4.4 Article

Heterologous Expression and Characterization of an Endoglucanase from a Symbiotic Protist of the Lower Termite, Reticulitermes speratus

Journal

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Volume 160, Issue 4, Pages 1168-1178

Publisher

HUMANA PRESS INC
DOI: 10.1007/s12010-009-8626-8

Keywords

Cellulase; Biomass; Termite; Protists

Funding

  1. New Energy and Industrial Technology Development Organization (NEDO)
  2. Eco-molecular Research Program (RIKEN)
  3. Bio-architect Research Program (RIKEN)
  4. Program for the Promotion of Basic Research Activity for Innovative Biosciences (PROBRAIN)
  5. Japanese Ministry of Education, Culture, Sports, Science and Technology
  6. 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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