Molecular Biology Reports

, 36:2169

Purification and characterization of the cold-active alkaline protease from marine cold-adaptive Penicillium chrysogenum FS010

Authors

  • Hui-Yuan Zhu
    • State Key Laboratory of Microbial TechnologyShandong University
    • College of Food and Biological EngineeringShandong Institute of Light Industry
  • Yong Tian
    • College of Food and Biological EngineeringShandong Institute of Light Industry
  • Yun-Hua Hou
    • College of Food and Biological EngineeringShandong Institute of Light Industry
    • State Key Laboratory of Microbial TechnologyShandong University
Article

DOI: 10.1007/s11033-008-9431-0

Cite this article as:
Zhu, H., Tian, Y., Hou, Y. et al. Mol Biol Rep (2009) 36: 2169. doi:10.1007/s11033-008-9431-0

Abstract

An extracellular cold-active alkaline serine protease from Penicillium chrysogenum FS010 has been purified. The purification procedure involved: ammonium sulfate precipitation, DEAE ion-exchange chromatography and sephadex G-100 gel chromatography. SDS–PAGE of the purified enzyme indicated a molecular weight of 41,000 ± 1,000 Da. The protease is stable in a pH range of 7.0–9.0 and has a maximum activity at pH 9.0. Compared with other industrial proteases, the enzyme shows a high hydrolytic activities at lower temperatures and a high sensitivity at a temperature over 50°C. The isoelectric point of the enzyme is approximate to 6.0. Enzymatic activity is enhanced by the addition of divalent cations such as Mg2+ and Ca2+ and inhibited by addition of Cu2+and Co2+. PMSF and DFP are its specific inhibitors. The application of the cold-active alkaline protease is extremely extensive, and widely used in detergents, feed, food, leather and many other industries.

Keywords

Penicillium chrysogenumCold-active alkaline proteasePurificationEnzymatic characterization

Copyright information

© Springer Science+Business Media B.V. 2009