Direct detection, cloning and characterization of a glucoside hydrolase from forest soil.

Hua, Mei; Zhao, Shubo; Zhang, Lili; Liu, Dongbo; Xia, Hongmei; Li, Fan; Chen, Shan

A glucoside hydrolase gene, egl01, was cloned from the soil DNA of Changbai Mountain forest by homologous PCR amplification. The deduced sequence of 517 amino acids included a catalytic domain of glycoside hydrolase family 5 and was homologous to a putative cellulase from Bacillus licheniformis. The recombinant enzyme, Egl01, was maximally active at pH 5 and 50 °C and it was stable at pH 3-9, 4-50 °C, and also stable in the presence of metal ions, organic solvents, surfactants and salt. Its activity was above 120 % in 2-3 M NaCl/KCl and over 70 % was retained in 1-4 M NaCl/KCl for 6d. Egl01 hydrolyzed carboxymethyl cellulose, beechwood xylan, crop stalk, laminarin, filter paper, and avicel but not pNPG, indicating its broad substrate specificity. These properties make this recombinant enzyme a promising candidate for industrial applications.

GLUCOSIDES; HYDROLASES; FOREST soils; MOLECULAR cloning; BACILLUS licheniformis; POLYMERASE chain reaction; RECOMBINANT proteins; ORGANIC solvents

Biotechnology Letters, 2015, Vol 37, Issue 6, p1227

0141-5492

Academic Journal

10.1007/s10529-015-1777-5