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KMID : 0624620110440100665
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BMB Reports
2011 Volume.44 No. 10 p.665 ~ p.668
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Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium
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Asghari S. Mohsen
Khajeh Khosro
Dalfard Arastoo Badoei
Pazhang Mohammad
Karbalaei-Heidari Hamid Reza
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Abstract
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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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KEYWORD
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Autolysis, Neutral proteases, Organic solvent stability, pH stability, Thermostability
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