Enhancing the soluble expression of an amylase in Escherichia coli by the mutations related to its domain interactions

文献类型： 外文期刊

第一作者： Wang, Peili

作者： Wang, Peili;Qin, Weitong;Xu, Jiangtao;Yan, Yaru;Tian, Jian;Wu, Ningfeng;Wang, Peili;Yao, Bin

作者机构：

关键词： alpha-Amylase (BLA);Domain interaction;Escherichia coli;Soluble expression;Mutation

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： The sequence and structure of the target protein exert a marked effect on its soluble expression in Escherichia coli. The effects of the mutation of an amylase isolated from Bacillus licheniformis (BLA) on its soluble expression in E. coli were investigated. A random mutation library of BLA was constructed to screen for mutations that resulted in enhanced soluble expression in E. coll. Two interesting mutations (A390I and D401V) were identified, which are located at the interaction surface between the A and C domains of BLA. The A390I mutation enhanced soluble BLA expression by 2.0-fold compared to wild type, while D401V decreased soluble expression 160-fold. Structural analysis revealed that A390 and D401 residues could affect the interaction between the A and C domains of BLA. Therefore, soluble expression of the target protein in E. coli could be affected by introduction of a mutation in the protein sequence. (C) 2015 Elsevier Inc. All rights reserved.

分类号： Q51

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