Analysis of the mechanism of efficient degradation of crystalline substrate by cellulases from Actinomycetes
| Project/Area Number |
15K07383
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
Uchiyama Taku 東京大学, 大学院農学生命科学研究科(農学部), 特任研究員 (70450658)
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| Co-Investigator(Renkei-kenkyūsha) |
UCHIHASHI TAKAYUKI 金沢大学, 理工研究領域数物科学系, 准教授 (30326300)
ISHIDA TAKUYA 東京大学, 大学院農学生命科学研究科森林化学研究室, 特任助教 (10714628)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | Cellulase / Processivity / HS-AFM |
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| Outline of Final Research Achievements |
Toward to the realization of “Biorefinery”, we aimed to increase the efficiency of enzymatic saccharification, and attempted to elucidate the enzymatic reaction mechanism involved in cellulases efficient crystalline cellulose degradation. Specifically, we attempted to elucidate such a mechanism through the biochemical experiment, HS-AFM observation, and protein crystal structure analysis of cellulase SaCel6B derived from Actinomycetes. As a result of experiments and observations, we found two amino acid residues involved in efficient crystalline cellulose degradation of cellulase SaCel6B and clarified the importance of these residues. Based on information of such amino acid residues, it could be possible to try to discover cellulases with highly saccharification efficiency or synthesize novel cellulases with high efficiency of saccharification.
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Report
(4 results)
Research Products
(10 results)
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[Journal Article] Single-molecule imaging analysis of binding, processive movement, and dissociation of cellobiohydrolase Trichoderma reesei Cel6A and its domains on crystalline cellulose2016
Author(s)
Nakamura A, Tasaki T, Ishiwata D, Yamamoto M, Okuni Y, Visootsat A, Maximilien M, Noji H, Uchiyama T, Samejima M, Igarashi K, Iino R
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Journal Title
J. Biol. Chem.
Volume: 291
Issue: 43
Pages: 22404-22413
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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[Journal Article] Development of simple random mutagenesis protocol for the protein expression system in Pichia pastoris2016
Author(s)
Tachioka, M., Sugimoto, N., Nakamura, A., Sunagawa, N., Ishida, T., Uchiyama, T., Igarashi, K., and Samejima, M.
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Journal Title
Biotechnol. Biofuels
Volume: 9
Issue: 1
Pages: 199-199
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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