JP2016015894A - β−グルコシダーゼ - Google Patents
β−グルコシダーゼ Download PDFInfo
- Publication number
- JP2016015894A JP2016015894A JP2014138557A JP2014138557A JP2016015894A JP 2016015894 A JP2016015894 A JP 2016015894A JP 2014138557 A JP2014138557 A JP 2014138557A JP 2014138557 A JP2014138557 A JP 2014138557A JP 2016015894 A JP2016015894 A JP 2016015894A
- Authority
- JP
- Japan
- Prior art keywords
- glucosidase
- amino acid
- protein
- activity
- substitution
- 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
- 108010047754 beta-Glucosidase Proteins 0.000 title claims abstract description 43
- 102000006995 beta-Glucosidase Human genes 0.000 title claims abstract description 43
- 230000000694 effects Effects 0.000 claims abstract description 48
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 42
- 235000018102 proteins Nutrition 0.000 claims abstract description 40
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 40
- 125000000539 amino acid group Chemical group 0.000 claims abstract description 27
- 230000035772 mutation Effects 0.000 claims abstract description 23
- 101710099628 Beta-glucosidase 1 Proteins 0.000 claims abstract description 14
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims abstract description 14
- 235000013922 glutamic acid Nutrition 0.000 claims abstract description 14
- 239000004220 glutamic acid Substances 0.000 claims abstract description 14
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims abstract description 9
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims abstract description 9
- 238000006467 substitution reaction Methods 0.000 claims description 17
- 150000001413 amino acids Chemical group 0.000 claims description 16
- 108010059892 Cellulase Proteins 0.000 claims description 15
- 239000013604 expression vector Substances 0.000 claims description 9
- 239000003795 chemical substances by application Substances 0.000 claims description 8
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 7
- 239000004474 valine Substances 0.000 claims description 7
- 241000228212 Aspergillus Species 0.000 claims description 6
- 229930182817 methionine Natural products 0.000 claims description 5
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 4
- 239000004475 Arginine Substances 0.000 claims description 3
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 3
- 239000004473 Threonine Substances 0.000 claims description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 3
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims description 2
- 101710081627 Beta-glucosidase 1A Proteins 0.000 claims 1
- 150000002309 glutamines Chemical class 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 19
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 abstract description 5
- 241000228215 Aspergillus aculeatus Species 0.000 abstract description 4
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 abstract 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 34
- 108090000790 Enzymes Proteins 0.000 description 34
- 229940088598 enzyme Drugs 0.000 description 34
- 101150100570 bglA gene Proteins 0.000 description 25
- 102000004366 Glucosidases Human genes 0.000 description 21
- 108010056771 Glucosidases Proteins 0.000 description 21
- 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 19
- 235000001014 amino acid Nutrition 0.000 description 17
- 239000000758 substrate Substances 0.000 description 15
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 13
- 239000008103 glucose Substances 0.000 description 13
- 101100437484 Arabidopsis thaliana BGLU18 gene Proteins 0.000 description 10
- 101100342633 Bos taurus LLGL1 gene Proteins 0.000 description 10
- 101100065855 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) EXG1 gene Proteins 0.000 description 10
- 101100058298 Saccharomycopsis fibuligera BGL1 gene Proteins 0.000 description 10
- 210000004027 cell Anatomy 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 238000000034 method Methods 0.000 description 9
- 229920002678 cellulose Polymers 0.000 description 8
- 239000001913 cellulose Substances 0.000 description 8
- 239000002609 medium Substances 0.000 description 8
- 240000006439 Aspergillus oryzae Species 0.000 description 7
- 102220576074 HLA class I histocompatibility antigen, B alpha chain_E69M_mutation Human genes 0.000 description 7
- 229940106157 cellulase Drugs 0.000 description 7
- 244000005700 microbiome Species 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 239000013613 expression plasmid Substances 0.000 description 6
- 238000012216 screening Methods 0.000 description 6
- IFBHRQDFSNCLOZ-RMPHRYRLSA-N 4-nitrophenyl beta-D-glucoside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC=C([N+]([O-])=O)C=C1 IFBHRQDFSNCLOZ-RMPHRYRLSA-N 0.000 description 5
- 239000002028 Biomass Substances 0.000 description 5
- 102000005575 Cellulases Human genes 0.000 description 5
- 108010084185 Cellulases Proteins 0.000 description 5
- 108020004705 Codon Proteins 0.000 description 5
- 241000223259 Trichoderma Species 0.000 description 5
- 238000012258 culturing Methods 0.000 description 5
- 241000233866 Fungi Species 0.000 description 4
- 241000499912 Trichoderma reesei Species 0.000 description 4
- 239000012228 culture supernatant Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 241000282326 Felis catus Species 0.000 description 3
- 239000002585 base Substances 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 229930182478 glucoside Natural products 0.000 description 3
- 235000014304 histidine Nutrition 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 230000008929 regeneration Effects 0.000 description 3
- 238000011069 regeneration method Methods 0.000 description 3
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 3
- 101150105426 BGL1 gene Proteins 0.000 description 2
- 102220504540 Cyclin-dependent kinase inhibitor 2A_E69V_mutation Human genes 0.000 description 2
- 102220589468 DNA repair protein XRCC4_E69R_mutation Human genes 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 150000008575 L-amino acids Chemical class 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-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
- 241000209094 Oryza Species 0.000 description 2
- 235000007164 Oryza sativa Nutrition 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 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 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000012043 crude product Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 150000008131 glucosides Chemical class 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 239000012264 purified product Substances 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 235000009566 rice Nutrition 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000010902 straw Substances 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- QIGJYVCQYDKYDW-UHFFFAOYSA-N 3-O-alpha-D-mannopyranosyl-D-mannopyranose Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(CO)OC(O)C1O QIGJYVCQYDKYDW-UHFFFAOYSA-N 0.000 description 1
- OPIFSICVWOWJMJ-LNNRFACYSA-N 5-bromo-4-chloro-3-indolyl beta-D-glucoside 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-LNNRFACYSA-N 0.000 description 1
- 241000228245 Aspergillus niger Species 0.000 description 1
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 102220504489 Cyclin-dependent kinase inhibitor 2A_E69G_mutation Human genes 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- 241000701533 Escherichia virus T4 Species 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 229920002488 Hemicellulose Polymers 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
- 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
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- AYRXSINWFIIFAE-UHFFFAOYSA-N O6-alpha-D-Galactopyranosyl-D-galactose Natural products OCC1OC(OCC(O)C(O)C(O)C(O)C=O)C(O)C(O)C1O AYRXSINWFIIFAE-UHFFFAOYSA-N 0.000 description 1
- 241000205156 Pyrococcus furiosus Species 0.000 description 1
- 241000193448 Ruminiclostridium thermocellum Species 0.000 description 1
- 239000004147 Sorbitan trioleate Substances 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 241000204666 Thermotoga maritima Species 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 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
- 239000008351 acetate buffer Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- DLRVVLDZNNYCBX-CQUJWQHSSA-N gentiobiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)C(O)O1 DLRVVLDZNNYCBX-CQUJWQHSSA-N 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 229940059442 hemicellulase Drugs 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 150000002411 histidines Chemical class 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000011090 industrial biotechnology method and process Methods 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000012933 kinetic analysis Methods 0.000 description 1
- QIGJYVCQYDKYDW-LCOYTZNXSA-N laminarabiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@H]1[C@H](O)[C@@H](CO)OC(O)[C@@H]1O QIGJYVCQYDKYDW-LCOYTZNXSA-N 0.000 description 1
- 229920005610 lignin Polymers 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 239000006225 natural substrate Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000010893 paper waste Substances 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000006276 transfer reaction Methods 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
Description
立体構造情報を元にセロビオース(C2)の認識に関わる可能性がある、活性部位周辺のアミノ酸を13箇所(W68、E69、R98、D99、R200、Q201、E204、Y248、F305、W358、S436、D437、Y511)選抜した。PCR法を用いて、bgl1遺伝子に部位特異的飽和変異を導入して変異ライブラリを構築し、S. cerevisiae DC5 株を宿主として、C2に対する活性が向上した変異酵素のスクリーニングを行った。
実施例1でスクリーニングされた9種類の変異酵素を糸状菌で発現させ、その酵素活性などについて調べた。
部位特異的飽和変異を導入するために、表4に示すプライマーを作製した。これらのプライマーを用いて実施例1と同様の方法で2段階のPCRによりオリゴDNA断片を増幅した。増幅したbgl1断片は、糸状菌用の高発現ベクターと共にNot IとSph Iにより消化し、ライゲーションを行うことで糸状菌用高発現ベクターを作製した。
各アミノ酸置換において最もC2に対する触媒効率を上昇させたE69M、Q201Eに加えて、比活性を向上させたS436Vの3種類のアミノ酸置換を組み合わせた二重変異体(E69M/Q201E、Q201E/S436V、E69M/S436V)、及び三重変異体 (E69M/Q201E/S436V) の作製を行った。表4に示すプライマーと鋳型プラスミドを用いて、実施例1と同様にして糸状菌用高発現プラスミドの構築を行った。PCRにおいては、表6及び表7に示すプライマーセットを用いた。また、実施例1と同様にして精製した二重変異体及び三重変異体を用いて酵素活性及び酵素特性を調べた。その結果を表8と図6に示した
Claims (10)
- アスペルギルス・アキュレータス由来の野生型β−グルコシダーゼ1のアミノ酸配列と90%以上の同一性を有するアミノ酸配列と、
前記野生型β−グルコシダーゼ1の68番目、69番目、98番目、99番目、200番目、201番目、204番目、248番目、305番目、358番目、436番目、437番目、511番目に対応する位置のアミノ酸残基のうちいずれか1又は2箇所以上のアミノ酸残基が異なるアミノ酸残基に置換された変異と、
を有するタンパク質。 - 前記野生型β−グルコシダーゼ1に対して90%以上のβ−グルコシダーゼ活性を有する請求項1に記載のタンパク質。
- 前記野生型β−グルコシダーゼ1の69番目、201番目、436番目に対応する位置のアミノ酸残基のうちのいずれか1又は2以上のアミノ酸残基が異なるアミノ酸残基に置換された変異を有する請求項1又は2に記載のタンパク質。
- 69番目のグルタミン酸のバリン又はアルギニン又はメチオニンへの置換、201番目のグルタミンのグルタミン酸への置換、436番目のセリンのバリン又はスレオニンへの置換の何れか1又は2以上の変異を有する請求項1〜3の何れか1項に記載のタンパク質。
- 201番目のグルタミンのグルタミン酸への置換と、436番目のセリンのバリンへの置換の変異を有する請求項1又は2に記載のタンパク質。
- さらに69番目のグルタミン酸のメチオニンへの置換の変異を含む請求項5に記載のタンパク質。
- 請求項1〜6の何れか1項に記載のタンパク質をコードするDNA。
- 請求項7に記載のDNAを含む発現ベクター。
- 請求項7に記載のDNAを発現可能に含む組換え体。
- 請求項1〜6の何れか1項に記載のタンパク質、又は請求項9に記載の組換え体の処理物を含むセルラーゼ酵素剤。
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2014138557A JP6449573B2 (ja) | 2014-07-04 | 2014-07-04 | β−グルコシダーゼ |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2014138557A JP6449573B2 (ja) | 2014-07-04 | 2014-07-04 | β−グルコシダーゼ |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2016015894A true JP2016015894A (ja) | 2016-02-01 |
JP6449573B2 JP6449573B2 (ja) | 2019-01-09 |
Family
ID=55231674
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2014138557A Active JP6449573B2 (ja) | 2014-07-04 | 2014-07-04 | β−グルコシダーゼ |
Country Status (1)
Country | Link |
---|---|
JP (1) | JP6449573B2 (ja) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2019163886A1 (ja) * | 2018-02-26 | 2019-08-29 | 花王株式会社 | 変異β-グルコシダーゼ |
WO2019167788A1 (ja) * | 2018-02-27 | 2019-09-06 | 花王株式会社 | 変異β-グルコシダーゼ |
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 (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2012128260A1 (ja) * | 2011-03-24 | 2012-09-27 | 旭硝子株式会社 | シゾサッカロミセス属酵母の形質転換体、該形質転換体の製造方法、β-グルコシダーゼの製造方法、およびセルロースの分解方法 |
-
2014
- 2014-07-04 JP JP2014138557A patent/JP6449573B2/ja active Active
Patent Citations (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2012128260A1 (ja) * | 2011-03-24 | 2012-09-27 | 旭硝子株式会社 | シゾサッカロミセス属酵母の形質転換体、該形質転換体の製造方法、β-グルコシダーゼの製造方法、およびセルロースの分解方法 |
Non-Patent Citations (2)
Title |
---|
BIOCHEM. J., vol. Vol.452, JPN6018016497, 2013, pages 211 - 221 * |
BIOMOLECULES, vol. Vol.3, JPN6018016494, 2013, pages 612 - 631 * |
Cited By (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2019163886A1 (ja) * | 2018-02-26 | 2019-08-29 | 花王株式会社 | 変異β-グルコシダーゼ |
JP2019146499A (ja) * | 2018-02-26 | 2019-09-05 | 花王株式会社 | 変異β−グルコシダーゼ |
US11261436B2 (en) | 2018-02-26 | 2022-03-01 | Kao Corporation | Mutant β-glucosidase |
JP7051491B2 (ja) | 2018-02-26 | 2022-04-11 | 花王株式会社 | 変異β-グルコシダーゼ |
WO2019167788A1 (ja) * | 2018-02-27 | 2019-09-06 | 花王株式会社 | 変異β-グルコシダーゼ |
US11225679B2 (en) | 2018-02-27 | 2022-01-18 | Kao Corporation | Mutant β-glucosidase |
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 |
Also Published As
Publication number | Publication date |
---|---|
JP6449573B2 (ja) | 2019-01-09 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Morimoto et al. | Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain | |
US9447400B2 (en) | Beta-glucosidase I variants with improved properties | |
Anand et al. | Characteristics of thermostable endoxylanase and β-xylosidase of the extremely thermophilic bacterium Geobacillus thermodenitrificans TSAA1 and its applicability in generating xylooligosaccharides and xylose from agro-residues | |
Sharma et al. | Evaluation of glycosyl hydrolases in the secretome of Aspergillus fumigatus and saccharification of alkali-treated rice straw | |
Singhvi et al. | Comparative production of cellulases by mutants of Penicillium janthinellum NCIM 1171 and its application in hydrolysis of Avicel and cellulose | |
CA3021166A1 (en) | Heterologous expression of fungal cellobiohydrolases in yeast | |
Rai et al. | Evaluation of secretome of highly efficient lignocellulolytic Penicillium sp. Dal 5 isolated from rhizosphere of conifers | |
JP2014503185A (ja) | 熱安定性トリコデルマ(trichoderma)セルラーゼ | |
Chen et al. | A highly active beta-glucanase from a new strain of rumen fungus Orpinomyces sp. Y102 exhibits cellobiohydrolase and cellotriohydrolase activities | |
Huang et al. | Improved expression and characterization of a multidomain xylanase from Thermoanaerobacterium aotearoense SCUT27 in Bacillus subtilis | |
US20180371443A1 (en) | Novel cellulase complex, and glycosidase hydrolases thereof, and methods of using thereof | |
JP6449573B2 (ja) | β−グルコシダーゼ | |
US11242514B2 (en) | Endocellulases and uses thereof | |
Loaces et al. | EndoG: A novel multifunctional halotolerant glucanase and xylanase isolated from cow rumen | |
US9580702B2 (en) | Thermostable cellobiohydrolase and amino acid substituted variant thereof | |
JP2015173602A (ja) | 酵素の自然変異体の取得方法及び超耐熱性セロビオハイドロラーゼ | |
Zhou et al. | Purification and properties of a psychrotrophic Trichoderma sp. xylanase and its gene sequence | |
Ramoni et al. | Trichoderma reesei xylanase 5 is defective in the reference strain QM6a but functional alleles are present in other wild-type strains | |
WO2010101158A1 (ja) | クロストリジウム セルロボランス由来新規遺伝子及びその利用 | |
US9725749B2 (en) | Glycoside hydrolases having multiple hydrolase activities | |
JP2016049035A (ja) | Ghファミリー10に属する耐熱性キシラナーゼ | |
JP6950873B2 (ja) | セルラーゼ及びキシラナーゼを生産するための変異株アスペルギルス・アクレアツス並びにその調製方法 | |
JP7051491B2 (ja) | 変異β-グルコシダーゼ | |
Park et al. | Cloning and sequencing of an exoglucanase gene from Streptomyces sp. M23, and its expression in Streptomyces lividans TK-24 | |
JP2011223962A (ja) | 新規セルラーゼ |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20170627 |
|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20170630 |
|
A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20171113 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20171113 |
|
A977 | Report on retrieval |
Free format text: JAPANESE INTERMEDIATE CODE: A971007 Effective date: 20180425 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20180515 |
|
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: 20181127 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20181206 |
|
R151 | Written notification of patent or utility model registration |
Ref document number: 6449573 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R151 |
|
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 |