
CN103459605B (zh) | 2011-01-31 | 2016-08-24 | 诺维信北美公司 | 用于酶法精制经预处理的纤维素材料以供糖化的工艺 |
US9051376B2 (en) | 2011-02-23 | 2015-06-09 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
CN103384678B (zh) | 2011-02-23 | 2017-01-18 | 诺维信股份有限公司 | 具有纤维素水解增强活性的多肽及其编码多核苷酸 |
EP3339442B1 (en) | 2011-03-09 | 2022-05-11 | Novozymes A/S | Methods of increasing the cellulolytic enhancing activity of a polypeptide |
US9409958B2 (en) | 2011-03-10 | 2016-08-09 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
BR112013023757A2 (pt) * | 2011-03-17 | 2017-06-06 | Danisco Us Inc | método para redução de viscosidade no processo de sacarificação |
KR20140027154A (ko) * | 2011-03-17 | 2014-03-06 | 다니스코 유에스 인크. | 글리코실 가수분해효소 및 바이오매스 가수분해를 위한 그의 용도 |
DK2689011T3 (en) | 2011-03-25 | 2018-01-22 | Novozymes As | PROCEDURE FOR DEGRADATION OR CONVERSION OF CELLULOSE-SUBSTANCING MATERIAL |
US20140080182A1 (en) | 2011-03-31 | 2014-03-20 | Novozymes, Inc. | Cellulose Binding Domain Variants and Polynucleotides Encoding Same |
US9410136B2 (en) * | 2011-03-31 | 2016-08-09 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
US9340810B2 (en) | 2011-04-25 | 2016-05-17 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
US9926547B2 (en) | 2011-04-28 | 2018-03-27 | Novozymes, Inc. | Polypeptides having endoglucanase activity and polynucleotides encoding same |
US9624518B2 (en) | 2011-04-29 | 2017-04-18 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
WO2012159009A1 (en) | 2011-05-19 | 2012-11-22 | Novozymes, Inc. | Methods for enhancing the degradation of cellulosic material with chitin binding proteins |
EP2710132A1 (en) | 2011-05-19 | 2014-03-26 | Novozymes, Inc. | Methods for enhancing the degradation of cellulosic material with chitin binding proteins |
US20140106427A1 (en) | 2011-06-28 | 2014-04-17 | Novozymes A/S | Biogas From Enzyme-Treated Bagasse |
DK2734633T3 (da) | 2011-07-22 | 2019-06-11 | Novozymes North America Inc | Fremgangsmåder til forbehandling af celluloseholdigt materiale og forbedring af hydrolyse deraf |
DK2739728T3 (en) | 2011-08-04 | 2017-10-16 | Novozymes As | Polypeptides with endoglucanase activity and polynucleotides encoding them |
CN108823184B (zh) | 2011-08-04 | 2022-04-05 | 诺维信公司 | 具有木聚糖酶活性的多肽及其编码多核苷酸 |
WO2013028928A1 (en) | 2011-08-24 | 2013-02-28 | Novozymes, Inc. | Cellulolytic enzyme compositions and uses thereof |
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 |
BR112014004188A2 (pt) | 2011-08-24 | 2017-03-21 | Novozymes Inc | método para obter transformantes positivos de uma célula hospedeira fúngica filamentosa, célula hospedeira fúngica filamentosa, método para produzir múltiplos polipeptídeos recombinantes, e, construto em tandem |
CA2847879C (en) * | 2011-09-09 | 2020-06-23 | Novozymes A/S | Improving properties of paper materials |
WO2013039776A1 (en) | 2011-09-13 | 2013-03-21 | Novozymes North America, Inc. | Methods of hydrolyzing and fermenting cellulosic material |
WO2013043910A1 (en) | 2011-09-20 | 2013-03-28 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
DK2748313T3 (en) | 2011-09-23 | 2016-07-25 | Novozymes As | Methods for hydrolysis of acetylated cellulosic material |
US10017753B2 (en) | 2011-09-29 | 2018-07-10 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
CN103930438A (zh) | 2011-09-30 | 2014-07-16 | 诺维信股份有限公司 | 具有β-葡糖苷酶活性的嵌合多肽和对其进行编码的多核苷酸 |
US10308921B2 (en) | 2011-10-31 | 2019-06-04 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
EP2780449B1 (en) | 2011-11-18 | 2018-04-11 | Novozymes, Inc. | Polypeptides having beta-glucosidase activity, beta-xylosidase activity, or beta-glucosidase and beta-xylosidase activity and polynucleotides encoding same |
BR112014012165A2 (pt) | 2011-11-21 | 2020-06-23 | Novozymes, Inc. | Variante de um polipeptídeo gh61, polinucleotídeo isolado, célula hospedeira recombinante, método para produção de uma variante de um polipeptídeo gh61, processos para degradação ou conversão de um material celulósico, para produção de um produto de fermentação, e para fermentação de um material celulósico, composição enzimática, formulação de caldo completo, ou composição de cultura celular, composição detergente, e método de limpeza ou lavagem de uma superfície dura ou roupa. |
DK2782998T3 (en) | 2011-11-22 | 2018-04-16 | Novozymes Inc | POLYPEPTIDES WITH BETA-XYLOSIDASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
DK2785732T3 (en) | 2011-12-01 | 2017-06-19 | Novozymes Inc | POLYPEPTIDES WITH BETA-XYLOSIDASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
WO2013083801A2 (en) | 2011-12-09 | 2013-06-13 | Novozymes A/S | Biogas from substrates comprising animal manure and enzymes |
EP2791330B1 (en) | 2011-12-16 | 2017-07-26 | Novozymes, Inc. | Polypeptides having laccase activity and polynucleotides encoding same |
CN104768391A (zh) | 2011-12-19 | 2015-07-08 | 诺维信公司 | 用于增加纤维素材料的消化率的方法和组合物 |
BR112014014697A2 (pt) | 2011-12-19 | 2020-10-27 | Novozymes, Inc. | polipeptídeo isolado, composição, polinucleotídeo isolado, construto de ácido nucleico ou vetor de expressão, célula hospedeira recombinante, métodos para produzir um polipeptídeo e uma proteína, para gerar oxigênio molecular, e para remover peróxido de hidrogênio do tecido, processos para degradar ou converter um material celulósico, e para produzir um produto de fermentação, e, formulação de caldo integral ou composição de cultura de células |
CA2878019A1 (en) | 2011-12-20 | 2013-06-27 | Novozymes, Inc. | Cellobiohydrolase variants and polynucleotides encoding same |
WO2013096652A1 (en) | 2011-12-21 | 2013-06-27 | Novozymes, Inc. | Methods for determining the degradation of a biomass material |
US20150010958A1 (en) * | 2012-01-29 | 2015-01-08 | Novoztmes A/S | Methods for Degrading or Converting Cellulosic Material |
JP2013169154A (ja) * | 2012-02-17 | 2013-09-02 | Toyota Motor Corp | セルロース系バイオマス分解増強活性ポリペプチド |
IN2014DN07894A (ja) * | 2012-03-26 | 2015-04-24 | Kansai Chem Eng | |
CA2862703A1 (en) | 2012-03-26 | 2013-10-03 | Novozymes North America, Inc. | Methods of preconditioning cellulosic material |
EP2859110B1 (en) | 2012-03-30 | 2022-10-26 | Novozymes North America, Inc. | Processes of producing fermentation products |
ES2935920T3 (es) | 2012-03-30 | 2023-03-13 | Novozymes North America Inc | Procesos de elaboración de productos de fermentación |
DK2841570T3 (en) | 2012-04-23 | 2018-03-12 | Novozymes As | POLYPEPTIDES WITH GLUCURONYL STERASE ACTIVITY AND POLYNUCLEOTIDES CODING THEM |
CN104245929A (zh) | 2012-04-23 | 2014-12-24 | 诺维信公司 | 具有α-葡糖醛酸糖苷酶活性的多肽以及编码其的多核苷酸 |
WO2013163590A2 (en) | 2012-04-27 | 2013-10-31 | Novozymes, Inc. | Gh61 polypeptide variants and polynucleotides encoding same |
US9458440B2 (en) | 2012-06-07 | 2016-10-04 | Roal Oy | Proteins for the treatment of cellulosic material |
FI124477B (en) | 2012-06-07 | 2014-09-15 | Roal Oy | New proteins for the treatment of cellulose materials |
CN104427869A (zh) | 2012-07-06 | 2015-03-18 | 诺维信公司 | 用于酶回收的液体酶组合物及方法 |
BR112014032865A2 (pt) | 2012-07-18 | 2017-08-01 | Novozymes As | método para tratamento de têxtil de poliéster, e, composição |
CN104540955A (zh) * | 2012-07-19 | 2015-04-22 | 诺维信公司 | 用于增加纤维素材料的酶水解的方法 |
US20150247137A1 (en) * | 2012-09-19 | 2015-09-03 | Novozymes A/S | Polypeptides Having Cellulolytic Enhancing Activity and Polynucleotides Encoding Same |
EP2898068A2 (en) | 2012-09-19 | 2015-07-29 | Novozymes, Inc. | Methods for enhancing the degradation or conversion of cellulosic material |
US9708592B2 (en) | 2012-09-28 | 2017-07-18 | Novosymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
DK2903412T3 (da) | 2012-10-08 | 2019-12-16 | Novozymes As | Polypeptider med cellulolyseforbedrende aktivitet og polynukleotider, som koder for dem |
US20150275194A1 (en) | 2012-10-24 | 2015-10-01 | Novozymes A/S | Polypeptides Having Cellulolytic Enhancing Activity And Polynucleotides Encoding Same |
DK2925790T3 (da) | 2012-11-27 | 2021-10-11 | Novozymes As | Formalingsproces |
CA2892031A1 (en) | 2012-11-27 | 2014-06-05 | Novozymes A/S | Milling process |
US9765373B2 (en) | 2012-12-14 | 2017-09-19 | Novozymes A/S | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
WO2014099798A1 (en) | 2012-12-19 | 2014-06-26 | Novozymes A/S | Polypeptides having cellulolytic enhancinc activity and polynucleotides encoding same |
CN105074001A (zh) | 2013-02-21 | 2015-11-18 | 诺维信公司 | 糖化和发酵纤维素材料的方法 |
EP2964760B1 (en) | 2013-03-08 | 2021-05-12 | Novozymes A/S | Cellobiohydrolase variants and polynucleotides encoding same |
WO2014140165A1 (en) | 2013-03-14 | 2014-09-18 | Dsm Ip Assets B.V. | Cell wall deconstruction enzymes of paecilomyces byssochlamydoides and uses thereof |
WO2014140167A1 (en) | 2013-03-14 | 2014-09-18 | Dsm Ip Assets B.V. | Cell wall deconstruction enzymes of malbranchea cinnamomea and uses thereof |
CA2910239A1 (en) | 2013-05-10 | 2014-11-13 | Novozymes A/S | Polypeptides having xylanase activity and polynucleotides encoding same |
JP2016533741A (ja) | 2013-07-29 | 2016-11-04 | ダニスコ・ユーエス・インク | 酵素の変異体 |
WO2015035029A1 (en) | 2013-09-04 | 2015-03-12 | Novozymes A/S | Processes for increasing enzymatic hydrolysis of cellulosic material |
EP3063282B1 (en) | 2013-09-11 | 2020-03-25 | Novozymes A/S | Processes for producing fermentation products |
US9938552B2 (en) | 2013-11-01 | 2018-04-10 | Novozymes A/S | Methods of saccharifying and fermenting a cellulosic material |
WO2015081139A1 (en) | 2013-11-26 | 2015-06-04 | Novozymes A/S | Enzyme compositions and uses thereof |
EP3511418B1 (en) | 2014-01-07 | 2020-07-15 | Novozymes A/S | Corollospora maritima mannanase and its use |
CN115975994A (zh) | 2014-06-06 | 2023-04-18 | 诺维信公司 | 酶组合物及其用途 |
EP3191597A1 (en) | 2014-08-21 | 2017-07-19 | Novozymes A/S | Process for saccharifying cellulosic material under oxygen addition |
DK3183352T3 (da) | 2014-08-22 | 2021-06-14 | Cysbio Aps | Fremgangsmåde til fremstilling af et fermenteringsprodukt ud fra et lignocelluloseholdigt materiale |
DK3186372T3 (da) | 2014-08-28 | 2020-12-21 | Novozymes As | Solubilisering af kommunalt fast affald (MSW) ved hjælp af en enzymblanding |
BR112017004251A2 (pt) | 2014-09-05 | 2017-12-12 | Novozymes As | variantes de módulos de ligação a carboidrato e polinucleotídeos que os codificam |
CN107109346B (zh) | 2014-09-23 | 2021-07-20 | 诺维信公司 | 用于生产乙醇的方法和发酵生物 |
DK3640336T3 (da) | 2015-01-28 | 2022-06-27 | Dsm Ip Assets Bv | Fremgangsmåde til enzymatisk hydrolyse af lignocellulosemateriale og fermentering af sukre |
WO2016120298A1 (en) | 2015-01-28 | 2016-08-04 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
CA2973302C (en) | 2015-01-28 | 2022-10-25 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
WO2016138167A2 (en) | 2015-02-24 | 2016-09-01 | Novozymes A/S | Cellobiohydrolase variants and polynucleotides encoding same |
US10308963B2 (en) | 2015-02-27 | 2019-06-04 | Novozymes A/S | Processes of producing ethanol using a fermenting organism |
CN107404915A (zh) | 2015-03-04 | 2017-11-28 | 杜邦营养生物科学有限公司 | 谷粒加工 |
BR112017018461A2 (pt) | 2015-03-12 | 2018-04-17 | Novozymes As | processos para hidrólise multiestágio, para produção de um produto de fermentação, e, para aumento de rendimento de açúcar de hidrólise. |
BR112017019331A2 (pt) | 2015-03-12 | 2018-06-05 | Beta Renewables Spa | processos para sacarificação de múltiplos estágios de um material lignocelulósico e para melhorar um rendimento de glicose ou xilose de sacarificação de um material lignocelulósico em um reator de tanque continuamente agitado |
TN2017000318A1 (en) | 2015-03-12 | 2019-01-16 | Beta Renewable Spa | Multi-stage enzymatic hydrolysis of lignocellulosic biomass |
WO2016169893A1 (en) | 2015-04-20 | 2016-10-27 | Dsm Ip Assets B.V. | Whole fermentation broth |
WO2016169892A1 (en) | 2015-04-20 | 2016-10-27 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
CN116676293A (zh) | 2015-05-27 | 2023-09-01 | 国投生物科技投资有限公司 | 具有纤维二糖水解酶活性的多肽以及对其进行编码的多核苷酸 |
WO2016205127A1 (en) | 2015-06-18 | 2016-12-22 | Novozymes A/S | Polypeptides having trehalase activity and the use thereof in process of producing fermentation products |
WO2016207144A1 (en) | 2015-06-22 | 2016-12-29 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
WO2017019491A1 (en) | 2015-07-24 | 2017-02-02 | Novozymes Inc. | Polypeptides having beta-xylosidase activity and polynucleotides encoding same |
BR112018001041A2 (pt) | 2015-07-24 | 2018-09-11 | Novozymes Inc | polipeptídeo isolado, composição, formulação de caldo inteiro ou composição de cultura de células, célula hospedeira recombinante, métodos para produção de um polipeptídeo e para produção de uma proteína, planta, parte de planta ou célula de planta transgênica, e, processos para degradação de um material celulósico ou hemicelulósico, para produção de um produto de fermentação e para fermentação de um material celulósico ou hemicelulósico. |
EP3344761A1 (en) | 2015-09-04 | 2018-07-11 | Novozymes A/S | Methods of inhibiting aa9 lytic polysaccharide monooxygenase catalyzed inactivation of enzyme compositions |
CN108350044B (zh) | 2015-09-22 | 2022-05-24 | 诺维信公司 | 具有纤维二糖水解酶活性的多肽以及对其进行编码的多核苷酸 |
WO2017070219A1 (en) | 2015-10-20 | 2017-04-27 | Novozymes A/S | Lytic polysaccharide monooxygenase (lpmo) variants and polynucleotides encoding same |
BR112018007923A2 (pt) | 2015-10-23 | 2019-01-29 | Novozymes As | método para produção de polpa de dissolução, polpa de dissolução, fibra têxtil, celulose derivatizada, uso de uma polpa de dissolução, e, uso de celulase. |
WO2017076421A1 (en) | 2015-11-02 | 2017-05-11 | Renescience A/S | Solubilization of msw with blend enzymes |
EP3394275A1 (en) | 2015-12-22 | 2018-10-31 | Novozymes A/S | Process of extracting oil from thin stillage |
GB201522603D0 (en) | 2015-12-22 | 2016-02-03 | Dupont Nutrition Biosci Aps | Composition |
CN106929425B (zh) * | 2015-12-31 | 2021-07-09 | 国家电网公司 | 一种耐高温酸性嗜热子囊菌纤维素酶、其制备方法和应用 |
PL3416740T3 (pl) | 2016-02-19 | 2021-05-17 | Intercontinental Great Brands Llc | Procesy tworzenia wielu strumieni wartości ze źródeł biomasy |
WO2017144670A1 (en) | 2016-02-24 | 2017-08-31 | Danmarks Tekniske Universitet | Improved process for producing a fermentation product from a lignocellulose-containing material |
CN109415712A (zh) | 2016-03-02 | 2019-03-01 | 诺维信公司 | 纤维二糖水解酶变体和编码它们的多核苷酸 |
US11965189B2 (en) | 2016-03-24 | 2024-04-23 | Novozymes A/S | Cellobiohydrolase variants and polynucleotides encoding same |
WO2017205535A1 (en) | 2016-05-27 | 2017-11-30 | Novozymes, Inc. | Polypeptides having endoglucanase activity and polynucleotides encoding same |
EP3469090A1 (en) | 2016-06-09 | 2019-04-17 | DSM IP Assets B.V. | Seed train for large scale enzyme production |
WO2018019948A1 (en) | 2016-07-29 | 2018-02-01 | Dsm Ip Assets B.V. | Polypeptides having cellulolytic enhancing activity and uses thereof |
WO2018026868A1 (en) | 2016-08-01 | 2018-02-08 | Novozymes, Inc. | Polypeptides having endoglucanase activity and polynucleotides encoding same |
US20190233861A1 (en) | 2016-09-30 | 2019-08-01 | Norwegian University Of Life Sciences | Process for degrading a polysaccharide employing a lytic polysaccharide monooxygenase |
WO2018085370A1 (en) | 2016-11-02 | 2018-05-11 | Novozymes A/S | Processes for reducing production of primeverose during enzymatic saccharification of lignocellulosic material |
WO2018098381A1 (en) | 2016-11-23 | 2018-05-31 | Novozymes A/S | Improved yeast for ethanol production |
CA3043435A1 (en) | 2016-11-24 | 2018-05-31 | Dsm Ip Assets B.V. | Enzyme compositions with improved hydrolysis performance |
BR112019010355B1 (pt) | 2016-11-24 | 2024-03-05 | Dsm Ip Assets B.V. | Composição de enzimas |
EP3551759A1 (en) | 2016-12-06 | 2019-10-16 | Novozymes A/S | Improved processes for production of ethanol from xylose-containing cellulosic substrates using engineered yeast strains |
WO2018185071A1 (en) | 2017-04-03 | 2018-10-11 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
US11091753B2 (en) | 2017-05-31 | 2021-08-17 | Novozymes A/S | Xylose fermenting yeast strains and processes thereof for ethanol production |
AU2018275794A1 (en) | 2017-06-02 | 2019-12-05 | Novozymes A/S | Improved yeast for ethanol production |
EP4015524A1 (en) | 2017-06-28 | 2022-06-22 | Novozymes A/S | Polypeptides having trehalase activity and polynucleotides encoding same |
WO2019032477A1 (en) | 2017-08-07 | 2019-02-14 | Novozymes A/S | METHOD FOR TREATING WASTEWATER COMPRISING THE TREATMENT OF SLUDGE WITH HYDROLYTIC ENZYMES |
CN111094562A (zh) | 2017-08-08 | 2020-05-01 | 诺维信公司 | 具有海藻糖酶活性的多肽及其在产生发酵产物的方法中的用途 |
EP3682014A1 (en) | 2017-09-15 | 2020-07-22 | Novozymes A/S | Enzyme blends and processes for improving the nutritional quality of animal feed |
WO2019074828A1 (en) | 2017-10-09 | 2019-04-18 | Danisco Us Inc | CELLOBIOSE DEHYDROGENASE VARIANTS AND METHODS OF USE |
BR112020005439A2 (pt) | 2017-10-09 | 2020-09-24 | Dsm Ip Assets B.V. | processo para hidrólise enzimática de material lignocelulósico e fermentação de açúcares |
EP3701037A1 (en) | 2017-10-23 | 2020-09-02 | Novozymes A/S | Processes for reducing lactic acid in a biofuel fermentation system |
EP3704259A1 (en) | 2017-10-30 | 2020-09-09 | DSM IP Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
WO2019086370A1 (en) | 2017-10-30 | 2019-05-09 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of lignocellulosic material and fermentation of sugars |
CA3083854A1 (en) | 2017-12-22 | 2019-06-27 | Novozymes A/S | Wheat milling process and gh8 xylanases |
CN113286871A (zh) | 2018-01-29 | 2021-08-20 | 诺维信公司 | 用于乙醇生产的氮利用提高的微生物 |
CA3107124A1 (en) | 2018-02-15 | 2019-08-22 | Novozymes A/S | Improved yeast for ethanol production |
WO2019185681A1 (en) | 2018-03-28 | 2019-10-03 | Dsm Ip Assets B.V. | Enzyme composition |
EP3775189A1 (en) | 2018-03-28 | 2021-02-17 | DSM IP Assets B.V. | Enzyme composition |
WO2019201765A1 (en) | 2018-04-20 | 2019-10-24 | Renescience A/S | Method for determining chemical compounds in waste |
WO2019219804A1 (en) | 2018-05-17 | 2019-11-21 | Dsm Ip Assets B.V. | Process for producing a polypeptide |
LT3802843T (lt) | 2018-05-30 | 2023-04-25 | Versalis S.P.A. | Cukrų gamybos iš angliavandenių medžiagos būdas |
BR112020024347A2 (pt) | 2018-05-31 | 2021-02-23 | Novozymes A/S | processos para aumentar o crescimento e a produtividade de levedura |
CN112601818A (zh) | 2018-07-25 | 2021-04-02 | 诺维信公司 | 用于生产乙醇的表达酶的酵母 |
WO2020058248A1 (en) | 2018-09-18 | 2020-03-26 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of carbohydrate material and fermentation of sugars |
WO2020058253A1 (en) | 2018-09-18 | 2020-03-26 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of carbohydrate material and fermentation of sugars |
WO2020058249A1 (en) | 2018-09-18 | 2020-03-26 | Dsm Ip Assets B.V. | Process for enzymatic hydrolysis of carbohydrate material and fermentation of sugars |
US11807889B2 (en) | 2018-10-08 | 2023-11-07 | Novozymes A/S | Yeast expressing a heterologous phospholipase for ethanol production |
CN112912511A (zh) | 2018-10-24 | 2021-06-04 | 帝斯曼知识产权资产管理有限公司 | 用于碳水化合物材料酶促水解和糖发酵的方法 |
CN109337828B (zh) * | 2018-11-29 | 2021-10-12 | 中国科学院成都生物研究所 | 一种水稻秸秆发酵处理工艺 |
CN109468343B (zh) * | 2018-11-29 | 2021-11-02 | 中国科学院成都生物研究所 | 一种秸秆厌氧发酵产沼气促进剂及其制备方法和应用 |
BR112021011384A2 (pt) | 2018-12-12 | 2022-05-17 | Novozymes As | Polipeptídeo isolado, composição de enzimas, formulação de caldo inteiro ou composição de cultura de células, polinucleotídeo isolado, célula hospedeira recombinante, método de produção de um polipeptídeo, planta, parte da planta ou célula da planta transgênica, e, processos para degradação de um material celulósico ou hemicelulósico, para produção de um produto de fermentação e de fermentação de um material celulósico ou hemicelulósico |
BR112021014873A2 (pt) | 2019-01-31 | 2021-10-05 | Novozymes A/S | Polipeptídeo, combinação de enzimas, polinucleotídeo, construto de ácido nucleico ou vetor de expressão recombinante, célula hospedeira recombinante, método de produção de um polipeptídeo, e, processo de produção de um produto de fermentação |
EP3938525A1 (en) | 2019-03-12 | 2022-01-19 | DSM IP Assets B.V. | Process for producing a fermentation broth |
CN114402105B (zh) | 2019-07-26 | 2024-01-30 | 诺维信公司 | 纸浆的酶处理 |
WO2021021458A1 (en) | 2019-07-26 | 2021-02-04 | Novozymes A/S | Microorganisms with improved nitrogen transport for ethanol production |
CA3144423A1 (en) | 2019-08-05 | 2021-02-11 | Kurt Creamer | Enzyme blends and processes for producing a high protein feed ingredient from a whole stillage byproduct |
BR112021026477A2 (pt) | 2019-08-06 | 2022-02-08 | Novozymes As | Célula hospedeira recombinante, métodos de produção de um produto de fermentação a partir de um material contendo amido ou contendo celulose, de produção do polipeptídeo maduro, de produção de um derivado de uma célula hospedeira recombinante e de produção de etanol, construto de ácido nucleico ou vetor de expressão, composição, e, uso de uma célula hospedeira recombinante |
US20220340943A1 (en) | 2019-09-10 | 2022-10-27 | Dsm Ip Assets B.V. | Enzyme composition |
EP4031661A1 (en) | 2019-09-16 | 2022-07-27 | Novozymes A/S | Polypeptides having beta-glucanase activity and polynucleotides encoding same |
CN110791535A (zh) * | 2019-12-02 | 2020-02-14 | 齐齐哈尔龙江阜丰生物科技有限公司 | 一种生产和提取赖氨酸的工艺 |
AU2020402990A1 (en) | 2019-12-10 | 2022-06-09 | Novozymes A/S | Microorganism for improved pentose fermentation |
WO2021126966A1 (en) | 2019-12-16 | 2021-06-24 | Novozymes A/S | Processes for producing fermentation products |
JP2023507210A (ja) * | 2019-12-19 | 2023-02-21 | ▲華▼▲東▼理工大学 | 乳酸光学プローブ及びその調製方法並びに使用 |
EP4103709A2 (en) | 2020-02-10 | 2022-12-21 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
GB202005073D0 (en) | 2020-04-06 | 2020-05-20 | Mellizyme Biotechnology Ltd | Enzymatic degradation of plastics |
WO2022013148A1 (en) | 2020-07-13 | 2022-01-20 | Dsm Ip Assets B.V. | Process for the production of biogas |
MX2023002490A (es) | 2020-09-04 | 2023-03-09 | Novozymes As | Organismo fermentador mejorado para la produccion de etanol. |
US20230399632A1 (en) | 2020-11-02 | 2023-12-14 | Novozymes A/S | Glucoamylase Variants and Polynucleotides Encoding Same |
WO2022096406A1 (en) | 2020-11-04 | 2022-05-12 | Renescience A/S | Method for enzymatic and/or microbial processing of waste comprising recirculation of process water |
BR112023020357A2 (pt) | 2021-04-06 | 2023-11-21 | Dsm Ip Assets Bv | Composição de enzima |
CA3213845A1 (en) | 2021-04-06 | 2022-10-13 | Dsm Ip Assets B.V. | Enzyme composition |
US20240182936A1 (en) | 2021-04-06 | 2024-06-06 | Dsm Ip Assets B.V. | Enzyme composition |
WO2022214460A1 (en) | 2021-04-08 | 2022-10-13 | Dsm Ip Assets B.V. | Process for the preparation of a sugar product and a fermentation product |
WO2022261003A1 (en) | 2021-06-07 | 2022-12-15 | Novozymes A/S | Engineered microorganism for improved ethanol fermentation |
CN114806890A (zh) * | 2022-04-26 | 2022-07-29 | 湖南农业大学 | 辣椒秸秆木质素降解菌剂组合及其应用 |
CN114736881B (zh) * | 2022-06-09 | 2022-09-27 | 中国农业科学院北京畜牧兽医研究所 | 酸稳定性提高的葡萄糖氧化酶GoxM10突变体A4D及其衍生突变体和应用 |
WO2024064901A2 (en) | 2022-09-23 | 2024-03-28 | Novozymes A/S | Improved fermenting organism for ethanol production |
Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2002095014A2 (en) * | 2001-05-18 | 2002-11-28 | Novozymes A/S | Polypeptides having cellobiase activity and polynucleotides encoding same |
WO2005074656A2 (en) * | 2004-02-06 | 2005-08-18 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
NZ242074A (en) | 1991-03-22 | 1993-08-26 | Novo Nordisk As | Extracellular production of a heterologous heme protein in a filamentous fungus; dna construct therefor |
US7045331B2 (en) * | 2001-12-18 | 2006-05-16 | Genencor International, Inc. | EGVII endoglucanase and nucleic acids encoding the same |
-
2005
- 2005-02-04 EP EP05726395A patent/EP1733033B1/en active Active
- 2005-02-04 CN CN201310362275.5A patent/CN103667215A/zh active Pending
- 2005-02-04 MX MXPA06008745A patent/MXPA06008745A/es active IP Right Grant
- 2005-02-04 BR BRPI0507431-2A patent/BRPI0507431B1/pt active IP Right Grant
- 2005-02-04 CN CN2005800119170A patent/CN1965078B/zh active Active
- 2005-02-04 ES ES05726395T patent/ES2389442T3/es active Active
- 2005-02-04 DK DK05726395.6T patent/DK1733033T3/da active
- 2005-02-04 JP JP2006552324A patent/JP5015610B2/ja not_active Expired - Fee Related
- 2005-02-04 WO PCT/US2005/003802 patent/WO2005074656A2/en active Application Filing
- 2005-02-04 US US11/051,670 patent/US7271244B2/en active Active
- 2005-02-04 CA CA2554784A patent/CA2554784C/en not_active Expired - Fee Related
-
2007
- 2007-08-08 US US11/835,872 patent/US7534594B2/en active Active
-
2011
- 2011-06-02 JP JP2011124595A patent/JP5221710B2/ja active Active
Patent Citations (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2002095014A2 (en) * | 2001-05-18 | 2002-11-28 | Novozymes A/S | Polypeptides having cellobiase activity and polynucleotides encoding same |
WO2005074656A2 (en) * | 2004-02-06 | 2005-08-18 | Novozymes, Inc. | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
Non-Patent Citations (2)
Title |
---|
JPN5007000723; Biochem. J. 193(1981), p.67-74 * |
JPN7010004245; Eur. J. Biochem. 249(1997), p.584-591 * |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2015037389A (ja) * | 2013-08-19 | 2015-02-26 | 独立行政法人産業技術総合研究所 | 脂質分解酵素及び非イオン性界面活性剤添加によるリグノセルロース系バイオマスからの酵素糖化反応および同時糖化発酵の改善方法 |
Also Published As
Publication number | Publication date |
---|---|
CN1965078B (zh) | 2013-09-18 |
CA2554784A1 (en) | 2005-08-18 |
DK1733033T3 (da) | 2012-09-24 |
EP1733033A4 (en) | 2007-06-13 |
BRPI0507431B1 (pt) | 2021-07-27 |
JP2007523646A (ja) | 2007-08-23 |
JP5015610B2 (ja) | 2012-08-29 |
CA2554784C (en) | 2013-05-28 |
BRPI0507431A (pt) | 2007-07-03 |
EP1733033A2 (en) | 2006-12-20 |
EP1733033B1 (en) | 2012-06-20 |
WO2005074656A3 (en) | 2006-11-30 |
MXPA06008745A (es) | 2007-01-23 |
US7534594B2 (en) | 2009-05-19 |
ES2389442T3 (es) | 2012-10-26 |
US7271244B2 (en) | 2007-09-18 |
US20080003645A1 (en) | 2008-01-03 |
WO2005074656A2 (en) | 2005-08-18 |
JP5221710B2 (ja) | 2013-06-26 |
CN1965078A (zh) | 2007-05-16 |
CN103667215A (zh) | 2014-03-26 |
US20060005279A1 (en) | 2006-01-05 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP5221710B2 (ja) | セルロース分解増強活性を有するポリペプチド及びそれをコードするポリヌクレオチド | |
US10544195B2 (en) | Polypeptides having cellulolytic enhancing activity and nucleic acids encoding same | |
JP5129142B2 (ja) | セルロース材料の分解又は転換を増強するための方法 | |
NZ589570A (en) | Methods for enhancing the degradation or conversion of cellulosic material |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20121002 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20121227 |
|
A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20130107 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20130118 |
|
TRDD | Decision of grant or rejection written | ||
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20130205 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20130307 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20160315 Year of fee payment: 3 |
|
R150 | Certificate of patent or registration of utility model |
Ref document number: 5221710 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |