Research and Development

@article{Otagiri2013,

title = {Heterologous Expression and Characterization of a Glycoside Hydrolase Family 45 endo-β-1,4-Glucanase from a Symbiotic Protist of the Lower Termite, Reticulitermes speratus},

author = {Masato Otagiri and Crisanto M. Lopez and Katsuhiko Kitamoto and Manabu Arioka and Toshiaki Kudo and Shigeharu Moriya},

url = {https://link.springer.com/article/10.1007/s12010-012-9992-1},

doi = {10.1007/s12010-012-9992-1},

year  = {2013},

date = {2013-01-25},

journal = {Applied Biochemistry and Biotechnology},

volume = {169},

pages = {1910-1918},

abstract = {The termite symbiotic system is one of the efficient lignocellulose degradation systems. We tried to express and characterize a novel cellulolytic enzyme from this system. Here, we report the isolation of an endo-β-1,4-glucanase gene homolog of glycoside hydrolase family 45 from a symbiotic protistan community of Reticulitermes speratus. Heterologous expression of this gene was performed using the expression system of Aspergillus oryzae. Analysis of enzymatic properties revealed 786 μmol/min/mg protein in specific activity, a V max of 833.0 units/mg protein, and a K m value of 2.58 mg/ml with carboxymethyl cellulose as the substrate. Thin-layer chromatography analysis showed that RsSymEG2 produces cellobiose from cellodextrins larger than cellohexaose. This enzyme showed high specific activity like other endo-β-1,4-glucanases from the symbiotic system of termites. It means that the termite symbiotic system is a good resource for highly active endo-β-1,4-glucanases.},

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

pubstate = {published},

tppubtype = {article}

}