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Title of Journal: Biotechnol Lett

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Abbravation: Biotechnology Letters

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Springer Netherlands

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DOI

10.1002/pro.5560051109

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ISSN

1573-6776

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Direct detection cloning and characterization of

Authors: Mei Hua Shubo Zhao Lili Zhang Dongbo Liu Hongmei Xia Fan Li Shan Chen
Publish Date: 2015/02/21
Volume: 37, Issue: 6, Pages: 1227-1232
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Abstract

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

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