Purification and Characterization of an Extracellular Protease from Bacillus pumilus CN8

  • Jin, Yong-Guo (College of Food Science and Technology, Huazhong Agricultural University) ;
  • Li, Hao-Li (College of Food Science and Technology, Huazhong Agricultural University) ;
  • Mal, Mei-Hu (College of Food Science and Technology, Huazhong Agricultural University) ;
  • Wang, Jun (Department of Food Science and Biotechnology and Institute of Bioscience and Biotechnology, Kangwon National University) ;
  • Kim, Ha-Na (Department of Food Science and Biotechnology and Institute of Bioscience and Biotechnology, Kangwon National University) ;
  • Oh, Deog-Hwan (Department of Food Science and Biotechnology and Institute of Bioscience and Biotechnology, Kangwon National University)
  • Received : 2011.02.21
  • Accepted : 2011.03.17
  • Published : 2011.03.31

Abstract

The protease produced by a Bacillus pumilus CN8 strain was purified by DEAE-Cellulose-52 ion exchange. It has a molecular weight of approximately 96,920 Dalton. In the present study, this protease showed strong activity over a broad range of pH (6.5-9.5) and temperature from $40^{\circ}C$ to $60^{\circ}C$, and the protease performed the maximal activity at pH 7.3 at $42^{\circ}C$. The effect of metal ions on protease activity showed that $K^+$ could slightly increase the protease activity, and other ions such as $Zn^{2+}$, $Fe^{2+}$, $Na^+$, $Ca^{2+}$, $Mg^{2+}$ had no significant activation or inhibition to the protease (P> 0.05), and the more important is that $Cu^{2+}$, $Mn^{2+}$, $Sn^{2+}$, $Cd^{2+}$ had a strong inhibitory effect on the protease activity.

Keywords

References

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