Screening, Gene Cloning, and Characterizations of an Acid-Stable alpha-Amylase
文献类型: 外文期刊
第一作者: Liu, Xinyu
作者: Liu, Xinyu;An, Yi;Cheng, Kun;Wang, Mingdao;Yang, Sen;Chen, Hongge;Jia, Wei
作者机构:
关键词: alpha-Amylase;Bacillus amyloliquefaciens;raw starch;starch-binding domain
期刊名称:JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY ( 影响因子:2.351; 五年影响因子:2.65 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: Based on its alpha-amylase activity at pH 5.0 and optimal pH of the crude enzyme, a strain (named B-5) with acid alpha-amylase production was screened. The B-5 strain was identified as Bacillus amyloliquefaciens through morphological, physiological, and biochemical characteristics analysis, as well as 16S rDNA phylogenetic analysis. Its alpha-amylase gene of GenBank Accession No. GU318401 was cloned and expressed in Escherichia coli. The purified recombinant alpha-amylase AMY-Ba showed the optimal pH of 5.0, and was stable at a pH range of 4.0-6.0. When hydrolyzing soluble starch, amylose, and amylopectin, AMY-Ba released glucose and maltose as major end products. The vamylase AMY-Ba in this work was different from the well-investigated J01542-type alpha-amylase which also came from B. amyloliquefaciens. AMY-Ba exhibited notable adsorption and hydrolysis ability towards various raw starches. Structure analysis of AMY-Ba suggested the presence of a new starch-binding domain at its C-terminal region.
分类号: Q93
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