| Literature DB >> 20417096 |
Aihua Deng1, Jie Wu, Yun Zhang, Guoqiang Zhang, Tingyi Wen.
Abstract
The newly isolated alkalophilic Bacillus sp. B001 produced a high level of proteolytic activity (34277 U/mL) 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 Bacillusclausii, Bacillusalcalophilus, and Bacillus lentus. High stability of AprB towards surfactants and oxidizing agents, an optimal pH of 10.0, and an optimal temperature of 60 degrees C suggest that this high-alkaline protease has potential applications for various industrial processes. Copyright 2010 Elsevier Ltd. All rights reserved.Entities:
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Year: 2010 PMID： 20417096 DOI： 10.1016/j.biortech.2010.03.130
Source DB: PubMed Journal: Bioresour Technol ISSN： 0960-8524 Impact factor: 9.642