Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Properties of a Thermolabile Alkaline Phosphatase from the Marine Bacterium Vibrio sp. M-96

해수에서 분리한 Vibrio sp. M-96 균주의 열감수성 alkaline phosphatase 성질

  • 박문경 (부경대학교 생물공학과) ;
  • 진덕희 (부경대학교 생물공학과) ;
  • 김중균 (부경대학교 생물공학과) ;
  • 공인수 (부경대학교 생물공학과) ;
  • 김광현 (동의대학교 미생물학과) ;
  • 홍용기 (부경대학교 생물공학과)
  • Published : 1996.09.01
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Abstract

A thermolabile alkaline phosphatase has been purified through steps of osmotic shock, ammonium sulfate salting-out, and DAEA-cellulose chromatography from the cultured broth of the marine Vibrio sp. M-96 strain. The optimal temperature for the enzyme activity was 35$\circ$C. The optimal pH was pH11.0, and the range of pHstability was pH10.4 to 12.0. Thermal inactivation occured within 6 mintes at 60$\circ$C. 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 9.098 Kcal/mol, respectively. The Km and Vmax values of the enzyme for p-introphenylphosphate were found to be 0.0465mM and 0.001334mM/min, respectively. Active form of the enzyme had a molecular weight of 57,000 dalton determined by the Sephadex G-200 gel filtration method.

Keywords

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