Molecular cloning of novel cellulase genes cel9A and cel12A from Bacillus licheniformis GXN151 and Synergism of their encoded polypeptides

文献类型： 外文期刊

第一作者： Liu, YS

作者： Liu, YS;Zhang, J;Liu, Q;Zhang, CG;Ma, QS

作者机构：

关键词： Sequence;Endoglucanase;Binding;Domain

期刊名称：CURRENT MICROBIOLOGY （ 影响因子：2.188； 五年影响因子：2.197 ）

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年卷期：

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收录情况： SCI

摘要： A thermophilic bacterial strain GXN151 which could degrade Avicel efficiently was isolated and identified as Bacillus licheniformis. A genomic library of GXN151 was constructed and two novel endoglucanase genes designated cel9A and cel12A were isolated by screening the library on carboxylmethyl cellulase indicator plates. The analysis of amino acid sequences deduced from the genes indicated that Cel9A consisted of a catalytic domain belonging to glycosyl hydrolase family 9, a linker domain, and a carbohydrate binding module family 3 from N-terminal to C-terminal; Cel12A had only one catalytic domain belonging to glycosyl hydrolase family 12. The combinations of Cel9A and Cel12A produced by the recombinant E. coli exhibited synergistic action against substrates of carboxylmethyl cellulose as well as Avicel. [References: 19]

分类号： Q93

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