Heterologous expression and characterization of an endoglucanase from a symbiotic protist of the lower termite, Reticulitermes speratus

Appl Biochem Biotechnol. 2010 Feb;160(4):1168-78. doi: 10.1007/s12010-009-8626-8. Epub 2009 Apr 29.

Abstract

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 micromol 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 K(m) 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspergillus oryzae / genetics
  • Cellulase / genetics*
  • Cellulase / metabolism
  • Chromatography, Thin Layer
  • Gene Expression
  • Hydrogen-Ion Concentration
  • Isoptera / microbiology
  • Kinetics
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Substrate Specificity
  • Symbiosis

Substances

  • Recombinant Proteins
  • Cellulase