Purification and characterization of a surfactant-stable high-alkaline protease from Bacillus sp. B001.
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.
Deng
Aihua
A
Department of Industrial Microbiology and Biotechnology, Institute of Microbiology, Chinese Academy of Sciences, 100101 Beijing, China.
Wu
Jie
J
Zhang
Yun
Y
Zhang
Guoqiang
G
Wen
Tingyi
T
D001407:Bacillus / Q000145:classification* / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D010450:Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D004795:Enzyme Stability; D013045:Species Specificity; D013501:Surface-Active Agents / Q000737:chemistry*
D001426:Bacterial Proteins; D013501:Surface-Active Agents; D010450:Endopeptidases; C087822:alkaline protease