Analysis of the mechanism of efficient degradation of crystalline substrate by cellulases from Actinomycetes

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K07383
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Applied biochemistry
• Research Institution: The University of Tokyo
• 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)
• 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)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: Cellulase / Processivity / HS-AFM

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.

Free Research Field

酵素利用学