文献类型： 外文期刊
作者： Liu, Xinyu 1 ; Jia, Wei 2 ; An, Yi 1 ; Cheng, Kun 1 ; Wang, Mingdao 1 ; Yang, Sen 1 ; Chen, Hongge 1 ;
作者机构： 1.Henan Agr Univ, Minist Agr, Coll Life Sci, Key Lab Enzyme Engn Agr Microbiol, Zhengzhou 450002, Peoples R China
2.Shanghai Acad Agr Sci, Inst Edible Fungi, Shanghai 201403, Peoples R China
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：
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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.
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