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