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http://dx.doi.org/10.5483/BMBRep.2011.44.10.665

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)

Publication Information

BMB Reports / v.44, no.10, 2011 , pp. 665-668 More about this Journal

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.

Keywords

Autolysis; Neutral proteases; Organic solvent stability; pH stability; Thermostability;

Citations & Related Records

Times Cited By Web Of Science : 1 (Related Records In Web of Science)
Times Cited By SCOPUS : 1

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