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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium

  • Asghari, S. Mohsen (Department of Biology, Faculty of Science, University of Guilan) ;
  • Khajeh, Khosro (Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University) ;
  • Dalfard, Arastoo Badoei (Department of Biology, Faculty of Science, Shahid Bahonar University of Kerman) ;
  • Pazhang, Mohammad (Department of Cellular and Molecular Biology, Faculty of Science, Azarbaijan University of Tarbiat Moallem) ;
  • Karbalaei-Heidari, Hamid Reza (Department of Biology, College of Sciences, Shiraz University)
  • Received : 2011.05.13
  • Accepted : 2011.07.29
  • Published : 2011.10.31
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Abstract

In order to clarify the impact of Ca-binding sites (Ca1 and 2) on the conformational stability of neutral proteases (NPs), we have analyzed the thermal, pH and organic solvent stability of a NP variant, V189P/A195E/G203D/A268E (Q-mutant), from Salinovibrio proteolyticus. This mutant has shown to bind calcium more tightly than the wild-type (WT) at Ca1 and to possess Ca2. Q-mutant was resisted against autolysis, thermoinactivation and pH denaturation in a Ca-dependent manner and exhibited better activity in organic solvents compared to the WT enzyme. These results imply that Ca1 and Ca2 are important for the conformational stability of NPs.

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References

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