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Current Microbiology

, Volume 46, Issue 3, pp 0169–0173 | Cite as

Purification and Characterization of an Extracellular Alkaline Serine Protease with Dehairing Function from Bacillus pumilus

  • Qing Huang
  • Yong Peng
  • Xin Li
  • Haifeng Wang
  • Yizheng Zhang

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.

Keywords

Enzyme Fluoride Bacillus Amino Acid Residue Hydrophobic Interaction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag New York Inc. 2003

Authors and Affiliations

  • Qing Huang
    • 1
  • Yong Peng
    • 1
  • Xin Li
    • 1
  • Haifeng Wang
    • 1
  • Yizheng Zhang
    • 1
  1. 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 ChinaCN

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