Research and Development

@article{Todaka2009,

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

author = {Nemuri Todaka and Crisanto M. Lopez and Tetsushi Inoue and Kanako Saita and Jun-ichi Maruyama and Manabu Arioka and Katsuhiko Kitamoto and Toshiaki Kudo and Shigeharu Moriya},

url = {https://link.springer.com/article/10.1007/s12010-009-8626-8},

doi = {10.1007/s12010-009-8626-8},

year  = {2009},

date = {2009-04-29},

journal = {Applied Biochemistry and Biotechnology},

volume = {160},

pages = {1168-1178},

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 μmol 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 β-1,4-cellulosic linkage of cellodextrins into cellobiose and glucose.},

keywords = {biomass, cellulase, protists, termite},

pubstate = {published},

tppubtype = {article}

}