Journal
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Volume 160, Issue 4, Pages 1168-1178Publisher
HUMANA PRESS INC
DOI: 10.1007/s12010-009-8626-8
Keywords
Cellulase; Biomass; Termite; Protists
Funding
- New Energy and Industrial Technology Development Organization (NEDO)
- Eco-molecular Research Program (RIKEN)
- Bio-architect Research Program (RIKEN)
- Program for the Promotion of Basic Research Activity for Innovative Biosciences (PROBRAIN)
- Japanese Ministry of Education, Culture, Sports, Science and Technology
- Japanese National Commission for UNESCO
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RsSymEG, an endoglucanase of glycosyl hydrolase family (GHF) 7 encoded by a transcript isolated from the symbiotic protist of the termite Reticulitermes speratus, is expressed in Aspergillus oryzae. Interestingly, purified RsSymEG1 has a relatively higher specific activity (603 mu mol min(-1) mg(-1) protein) and V-max value (769.6 unit/mg protein) than previously reported data for GHF7 endoglucanase of Trichoderma ressei. It also has the same Km value (1.97 mg/ml) with Clostridium cellulolyticum enzymes that contain cellulose binding module, a property indicative of high affinity to substrate, though no cellulose binding module is found within it. Thin-layer chromatography analysis revealed that RsSymEG1 preferentially hydrolyzes the beta-1,4-cellulosic linkage of cellodextrins into cellobiose and glucose.
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