Purification and Characterization of Cholesterol Oxidase from Bacillus sphaericus

Bacillus sphaericus로부터 Cholesterol Oxidase의 정제 및 특성

  • 서형주 (고려대학교 병설 보건전문대학 식품영양과) ;
  • 김태웅 (강원대학교 생화학과) ;
  • 손흥수 (한림대학교 한국영양연구소)
  • Published : 1993.10.01

Abstract

The cholesterol oxidase produced from Bacillus sphaericus was purified and characterized. Through a series of purification procedures including DEAE-Toyoperal 650C, Sephadex G-200 and DEAE-Sephadex A-50 column chromatography, the purified enzyme was shown to have a specific activity of 0.179 units/mg protein having 31.8 fold purification and final yield of 12%. The molecular weight of the enzyme was estimated to be 47kDa and 47.tkDa by Sephadex G-200 chromatography and SDS-PAGE. The optimum temperature and pH for the enzyme were 30C and 6.0, respectively. The activity of the purified cholesterol oxidase was inhibited by Fe2+ and Hg+.

Keywords

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