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KMID : 0545120140240121699
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Journal of Microbiology and Biotechnology
2014 Volume.24 No. 12 p.1699 ~ p.1706
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Characterization of a Lichenase Isolated from Soil Metagenome
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Kim Sang-Yoon
Oh Doo-Byoung
Kwon Oh-Suk
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Abstract
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A lichenase gene (mt-lic) was identified for the first time through function-based screening of a soil metagenomic library. Its deduced amino acid sequence exhibited a high degree of homology with endo-β-1,3-1,4-glucanase (having both lichenase and chitosanase activities), encoded by the bgc gene of Bacillus circulans WL-12. The recombinant lichenase overexpressed and purified from Escherichia coli was able to efficiently hydrolyze both barley β-glucan and lichenan. The enzyme showed maximal activity at a pH of 6.0 at 50°C, with Azo-barley-glucan as the substrate. The metal ions Mn2+, Mg2+, Ca2+, and Fe2+ enhanced the enzymatic activity, whereas the Cu2+ and Zn2+ ions inhibited the enzymatic activity. The Km and Vmax values of the purified lichenase were determined to be 0.45 mg/ml and 24.83 U/min/mg of protein, respectively.
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KEYWORD
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Endo-β-1, 3-1, 4-glucanase, Glycosyl hydrolase family 8, Lichenase, Recombinant protein, Soil metagenome
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