MX2009001717A - Variantes de pululanasa con productividad incrementada. - Google Patents
Variantes de pululanasa con productividad incrementada.Info
- Publication number
- MX2009001717A MX2009001717A MX2009001717A MX2009001717A MX2009001717A MX 2009001717 A MX2009001717 A MX 2009001717A MX 2009001717 A MX2009001717 A MX 2009001717A MX 2009001717 A MX2009001717 A MX 2009001717A MX 2009001717 A MX2009001717 A MX 2009001717A
- Authority
- MX
- Mexico
- Prior art keywords
- pullulanase
- group
- seq
- host organism
- sequence
- Prior art date
Links
- 108090000637 alpha-Amylases Proteins 0.000 title claims abstract description 189
- 230000001965 increasing effect Effects 0.000 title description 16
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 80
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 78
- 238000000034 method Methods 0.000 claims abstract description 46
- 230000014509 gene expression Effects 0.000 claims description 70
- 150000007523 nucleic acids Chemical class 0.000 claims description 47
- 210000004027 cell Anatomy 0.000 claims description 45
- 102000004169 proteins and genes Human genes 0.000 claims description 44
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 41
- 125000003729 nucleotide group Chemical group 0.000 claims description 40
- 239000002773 nucleotide Substances 0.000 claims description 38
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 32
- 108020004414 DNA Proteins 0.000 claims description 27
- 108020004707 nucleic acids Proteins 0.000 claims description 27
- 102000039446 nucleic acids Human genes 0.000 claims description 27
- 238000004519 manufacturing process Methods 0.000 claims description 24
- 238000010276 construction Methods 0.000 claims description 21
- 241000194108 Bacillus licheniformis Species 0.000 claims description 16
- 239000000203 mixture Substances 0.000 claims description 16
- 241000894006 Bacteria Species 0.000 claims description 15
- 241000588724 Escherichia coli Species 0.000 claims description 15
- 230000000694 effects Effects 0.000 claims description 15
- 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 13
- 241000499912 Trichoderma reesei Species 0.000 claims description 11
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 9
- 241000233866 Fungi Species 0.000 claims description 8
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 8
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 claims description 8
- 241000228245 Aspergillus niger Species 0.000 claims description 7
- 239000001963 growth medium Substances 0.000 claims description 7
- 244000063299 Bacillus subtilis Species 0.000 claims description 6
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 6
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 claims description 5
- 238000012258 culturing Methods 0.000 claims description 3
- 230000001052 transient effect Effects 0.000 claims 1
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 47
- 239000013604 expression vector Substances 0.000 abstract description 23
- 125000000539 amino acid group Chemical group 0.000 abstract description 8
- 238000005457 optimization Methods 0.000 abstract description 7
- 235000013305 food Nutrition 0.000 abstract description 5
- 230000002255 enzymatic effect Effects 0.000 abstract description 4
- 238000000855 fermentation Methods 0.000 abstract description 4
- 230000004151 fermentation Effects 0.000 abstract description 4
- 239000004753 textile Substances 0.000 abstract description 3
- 235000018102 proteins Nutrition 0.000 description 42
- -1 for example Substances 0.000 description 41
- 239000013598 vector Substances 0.000 description 36
- 235000001014 amino acid Nutrition 0.000 description 31
- 150000001413 amino acids Chemical class 0.000 description 26
- 239000013612 plasmid Substances 0.000 description 26
- 229940024606 amino acid Drugs 0.000 description 25
- 239000012634 fragment Substances 0.000 description 24
- 229920001184 polypeptide Polymers 0.000 description 24
- 238000006467 substitution reaction Methods 0.000 description 18
- 241000193830 Bacillus <bacterium> Species 0.000 description 17
- 108020004705 Codon Proteins 0.000 description 16
- 102000004190 Enzymes Human genes 0.000 description 16
- 108090000790 Enzymes Proteins 0.000 description 16
- 229940088598 enzyme Drugs 0.000 description 16
- 238000000746 purification Methods 0.000 description 14
- 108091005804 Peptidases Proteins 0.000 description 13
- 238000013518 transcription Methods 0.000 description 12
- 230000035897 transcription Effects 0.000 description 12
- 230000009466 transformation Effects 0.000 description 12
- FFEARJCKVFRZRR-SCSAIBSYSA-N D-methionine Chemical compound CSCC[C@@H](N)C(O)=O FFEARJCKVFRZRR-SCSAIBSYSA-N 0.000 description 11
- 244000005700 microbiome Species 0.000 description 11
- 230000003321 amplification Effects 0.000 description 10
- 125000001475 halogen functional group Chemical group 0.000 description 10
- 238000003199 nucleic acid amplification method Methods 0.000 description 10
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 9
- 239000004365 Protease Substances 0.000 description 9
- 108010076504 Protein Sorting Signals Proteins 0.000 description 9
- 230000015556 catabolic process Effects 0.000 description 9
- 230000006870 function Effects 0.000 description 9
- 230000010354 integration Effects 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 230000001105 regulatory effect Effects 0.000 description 9
- 241000680658 Bacillus deramificans Species 0.000 description 8
- 230000027455 binding Effects 0.000 description 8
- 238000006731 degradation reaction Methods 0.000 description 8
- 108091026890 Coding region Proteins 0.000 description 7
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 7
- 238000004422 calculation algorithm Methods 0.000 description 7
- 230000002759 chromosomal effect Effects 0.000 description 7
- 230000004927 fusion Effects 0.000 description 7
- 238000002955 isolation Methods 0.000 description 7
- 108020004999 messenger RNA Proteins 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- AGPKZVBTJJNPAG-RFZPGFLSSA-N D-Isoleucine Chemical compound CC[C@@H](C)[C@@H](N)C(O)=O AGPKZVBTJJNPAG-RFZPGFLSSA-N 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 102000035195 Peptidases Human genes 0.000 description 6
- 229920001218 Pullulan Polymers 0.000 description 6
- 239000004373 Pullulan Substances 0.000 description 6
- 239000004229 Alkannin Substances 0.000 description 5
- WHUUTDBJXJRKMK-GSVOUGTGSA-N D-glutamic acid Chemical compound OC(=O)[C@H](N)CCC(O)=O WHUUTDBJXJRKMK-GSVOUGTGSA-N 0.000 description 5
- KZSNJWFQEVHDMF-SCSAIBSYSA-N D-valine Chemical compound CC(C)[C@@H](N)C(O)=O KZSNJWFQEVHDMF-SCSAIBSYSA-N 0.000 description 5
- 241000196324 Embryophyta Species 0.000 description 5
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 5
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 229960005091 chloramphenicol Drugs 0.000 description 5
- 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 5
- 230000002538 fungal effect Effects 0.000 description 5
- 230000002068 genetic effect Effects 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 235000019419 proteases Nutrition 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
- 229920001817 Agar Polymers 0.000 description 4
- 108010065511 Amylases Proteins 0.000 description 4
- 108010059892 Cellulase Proteins 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 229920002472 Starch Polymers 0.000 description 4
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 4
- 241000223259 Trichoderma Species 0.000 description 4
- 239000008272 agar Substances 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 210000000349 chromosome Anatomy 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 238000010369 molecular cloning Methods 0.000 description 4
- 210000001938 protoplast Anatomy 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
- 241000193422 Bacillus lentus Species 0.000 description 3
- DCXYFEDJOCDNAF-UWTATZPHSA-N D-Asparagine Chemical compound OC(=O)[C@H](N)CC(N)=O DCXYFEDJOCDNAF-UWTATZPHSA-N 0.000 description 3
- CKLJMWTZIZZHCS-UHFFFAOYSA-N D-OH-Asp Natural products OC(=O)C(N)CC(O)=O CKLJMWTZIZZHCS-UHFFFAOYSA-N 0.000 description 3
- CKLJMWTZIZZHCS-UWTATZPHSA-N D-aspartic acid Chemical compound OC(=O)[C@H](N)CC(O)=O CKLJMWTZIZZHCS-UWTATZPHSA-N 0.000 description 3
- ZDXPYRJPNDTMRX-GSVOUGTGSA-N D-glutamine Chemical compound OC(=O)[C@H](N)CCC(N)=O ZDXPYRJPNDTMRX-GSVOUGTGSA-N 0.000 description 3
- ROHFNLRQFUQHCH-RXMQYKEDSA-N D-leucine Chemical compound CC(C)C[C@@H](N)C(O)=O ROHFNLRQFUQHCH-RXMQYKEDSA-N 0.000 description 3
- AYFVYJQAPQTCCC-STHAYSLISA-N D-threonine Chemical compound C[C@H](O)[C@@H](N)C(O)=O AYFVYJQAPQTCCC-STHAYSLISA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 210000004102 animal cell Anatomy 0.000 description 3
- 235000013405 beer Nutrition 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 230000008030 elimination Effects 0.000 description 3
- 238000003379 elimination reaction Methods 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 239000004744 fabric Substances 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 239000002243 precursor Substances 0.000 description 3
- 230000017854 proteolysis Effects 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 239000006188 syrup Substances 0.000 description 3
- 235000020357 syrup Nutrition 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 230000002103 transcriptional effect Effects 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 102000013142 Amylases Human genes 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 2
- 241000193749 Bacillus coagulans Species 0.000 description 2
- 241000194107 Bacillus megaterium Species 0.000 description 2
- 241000193388 Bacillus thuringiensis Species 0.000 description 2
- 241000193764 Brevibacillus brevis Species 0.000 description 2
- 101100292361 Colletotrichum gloeosporioides CAP5 gene Proteins 0.000 description 2
- XUJNEKJLAYXESH-UWTATZPHSA-N D-Cysteine Chemical compound SC[C@@H](N)C(O)=O XUJNEKJLAYXESH-UWTATZPHSA-N 0.000 description 2
- ONIBWKKTOPOVIA-SCSAIBSYSA-N D-Proline Chemical compound OC(=O)[C@H]1CCCN1 ONIBWKKTOPOVIA-SCSAIBSYSA-N 0.000 description 2
- MTCFGRXMJLQNBG-UWTATZPHSA-N D-Serine Chemical compound OC[C@@H](N)C(O)=O MTCFGRXMJLQNBG-UWTATZPHSA-N 0.000 description 2
- QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 2
- ODKSFYDXXFIFQN-SCSAIBSYSA-N D-arginine Chemical compound OC(=O)[C@H](N)CCCNC(N)=N ODKSFYDXXFIFQN-SCSAIBSYSA-N 0.000 description 2
- KDXKERNSBIXSRK-RXMQYKEDSA-N D-lysine Chemical compound NCCCC[C@@H](N)C(O)=O KDXKERNSBIXSRK-RXMQYKEDSA-N 0.000 description 2
- COLNVLDHVKWLRT-MRVPVSSYSA-N D-phenylalanine Chemical compound OC(=O)[C@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-MRVPVSSYSA-N 0.000 description 2
- OUYCCCASQSFEME-MRVPVSSYSA-N D-tyrosine Chemical compound OC(=O)[C@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-MRVPVSSYSA-N 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 241000192125 Firmicutes Species 0.000 description 2
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 2
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 description 2
- WTDRDQBEARUVNC-UHFFFAOYSA-N L-Dopa Natural products OC(=O)C(N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-UHFFFAOYSA-N 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
- 150000008575 L-amino acids Chemical class 0.000 description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- 125000002707 L-tryptophyl group Chemical group [H]C1=C([H])C([H])=C2C(C([C@](N([H])[H])(C(=O)[*])[H])([H])[H])=C([H])N([H])C2=C1[H] 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- 239000004367 Lipase Substances 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 241001557886 Trichoderma sp. Species 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 235000019418 amylase Nutrition 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 229940088710 antibiotic agent Drugs 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 235000013361 beverage Nutrition 0.000 description 2
- 108010079344 calcyclin-associated protein 50 Proteins 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 229940106157 cellulase Drugs 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 230000001276 controlling effect Effects 0.000 description 2
- 235000005822 corn Nutrition 0.000 description 2
- 210000004748 cultured cell Anatomy 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 230000007515 enzymatic degradation Effects 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 239000005090 green fluorescent protein Substances 0.000 description 2
- PSFDQSOCUJVVGF-UHFFFAOYSA-N harman Chemical compound C12=CC=CC=C2NC2=C1C=CN=C2C PSFDQSOCUJVVGF-UHFFFAOYSA-N 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 235000019421 lipase Nutrition 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 230000001323 posttranslational effect Effects 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 235000019423 pullulan Nutrition 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 239000004575 stone Substances 0.000 description 2
- 238000004809 thin layer chromatography Methods 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- SMWADGDVGCZIGK-AXDSSHIGSA-N (2s)-5-phenylpyrrolidine-2-carboxylic acid Chemical compound N1[C@H](C(=O)O)CCC1C1=CC=CC=C1 SMWADGDVGCZIGK-AXDSSHIGSA-N 0.000 description 1
- JWBYADXJYCNKIE-SYKZBELTSA-N (2s)-5-phenylpyrrolidine-2-carboxylic acid;(2s)-pyrrolidine-2-carboxylic acid Chemical compound OC(=O)[C@@H]1CCCN1.N1[C@H](C(=O)O)CCC1C1=CC=CC=C1 JWBYADXJYCNKIE-SYKZBELTSA-N 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 229930024421 Adenine Natural products 0.000 description 1
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 229920000945 Amylopectin Polymers 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241001513093 Aspergillus awamori Species 0.000 description 1
- 241000351920 Aspergillus nidulans Species 0.000 description 1
- 241000193752 Bacillus circulans Species 0.000 description 1
- 241001328122 Bacillus clausii Species 0.000 description 1
- 241000194103 Bacillus pumilus Species 0.000 description 1
- 108091033380 Coding strand Proteins 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- AHLPHDHHMVZTML-SCSAIBSYSA-N D-Ornithine Chemical compound NCCC[C@@H](N)C(O)=O AHLPHDHHMVZTML-SCSAIBSYSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- HNDVDQJCIGZPNO-RXMQYKEDSA-N D-histidine Chemical compound OC(=O)[C@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-RXMQYKEDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-SECBINFHSA-N D-tryptophane Chemical compound C1=CC=C2C(C[C@@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-SECBINFHSA-N 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 101150108358 GLAA gene Proteins 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 229920000209 Hexadimethrine bromide Polymers 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000619708 Homo sapiens Peroxiredoxin-6 Proteins 0.000 description 1
- 101000579123 Homo sapiens Phosphoglycerate kinase 1 Proteins 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- 101100429194 Hypocrea jecorina (strain QM6a) xyn2 gene Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- 125000000899 L-alpha-glutamyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C([H])([H])C(O[H])=O 0.000 description 1
- 125000000010 L-asparaginyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C(=O)N([H])[H] 0.000 description 1
- 125000000415 L-cysteinyl group Chemical group O=C([*])[C@@](N([H])[H])([H])C([H])([H])S[H] 0.000 description 1
- 125000002061 L-isoleucyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])[C@](C([H])([H])[H])([H])C(C([H])([H])[H])([H])[H] 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
- 125000002435 L-phenylalanyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 description 1
- 125000000174 L-prolyl group Chemical group [H]N1C([H])([H])C([H])([H])C([H])([H])[C@@]1([H])C(*)=O 0.000 description 1
- 125000002842 L-seryl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])O[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
- 108010029541 Laccase Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 240000003183 Manihot esculenta Species 0.000 description 1
- 235000016735 Manihot esculenta subsp esculenta Nutrition 0.000 description 1
- 108090000301 Membrane transport proteins Proteins 0.000 description 1
- 102000003939 Membrane transport proteins Human genes 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 125000002288 PGK1 group Chemical group 0.000 description 1
- 241000194109 Paenibacillus lautus Species 0.000 description 1
- 102100022239 Peroxiredoxin-6 Human genes 0.000 description 1
- 102100028251 Phosphoglycerate kinase 1 Human genes 0.000 description 1
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 241000235403 Rhizomucor miehei Species 0.000 description 1
- 241000831652 Salinivibrio sharmensis Species 0.000 description 1
- 108091081021 Sense strand Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 241000187398 Streptomyces lividans Species 0.000 description 1
- 241001468239 Streptomyces murinus Species 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 241000223262 Trichoderma longibrachiatum Species 0.000 description 1
- 241000223261 Trichoderma viride Species 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 108060008724 Tyrosinase Proteins 0.000 description 1
- 102000003425 Tyrosinase Human genes 0.000 description 1
- 108700040099 Xylose isomerases Proteins 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 239000000370 acceptor Substances 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 229960000643 adenine Drugs 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 229940054340 bacillus coagulans Drugs 0.000 description 1
- 229940097012 bacillus thuringiensis Drugs 0.000 description 1
- 230000003542 behavioural effect Effects 0.000 description 1
- UCMIRNVEIXFBKS-UHFFFAOYSA-N beta-alanine Chemical compound NCCC(O)=O UCMIRNVEIXFBKS-UHFFFAOYSA-N 0.000 description 1
- 150000001576 beta-amino acids Chemical class 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 230000021523 carboxylation Effects 0.000 description 1
- 238000006473 carboxylation reaction Methods 0.000 description 1
- 101150114858 cbh2 gene Proteins 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000011098 chromatofocusing Methods 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 230000003750 conditioning effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000012937 correction Methods 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
- 125000004122 cyclic group Chemical group 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007850 degeneration Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000009990 desizing Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000004821 distillation Methods 0.000 description 1
- 238000011143 downstream manufacturing Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 235000019985 fermented beverage Nutrition 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 235000003599 food sweetener Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 235000015203 fruit juice Nutrition 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000003144 genetic modification method Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 235000019534 high fructose corn syrup Nutrition 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000006317 isomerization reaction Methods 0.000 description 1
- 231100000518 lethal Toxicity 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 238000001471 micro-filtration Methods 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 125000000740 n-pentyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 235000014593 oils and fats Nutrition 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 239000000123 paper Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 238000005498 polishing Methods 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 235000012015 potatoes Nutrition 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 108020003519 protein disulfide isomerase Proteins 0.000 description 1
- 230000020978 protein processing Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000000734 protein sequencing Methods 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 239000008262 pumice Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000010845 search algorithm Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000009987 spinning Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000003151 transfection method Methods 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 101150016309 trpC gene Proteins 0.000 description 1
- 238000013060 ultrafiltration and diafiltration Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 235000014101 wine Nutrition 0.000 description 1
- FYGDTMLNYKFZSV-BYLHFPJWSA-N β-1,4-galactotrioside Chemical group O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@H](CO)O[C@@H](O[C@@H]2[C@@H](O[C@@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-BYLHFPJWSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2451—Glucanases acting on alpha-1,6-glucosidic bonds
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01041—Pullulanase (3.2.1.41)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2451—Glucanases acting on alpha-1,6-glucosidic bonds
- C12N9/2457—Pullulanase (3.2.1.41)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Cell Biology (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US83973506P | 2006-08-23 | 2006-08-23 | |
| US90324707P | 2007-02-23 | 2007-02-23 | |
| PCT/US2007/018523 WO2008024372A2 (en) | 2006-08-23 | 2007-08-21 | Pullulanase variants with increased productivity |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2009001717A true MX2009001717A (es) | 2009-02-25 |
Family
ID=38969548
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2009001717A MX2009001717A (es) | 2006-08-23 | 2007-08-21 | Variantes de pululanasa con productividad incrementada. |
Country Status (14)
| Country | Link |
|---|---|
| US (2) | US7968691B2 (https=) |
| EP (1) | EP2054512B1 (https=) |
| JP (1) | JP2010501181A (https=) |
| KR (1) | KR20090041410A (https=) |
| CN (2) | CN101506360B (https=) |
| BR (1) | BRPI0715619A2 (https=) |
| CA (2) | CA2663948C (https=) |
| CO (1) | CO6160247A2 (https=) |
| EA (1) | EA017712B1 (https=) |
| ES (1) | ES2547857T3 (https=) |
| HU (1) | HUE025068T2 (https=) |
| MX (1) | MX2009001717A (https=) |
| PL (1) | PL2054512T3 (https=) |
| WO (1) | WO2008024372A2 (https=) |
Families Citing this family (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7968691B2 (en) * | 2006-08-23 | 2011-06-28 | Danisco Us Inc. | Pullulanase variants with increased productivity |
| IN2012DN00427A (https=) | 2009-07-01 | 2015-05-15 | Bayer Bioscience Nv | |
| ES2676895T5 (es) | 2013-03-11 | 2022-04-27 | Danisco Us Inc | Variantes combinatorias de alfa-amilasa |
| EP3022300B1 (en) * | 2013-07-17 | 2018-07-11 | Novozymes A/S | Pullulanase chimeras and polynucleotides encoding same |
| BR112016009416A2 (pt) | 2013-10-28 | 2017-10-03 | Danisco Us Inc | Levedura seca ativa geneticamente modificada de grande escala |
| MX2016006489A (es) | 2013-11-20 | 2016-08-03 | Danisco Us Inc | Alfa-amilasas variantes que tienen susceptibilidad reducida a la escision por proteasas y metodos de uso. |
| WO2016062875A2 (en) | 2014-10-23 | 2016-04-28 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| CN108064306B (zh) | 2014-12-23 | 2022-11-01 | 营养与生物科学美国4公司 | 酶促产生的纤维素 |
| EP3253869A4 (en) * | 2015-02-04 | 2018-11-07 | Nanjing Bestzyme Bio-Engineering Co. Ltd. | Truncated pullulanases, methods of production, and methods of use thereof |
| US20180030456A1 (en) | 2015-02-19 | 2018-02-01 | Danisco Us Inc. | Enhanced protein expression |
| CN109071615A (zh) | 2016-03-04 | 2018-12-21 | 丹尼斯科美国公司 | 用于在微生物中产生蛋白质的工程化核糖体启动子 |
| CN105925594A (zh) * | 2016-06-13 | 2016-09-07 | 广西大学 | 生淀粉糖化酶及其制备方法与其在生淀粉水解和生料同步糖化发酵产酒精中的应用 |
| US20190367932A1 (en) | 2017-01-23 | 2019-12-05 | Danisco Us Inc. | Methods and compositions for obtaining natural comptence in bacillus host cells |
| JP7231228B2 (ja) | 2017-02-24 | 2023-03-01 | ダニスコ・ユーエス・インク | バチルス・リケニフォルミスにおける増加したタンパク質産生のための組成物及び方法 |
| EP3703661A1 (en) | 2017-11-02 | 2020-09-09 | Danisco US Inc. | Freezing point depressed solid matrix compositions for melt granulation of enzymes |
| KR102715197B1 (ko) | 2018-01-03 | 2024-10-08 | 다니스코 유에스 인크. | 증가된 단백질 생산을 위한 돌연변이체 및 유전자 변형된 바실러스 세포 및 이의 방법 |
| WO2020172465A1 (en) * | 2019-02-20 | 2020-08-27 | Duke University | Compositions and methods for the treatment of genetic diseases |
| CN110184258B (zh) * | 2019-06-11 | 2020-11-06 | 南京林业大学 | 一种普鲁兰酶突变体 |
| CN110791513B (zh) * | 2019-11-15 | 2021-05-25 | 中国科学院南海海洋研究所 | 一种密码子优化的玉足海参α-淀粉酶基因及其重组表达载体与应用 |
| CN111662933B (zh) * | 2020-06-24 | 2023-03-24 | 江南大学 | 一种利用重组酵母进行高支链淀粉酒精发酵的方法 |
| US12508305B2 (en) * | 2020-12-26 | 2025-12-30 | Duke University | Compositions and methods for treating and/or preventing glycogen storage disease type III |
| EP4387982A2 (en) * | 2021-08-20 | 2024-06-26 | Danisco US Inc. | Methods and compositions for enhanced protein production in bacillus cells |
| EP4525615A2 (en) | 2022-05-14 | 2025-03-26 | Novozymes A/S | Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4760025A (en) * | 1984-05-29 | 1988-07-26 | Genencor, Inc. | Modified enzymes and methods for making same |
| US5264366A (en) * | 1984-05-29 | 1993-11-23 | Genencor, Inc. | Protease deficient bacillus |
| US4683195A (en) * | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| DE3650202T3 (de) | 1985-08-29 | 2004-06-03 | Genencor International, Inc., South San Francisco | Expression von heterologen Polypeptiden in filamentösen Pilzen, Verfahren zu deren Herstellung und Vektoren zu deren Herstellung. |
| DK0605040T3 (da) * | 1992-12-28 | 2000-03-13 | Genencor Int | Pullulanase, mikroorganismer producerende denne fremgangsmåde il fremstilling af denne pullulanase og anvendelse deraf |
| US5605793A (en) * | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| US6537776B1 (en) * | 1999-06-14 | 2003-03-25 | Diversa Corporation | Synthetic ligation reassembly in directed evolution |
| JP4307563B2 (ja) * | 1997-04-07 | 2009-08-05 | ユニリーバー・ナームローゼ・ベンノートシャープ | 糸状菌、特にアスペルギルス属に属する糸状菌のアグロバクテリウム媒介性形質転換 |
| EP0981628A1 (en) * | 1997-05-06 | 2000-03-01 | E.I. Dupont De Nemours And Company | Corn pullulanase |
| JP2002505108A (ja) * | 1998-03-04 | 2002-02-19 | ジェネンコア インターナショナル インコーポレーテッド | プルラナーゼの修飾形態 |
| CN1415016B (zh) * | 1999-12-30 | 2012-07-11 | 金克克国际有限公司 | Trichoderma reesei木聚糖酶 |
| US6350599B1 (en) * | 2000-01-12 | 2002-02-26 | Novozymes A/S | Pullulanase variants and methods for preparing such variants with predetermined properties |
| AU2663801A (en) * | 2000-01-12 | 2001-07-24 | Novozymes A/S | Pullulanase variants and methods for preparing such variants with predetermined properties |
| US7886330B2 (en) | 2000-06-30 | 2011-02-08 | Jlb Ventures Llc | Enhanced home entertainment system with removable long-term storage |
| WO2002014490A2 (en) | 2000-08-11 | 2002-02-21 | Genencor International, Inc. | Bacillus transformation, transformants and mutant libraries |
| US7713725B2 (en) * | 2002-09-10 | 2010-05-11 | Danisco Us Inc. | Induction of gene expression using a high concentration sugar mixture |
| US7968691B2 (en) * | 2006-08-23 | 2011-06-28 | Danisco Us Inc. | Pullulanase variants with increased productivity |
-
2007
- 2007-08-20 US US11/841,526 patent/US7968691B2/en not_active Expired - Fee Related
- 2007-08-21 CN CN200780031317.XA patent/CN101506360B/zh not_active Expired - Fee Related
- 2007-08-21 BR BRPI0715619-7A patent/BRPI0715619A2/pt not_active Application Discontinuation
- 2007-08-21 HU HUE07837179A patent/HUE025068T2/en unknown
- 2007-08-21 MX MX2009001717A patent/MX2009001717A/es active IP Right Grant
- 2007-08-21 CN CN201410181518.XA patent/CN103898080B/zh not_active Expired - Fee Related
- 2007-08-21 EP EP20070837179 patent/EP2054512B1/en not_active Not-in-force
- 2007-08-21 CA CA2663948A patent/CA2663948C/en not_active Expired - Fee Related
- 2007-08-21 WO PCT/US2007/018523 patent/WO2008024372A2/en not_active Ceased
- 2007-08-21 CA CA2949536A patent/CA2949536A1/en not_active Abandoned
- 2007-08-21 PL PL07837179T patent/PL2054512T3/pl unknown
- 2007-08-21 JP JP2009525612A patent/JP2010501181A/ja active Pending
- 2007-08-21 ES ES07837179.6T patent/ES2547857T3/es active Active
- 2007-08-21 KR KR1020097003544A patent/KR20090041410A/ko not_active Abandoned
- 2007-08-21 EA EA200970212A patent/EA017712B1/ru not_active IP Right Cessation
-
2009
- 2009-02-20 CO CO09017236A patent/CO6160247A2/es unknown
-
2011
- 2011-02-28 US US13/036,749 patent/US8354101B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| KR20090041410A (ko) | 2009-04-28 |
| EA017712B1 (ru) | 2013-02-28 |
| US7968691B2 (en) | 2011-06-28 |
| JP2010501181A (ja) | 2010-01-21 |
| CO6160247A2 (es) | 2010-05-20 |
| WO2008024372A2 (en) | 2008-02-28 |
| EP2054512A2 (en) | 2009-05-06 |
| HK1135137A1 (en) | 2010-05-28 |
| BRPI0715619A2 (pt) | 2013-06-25 |
| CN103898080B (zh) | 2017-04-12 |
| US20080108126A1 (en) | 2008-05-08 |
| CA2663948C (en) | 2017-01-03 |
| US8354101B2 (en) | 2013-01-15 |
| CA2949536A1 (en) | 2008-02-28 |
| CN101506360A (zh) | 2009-08-12 |
| ES2547857T3 (es) | 2015-10-09 |
| EP2054512B1 (en) | 2015-04-22 |
| CA2663948A1 (en) | 2008-02-28 |
| HUE025068T2 (en) | 2016-01-28 |
| US20110281326A1 (en) | 2011-11-17 |
| PL2054512T3 (pl) | 2015-09-30 |
| CN101506360B (zh) | 2014-06-11 |
| EA200970212A1 (ru) | 2009-08-28 |
| WO2008024372A3 (en) | 2008-04-24 |
| CN103898080A (zh) | 2014-07-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7968691B2 (en) | Pullulanase variants with increased productivity | |
| EP3104717B1 (en) | Sucrose reduction and generation of insoluble fiber in juices | |
| JP2014236730A (ja) | 糸状菌の分野における新規発現調節配列および発現産物 | |
| EP3380496B1 (en) | Enhanced protein production and methods thereof | |
| ES2703753T3 (es) | Procedimiento de expresión | |
| US20210024908A1 (en) | Amylase mutant having high specific activity and thermal stability, gene of mutant, and applications thereof | |
| US9347107B2 (en) | Vector containing multiple nucleotide sequences for the expression of enzymes | |
| WO2016126294A1 (en) | Truncated pullulanases, methods of production, and methods of use thereof | |
| RU2642324C2 (ru) | Способ экспрессии | |
| US20250382601A1 (en) | Improved expression of recombinant proteins | |
| Yebra et al. | Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae | |
| CN120500529A (zh) | 折叠酶用于改善分泌分子的异源表达的用途 | |
| US11104909B2 (en) | α-amylase variant and use thereof | |
| EP3271447B1 (en) | A brewing method | |
| US10450539B2 (en) | Use of M4 metalloprotease in wort production | |
| HK1135137B (en) | Pullulanase variants with increased productivity | |
| Yoshino-Yasuda et al. | Sequence analysis and heterologous expression of rhamnogalacturonan lyase A gene (AsrglA) from Shoyu Koji mold, Aspergillus sojae KBN1340 | |
| WO2008060596A9 (en) | Enhanced protein production in t. reesei by co-expression of selected genes |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Grant or registration |