Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium

Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium
Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium

ㆍ 저자명: Asghari. S. Mohsen,Khajeh. Khosro,Dalfard. Arastoo Badoei,Pazhang. Mohammad,Karbalaei-Heidari. Hamid Reza
ㆍ 간행물명: BMB reports
ㆍ 권/호정보: 2011년|44권 10호|pp.665-668 (4 pages)
ㆍ 발행정보: 생화학분자생물학회
ㆍ 파일정보: 정기간행물|ENG|
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ㆍ 주제분야: 기타

이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.

서지반출

기타언어초록

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.

키워드

Autolysis Neutral proteases Organic solvent stability pH stability Thermostability

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