CN113874498A - 一种热稳定性葡萄糖氧化酶 - Google Patents
一种热稳定性葡萄糖氧化酶 Download PDFInfo
- Publication number
- CN113874498A CN113874498A CN202080039321.6A CN202080039321A CN113874498A CN 113874498 A CN113874498 A CN 113874498A CN 202080039321 A CN202080039321 A CN 202080039321A CN 113874498 A CN113874498 A CN 113874498A
- Authority
- CN
- China
- Prior art keywords
- glucose oxidase
- seq
- amino acid
- niger
- thermostable
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 108010015776 Glucose oxidase Proteins 0.000 title claims abstract description 139
- 239000004366 Glucose oxidase Substances 0.000 title claims abstract description 137
- 229940116332 glucose oxidase Drugs 0.000 title claims abstract description 137
- 235000019420 glucose oxidase Nutrition 0.000 title claims abstract description 137
- 241000228245 Aspergillus niger Species 0.000 claims abstract description 58
- 235000013305 food Nutrition 0.000 claims abstract description 8
- 239000000126 substance Substances 0.000 claims abstract description 7
- 125000000539 amino acid group Chemical group 0.000 claims description 29
- 230000035772 mutation Effects 0.000 claims description 25
- 210000004027 cell Anatomy 0.000 claims description 24
- 150000001413 amino acids Chemical group 0.000 claims description 16
- 101000904208 Aspergillus niger Glucose oxidase Proteins 0.000 claims description 12
- 102000040430 polynucleotide Human genes 0.000 claims description 12
- 108091033319 polynucleotide Proteins 0.000 claims description 12
- 239000002157 polynucleotide Substances 0.000 claims description 12
- 241000235058 Komagataella pastoris Species 0.000 claims description 8
- 102220306436 rs200293248 Human genes 0.000 claims description 8
- 102220640318 Aldehyde dehydrogenase, mitochondrial_T30V_mutation Human genes 0.000 claims description 7
- 102220097966 rs753204096 Human genes 0.000 claims description 7
- 102220492283 Replication stress response regulator SDE2_R37K_mutation Human genes 0.000 claims description 6
- 102220052934 rs188516326 Human genes 0.000 claims description 6
- 102220065478 rs201056963 Human genes 0.000 claims description 6
- 102200131194 rs3219154 Human genes 0.000 claims description 6
- 102220042823 rs35942089 Human genes 0.000 claims description 6
- 102220032610 rs63751278 Human genes 0.000 claims description 6
- 241000196324 Embryophyta Species 0.000 claims description 5
- 102220512241 Endosomal/lysosomal potassium channel TMEM175_S45T_mutation Human genes 0.000 claims description 4
- FFFHZYDWPBMWHY-VKHMYHEASA-N L-homocysteine Chemical group OC(=O)[C@@H](N)CCS FFFHZYDWPBMWHY-VKHMYHEASA-N 0.000 claims description 4
- 241000235648 Pichia Species 0.000 claims description 4
- 230000002538 fungal effect Effects 0.000 claims description 4
- 230000001580 bacterial effect Effects 0.000 claims description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 3
- 102220497076 5-hydroxytryptamine receptor 3B_T34V_mutation Human genes 0.000 claims description 2
- 102220470113 Aldo-keto reductase family 1 member C2_N43A_mutation Human genes 0.000 claims description 2
- 102220531710 Calcium channel flower homolog_I94A_mutation Human genes 0.000 claims description 2
- 108020004705 Codon Proteins 0.000 claims description 2
- 102220519462 Enoyl-CoA hydratase, mitochondrial_Q90A_mutation Human genes 0.000 claims description 2
- 102220502392 Putative C->U-editing enzyme APOBEC-4_E84A_mutation Human genes 0.000 claims description 2
- 102220492229 Replication stress response regulator SDE2_R37A_mutation Human genes 0.000 claims description 2
- 102220474378 Solute carrier family 13 member 3_S96A_mutation Human genes 0.000 claims description 2
- 102220470411 Thymosin beta-4_S16A_mutation Human genes 0.000 claims description 2
- 102200128633 rs104893843 Human genes 0.000 claims description 2
- 102220014109 rs397516918 Human genes 0.000 claims description 2
- 102220093746 rs876661027 Human genes 0.000 claims description 2
- 210000005253 yeast cell Anatomy 0.000 claims description 2
- 102220074220 rs796051883 Human genes 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 22
- 239000003814 drug Substances 0.000 abstract description 6
- 229940088598 enzyme Drugs 0.000 description 41
- 102000004190 Enzymes Human genes 0.000 description 40
- 108090000790 Enzymes Proteins 0.000 description 40
- 230000000694 effects Effects 0.000 description 35
- 239000000243 solution Substances 0.000 description 15
- 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 12
- 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 10
- 239000008103 glucose Substances 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 8
- 235000001014 amino acid Nutrition 0.000 description 8
- 238000000034 method Methods 0.000 description 8
- JRBJSXQPQWSCCF-UHFFFAOYSA-N 3,3'-Dimethoxybenzidine Chemical compound C1=C(N)C(OC)=CC(C=2C=C(OC)C(N)=CC=2)=C1 JRBJSXQPQWSCCF-UHFFFAOYSA-N 0.000 description 7
- 239000012153 distilled water Substances 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 229940024606 amino acid Drugs 0.000 description 6
- 239000000523 sample Substances 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 4
- 241000233866 Fungi Species 0.000 description 4
- 241001506991 Komagataella phaffii GS115 Species 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 230000031700 light absorption Effects 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 230000004151 fermentation Effects 0.000 description 3
- 230000006872 improvement Effects 0.000 description 3
- 238000010348 incorporation Methods 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 150000007523 nucleic acids Chemical group 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- 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 description 2
- KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 2
- 240000006439 Aspergillus oryzae Species 0.000 description 2
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 2
- 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 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 108091092195 Intron Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-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
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 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
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000005520 cutting process Methods 0.000 description 2
- 238000007865 diluting Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 102200082816 rs34868397 Human genes 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 239000011550 stock solution Substances 0.000 description 2
- 238000001308 synthesis method Methods 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- YASYEJJMZJALEJ-UHFFFAOYSA-N Citric acid monohydrate Chemical compound O.OC(=O)CC(O)(C(O)=O)CC(O)=O YASYEJJMZJALEJ-UHFFFAOYSA-N 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- RGHNJXZEOKUKBD-UHFFFAOYSA-N D-gluconic acid Natural products OCC(O)C(O)C(O)C(O)C(O)=O RGHNJXZEOKUKBD-UHFFFAOYSA-N 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000620209 Escherichia coli DH5[alpha] Species 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102220623346 Non-histone chromosomal protein HMG-14_V20C_mutation Human genes 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 241000235347 Schizosaccharomyces pombe Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241001052560 Thallis Species 0.000 description 1
- 241000499912 Trichoderma reesei Species 0.000 description 1
- 108091061763 Triple-stranded DNA Proteins 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 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
- 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 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000016383 Zea mays subsp huehuetenangensis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 239000003674 animal food additive Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 235000008429 bread Nutrition 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 229960002303 citric acid monohydrate Drugs 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000010168 coupling process Methods 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
- 238000006356 dehydrogenation reaction Methods 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 102000038379 digestive enzymes Human genes 0.000 description 1
- 108091007734 digestive enzymes Proteins 0.000 description 1
- 239000012470 diluted sample Substances 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 235000013312 flour Nutrition 0.000 description 1
- 239000005452 food preservative Substances 0.000 description 1
- 235000019249 food preservative Nutrition 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 239000000174 gluconic acid Substances 0.000 description 1
- 235000012208 gluconic acid Nutrition 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 235000009973 maize Nutrition 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 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
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 102220198042 rs121913407 Human genes 0.000 description 1
- 102220289587 rs1554918207 Human genes 0.000 description 1
- 102200082912 rs33926764 Human genes 0.000 description 1
- 102220075276 rs771805307 Human genes 0.000 description 1
- 102220101274 rs777100532 Human genes 0.000 description 1
- 102220061998 rs786203249 Human genes 0.000 description 1
- 102220103580 rs863224363 Human genes 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 150000003588 threonines Chemical group 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- AURFVNDXGLQSNN-UHFFFAOYSA-K trisodium 2-hydroxypropane-1,2,3-tricarboxylic acid phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O.OC(=O)CC(O)(C(O)=O)CC(O)=O AURFVNDXGLQSNN-UHFFFAOYSA-K 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
- 238000012795 verification Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000005303 weighing Methods 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
- C12N15/815—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts for yeasts other than Saccharomyces
-
- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- 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)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/645—Fungi ; Processes using fungi
- C12R2001/66—Aspergillus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
- C12R2001/00—Microorganisms ; Processes using microorganisms
- C12R2001/645—Fungi ; Processes using fungi
- C12R2001/84—Pichia
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/03—Oxidoreductases acting on the CH-OH group of donors (1.1) with a oxygen as acceptor (1.1.3)
- C12Y101/03004—Glucose oxidase (1.1.3.4)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Medicinal Chemistry (AREA)
- Mycology (AREA)
- Cell Biology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
提供了一种通过在野生型黑曲霉葡萄糖氧化酶或突变型黑曲霉葡萄糖氧化酶的氨基酸序列中引入至少一对二硫键获得的热稳定性葡萄糖氧化酶。该葡萄糖氧化酶适合应用于食品、化工、医药、农业和饲料领域中。
Description
PCT国内申请，说明书已公开。
Claims (27)
- PCT国内申请，权利要求书已公开。
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201910469009 | 2019-05-31 | ||
| CN201910469009X | 2019-05-31 | ||
| PCT/CN2020/093205 WO2020239064A1 (zh) | 2019-05-31 | 2020-05-29 | 一种热稳定性葡萄糖氧化酶 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN113874498A true CN113874498A (zh) | 2021-12-31 |
Family
ID=73553508
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202080039321.6A Pending CN113874498A (zh) | 2019-05-31 | 2020-05-29 | 一种热稳定性葡萄糖氧化酶 |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US20220220454A1 (zh) |
| EP (1) | EP3978602A4 (zh) |
| CN (1) | CN113874498A (zh) |
| WO (1) | WO2020239064A1 (zh) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114736879A (zh) * | 2022-06-09 | 2022-07-12 | 中国农业科学院北京畜牧兽医研究所 | 热稳定性改善的葡萄糖氧化酶GoxM10突变体E361P及其衍生突变体和应用 |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112760299B (zh) * | 2021-02-06 | 2022-06-10 | 江南大学 | 热稳定性提高的葡萄糖氧化酶突变体及其编码基因和应用 |
| WO2023225459A2 (en) | 2022-05-14 | 2023-11-23 | Novozymes A/S | Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1238009A (zh) * | 1996-07-24 | 1999-12-08 | 衣阿华州立大学研究基金会股份有限公司 | 提高葡糖淀粉酶pH最适点、底物专一性和热稳定性的蛋白质工程方法 |
| US20160002609A1 (en) * | 2013-01-28 | 2016-01-07 | Roche Diabetes Care, Inc. | Glucose Oxidase Variants, As Well As Compositions, Devices, Kits and Uses Thereof |
| CN108251389A (zh) * | 2017-08-18 | 2018-07-06 | 青岛蔚蓝生物集团有限公司 | 一种耐热性提高的葡萄糖氧化酶突变体 |
| US10233430B1 (en) * | 2017-10-13 | 2019-03-19 | Dongguan Apac Biotechnology Co.,Ltd. | Glucose oxidase having improved thermostability |
| CN109666657A (zh) * | 2017-10-13 | 2019-04-23 | 东莞泛亚太生物科技有限公司 | 提升耐热性的葡萄糖氧化酶 |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5266688A (en) * | 1988-06-21 | 1993-11-30 | Chiron Corporation | Polynucleotide sequence for production of glucose oxidase in recombinant systems |
| US6537792B1 (en) * | 1996-07-24 | 2003-03-25 | Iowa State University | Protein engineering of glucoamylase to increase pH optimum, substrate specificity and thermostability |
| EP2796547B1 (en) | 2013-04-24 | 2016-09-14 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Novel glucose oxidase variants |
| CN108795891B (zh) * | 2017-04-26 | 2021-03-26 | 中国农业科学院北京畜牧兽医研究所 | 一种葡萄糖氧化酶CnGODA及其基因与应用 |
| CN107858338B (zh) * | 2017-11-29 | 2020-05-15 | 华南农业大学 | 一种组合二硫键的耐热突变脂肪酶及其制备方法与应用 |
| CN108913675B (zh) * | 2018-07-09 | 2020-05-22 | 华南理工大学 | 一种热稳定性提高的脂肪酶突变体及其应用 |
| CN109706137B (zh) * | 2019-01-21 | 2021-02-19 | 天津科技大学 | 一种通过增加二硫键提高肝素酶i热稳定性的突变体及制备方法 |
-
2020
- 2020-05-29 EP EP20814947.6A patent/EP3978602A4/en active Pending
- 2020-05-29 WO PCT/CN2020/093205 patent/WO2020239064A1/zh unknown
- 2020-05-29 US US17/615,342 patent/US20220220454A1/en active Pending
- 2020-05-29 CN CN202080039321.6A patent/CN113874498A/zh active Pending
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1238009A (zh) * | 1996-07-24 | 1999-12-08 | 衣阿华州立大学研究基金会股份有限公司 | 提高葡糖淀粉酶pH最适点、底物专一性和热稳定性的蛋白质工程方法 |
| US20160002609A1 (en) * | 2013-01-28 | 2016-01-07 | Roche Diabetes Care, Inc. | Glucose Oxidase Variants, As Well As Compositions, Devices, Kits and Uses Thereof |
| CN108251389A (zh) * | 2017-08-18 | 2018-07-06 | 青岛蔚蓝生物集团有限公司 | 一种耐热性提高的葡萄糖氧化酶突变体 |
| US10233430B1 (en) * | 2017-10-13 | 2019-03-19 | Dongguan Apac Biotechnology Co.,Ltd. | Glucose oxidase having improved thermostability |
| CN109666657A (zh) * | 2017-10-13 | 2019-04-23 | 东莞泛亚太生物科技有限公司 | 提升耐热性的葡萄糖氧化酶 |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114736879A (zh) * | 2022-06-09 | 2022-07-12 | 中国农业科学院北京畜牧兽医研究所 | 热稳定性改善的葡萄糖氧化酶GoxM10突变体E361P及其衍生突变体和应用 |
| CN114736879B (zh) * | 2022-06-09 | 2022-09-27 | 中国农业科学院北京畜牧兽医研究所 | 热稳定性改善的葡萄糖氧化酶GoxM10突变体E361P及其衍生突变体和应用 |
Also Published As
| Publication number | Publication date |
|---|---|
| US20220220454A1 (en) | 2022-07-14 |
| EP3978602A1 (en) | 2022-04-06 |
| WO2020239064A1 (zh) | 2020-12-03 |
| EP3978602A4 (en) | 2023-07-05 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN111349622B (zh) | 一种葡萄糖氧化酶突变体及其在工业化生产中的应用 | |
| CN113874498A (zh) | 一种热稳定性葡萄糖氧化酶 | |
| CN112301009B (zh) | 热稳定性提高的葡萄糖氧化酶突变体god及其基因和应用 | |
| CN113862233B (zh) | 提高葡萄糖氧化酶的酸稳定性的方法及突变体q241e/r499e、基因和应用 | |
| CN105950578A (zh) | 耐热的葡萄糖氧化酶突变体及其编码基因和应用 | |
| CN105950577A (zh) | 热稳定性提高的葡萄糖氧化酶突变体及其编码基因和应用 | |
| CN108118037B (zh) | 一种耐热性提高的葡萄糖氧化酶突变体 | |
| CN110713996B (zh) | 一种海藻糖酶及其载体与应用 | |
| CN112760299B (zh) | 热稳定性提高的葡萄糖氧化酶突变体及其编码基因和应用 | |
| CN108118038B (zh) | 一种葡萄糖氧化酶突变体 | |
| CN108251391A (zh) | 新型葡萄糖氧化酶突变体 | |
| CN108118036B (zh) | 新型葡萄糖氧化酶突变体 | |
| CN109666657B (zh) | 提升耐热性的葡萄糖氧化酶 | |
| CN113493799B (zh) | 一株高产酸性乳糖酶的黑曲霉菌株 | |
| CN108251390A (zh) | 一种葡萄糖氧化酶突变体 | |
| CN107988177B (zh) | 葡萄糖氧化酶突变体 | |
| CN114736880B (zh) | 酸稳定性提高葡萄糖氧化酶GoxM10的突变体D497N及其衍生突变体和应用 | |
| CN114736881B (zh) | 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 | |
| CN109423483B (zh) | 葡萄糖氧化酶突变体 | |
| CN108795891B (zh) | 一种葡萄糖氧化酶CnGODA及其基因与应用 | |
| CN112877306B (zh) | 一种超耐热葡萄糖氧化酶AtGOD及其基因和应用 | |
| CN108034642B (zh) | 葡萄糖氧化酶CnGOD19及其改良酶、基因和应用 | |
| CN114181288B (zh) | 制备l-缬氨酸的方法及其所用的基因与该基因编码的蛋白质 | |
| WO2015008637A1 (ja) | キサンチンオキシダーゼ遺伝子とそれをコードするアミノ酸配列 | |
| CN116063417A (zh) | Bbd29_14255基因突变体及其在制备l-谷氨酸中的应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination |