Cloning of an endoglycanase gene from Paenibacillus cookii and characterization of the recombinant enzyme

Abstract

An endoglycanase gene of Paenibacillus cookii SS-24 was cloned and sequenced. This Pgl8A gene had an open reading frame of 1,230 bp that encoded a putative signal sequence (31 amino acids) and mature enzyme (378 amino acids: 41,835 Da). The enzyme was most homologous to a β-1,3-1,4-glucanase of Bacillus circulans WL-12 with 84% identity. The recombinant enzyme hydrolyzed carboxymethyl cellulose, swollen celluloses, chitosan and lichenan but not Avicel, chitin powder or xylan. With chitosan as the substrate, the optimum temperature and hydrolysis products of the recombinant enzyme varied at pH 4.0 and 8.0. This is the first report that characterizes chitosanase activity under different pH conditions.

DOI: 10.1007/s10529-011-0759-5

Extracted Key Phrases

3 Figures and Tables

050100150201220132014201520162017
Citations per Year

123 Citations

Semantic Scholar estimates that this publication has 123 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Shinoda2011CloningOA, title={Cloning of an endoglycanase gene from Paenibacillus cookii and characterization of the recombinant enzyme}, author={Suguru Shinoda and Shin Kanamasa and Motoo Arai}, journal={Biotechnology Letters}, year={2011}, volume={34}, pages={281-286} }