Purification and Characterization of an Extracellular Alkaline Serine Protease with Dehairing Function from <Emphasis Type="Italic">Bacillus pumilus</Emphasis> |
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Authors: | Qing Huang Yong Peng Xin Li Haifeng Wang Yizheng Zhang |
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Institution: | (1) College of Life Science, Center for Green Chemistry and Technology, Sichuan University, Sichuan Key Laboratory of Molecular Biology and Biotechnology, Chengdu 610064, People's Republic of China, CN |
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Abstract: | An extracellular alkaline serine protease (called DHAP), produced by a Bacillus pumilus strain, demonstrates significant dehairing function. This protease is purified by hydrophobic interaction chromatography,
ion exchange, and gel filtration. DHAP had a pI of 9.0 and a molecular weight of approximately 32,000 Dalton. It shows maximal
activity at pH 10 and with a temperature of 55°C; the enzyme activity can be completely inhibited by phenylmethylsulfonyl
fluoride (PMSF) and diisopropyl fluorophosphates (DFP). The first 20 amino acid residues of the purified DHAP have been determined
with a sequence of AQTVPYGIPQIKAPAVHAQG. Alignment of this sequence with other alkaline protease demonstrates its high homology
with protease from another B. pumilus strain.
Received: 17 April 2002 / Accepted: 24 May 2002 |
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