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KMID : 0545120220320040484
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Journal of Microbiology and Biotechnology
2022 Volume.32 No. 4 p.484 ~ p.492
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Characterization of a Thermostable Lichenase from Bacillus subtilis B110 and Its Effects on β-Glucan Hydrolysis
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Huang Zhen
Ni Guorong
Wang Fei
Zhao Xiaoyan
Chen Yunda
Zhang Lixia
Qu Mingren
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Abstract
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Lichenase is an enzyme mainly implicated in the degradation of polysaccharides in the cell walls of grains. Emerging evidence shows that a highly efficient expression of a thermostable recombinant lichenase holds considerable promise for application in the beer-brewing and animal feed industries. Herein, we cloned a lichenase gene (CelA203) from Bacillus subtilis B110 and expressed it in E. coli. This gene contains an ORF of 729 bp, encoding a protein with 242 amino acids and a calculated molecular mass of 27.3 kDa. According to the zymogram results, purified CelA203 existed in two forms, a monomer, and a tetramer, but only the tetramer had potent enzymatic activity. CelA203 remained stable over a broad pH and temperature range and retained 40% activity at 70°C for 1 h. The Km and Vmax of CelA203 towards barley β-glucan and lichenan were 3.98 mg/ml, 1017.17 U/mg, and 2.78 mg/ml, 198.24 U/mg, respectively. Furthermore, trisaccharide and tetrasaccharide were the main products obtained from CelA203-mediated hydrolysis of deactivated oat bran. These findings demonstrate a promising role for CelA203 in the production of oligosaccharides in animal feed and brewing industries.
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KEYWORD
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Bacillus subtilis, lichenase, expression, characterization, oligosaccharide, β-glucan
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