Substrate binding affinities of catalytic modules from cellulases

2014 Fiscal Year Final Research Report

• Project/Area Number: 24580476
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Boundary agriculture
• Research Institution: Mie University
• Principal Investigator: KARITA Shuichi 三重大学, 地域イノベーション学研究科, 教授 (90233999)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: セルラーゼ / バイオマス / 糖化 / 基質親和性

Outline of Final Research Achievements

Microorganisms produce multiple cellulases for degradation of biomass. Substrate affinities of these cellulolytic enzymes were examined. Three catalytic modules of enzymes, Cel5A, Cel5B, and Cel5E from Clostridium thermocellum were mutated to lose catalytic activities. Mutated proteins were tested for binding affinities of cellulosic substrates. Binding capacity to acid-swollen cellulose was Cel5B > Cel5A > Cel5E, whereas that to ball-milled cellulose was Cel5E>Cel5A>Cel5B. These enzymes are endoglucanases, however, substrate affinities of these catalytic modules depend on morphology of cellulosic substrates.

Free Research Field

応用微生物学