Purification and characterization of a surfactant-stable high-alkaline protease from Bacillus sp B001

被引:180
作者
Deng, Aihua [1 ,2 ]
Wu, Jie [1 ,2 ]
Zhang, Yun [1 ]
Zhang, Guoqiang [1 ,2 ]
Wen, Tingyi [1 ]
机构
[1] Chinese Acad Sci, Inst Microbiol, Dept Ind Microbiol & Biotechnol, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
关键词
High-alkaline protease; Bacillus sp; Surfactant-stable; Purification; Degenerate primer; SERINE-PROTEASE; BIOCHEMICAL-CHARACTERIZATION; MOLECULAR-CLONING; STRUCTURAL GENE;
D O I
10.1016/j.biortech.2010.03.130
中图分类号
S2 [农业工程];
学科分类号
082806 [农业信息与电气工程];
摘要
The newly isolated alkalophilic Bacillus sp. B001 produced a high level of proteolytic activity (34277 MM..) when grown in production medium, and a 28 kDa protease, designated AprB, was purified from the culture supernatant Partial amino acid sequences were obtained by tandem mass spectrometry (MS/MS) and a pair of degenerate primers was developed to amplify a 467-bp genomic sequence The observed and predicted amino acid sequences showed similarity with sequences of high-alkaline proteases from Bacillus clausn, Bacillus alcalophilus, and Bacillus lentus High stability of AprB towards surfactants and oxidizing agents, an optimal pH of 100, and an optimal temperature of 60 degrees C suggest that this high-alkaline protease has potential applications for various industrial processes (C) 2010 Elsevier Ltd. All rights reserved
引用
收藏
页码:7100 / 7106
页数:7
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