해수에서 분리한 Vibrio sp. M-96 균주의 열감수성 alkaline phosphatase 성질 = Properties of a Thermolabile Alkaline Phosphatase from the Marine Bacterium Vibrio sp. M-96

다국어 초록 (Multilingual Abstract)

A thermolabile alkaline phosphatase has been purified through steps of osmotic shock, ammonium sulfate salting-out, and DEAE-cellulose chromatography from the cultured broth of the marine Vibrio sp. M-96 strain. The optimal temperature for the enzyme activity was 35℃. The optimal pH was pH 11.0, and the range of pH stability was pH 10.4 to 12.0. Thermal inactivation occured within 6 minutes at 60℃. The enzyme was considerably inactivated by 0.1mM concentrations of Hg^2+, Ni^2+ and Zn^2+, whereas activated up to 234% by 1mM of Mn^2+. The activation energy and deactivation energy by the Arrhenius equation were 4.02 Kcal/mol and 9.09 Kcal/mol, respectively. The Km and Vmax values of the enzyme for p-nitrophenylphosphate were found to be 0.0465mM and 0.001335mM/min. respectively. Active from of the enzyme had a molecular weight of 57,000 dalton determined by the Sephadex G-200 gel filtration method.