Pseudomonas sp. DJ-12에서 분리한 2,3-Dihydroxybiphenyl Dioxygenase의 효소학적 특성

Enzymatic Properties of the 2,3-Dihydroxybiphenyl Dioxygenase Purified from Pseudomonas sp. DJ-12

  • 성태경 (충북대학교 자연과학대학 미생물학과) ;
  • 남정현 (충북대학교 자연과학대학 미생물학과) ;
  • 김치경 (서울대학교 분자미생물학 연구센터)
  • 발행 : 1993.04.01

초록

The 2,3-dihydroxybiphenyl(2,3-DHBP) dioxygenase, the product of pcbC gene, was purified from the biphenyl and 4-chlorobiphenyl degrading Pseudomonas sp. DJ-12 by the methods of acetone precipitation, DEAE-Sephadex A-50 ion exchange chromatography, and Sephadex G-150 gel filtration chromatography. The enzyme was estimated to be about 260 kilodaltons in molecular weight and to be consisted of eight subunits. The Km value of the enzyme was 61 nM to 2,3-DHBP and the highest activity of the enzyme was observed at pH 8 and 30C.

키워드

참고문헌

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