Microbiology and Biotechnology Letters (한국미생물·생명공학회지)

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Enterobacter cloacae MG82에 의한Triphenylmethane흡수 특성과 탈색효소의 세포내 위치

  • 정민선 (영남대학교 식품가공학과) ;
  • 곽순전 (숙명여자대학교 생물학과) ;
  • 김병홍 (한국과학기술원 환경연구센터) ;
  • 정영건 (영남대학교 식품가공학과) ;
  • 강사욱 (서울대학교 미생물학과) ;
  • 민경희 (숙명여자대학교 생물학과)
  • Published : 1997.02.01
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Abstract

Triphenylmethane was decolorized rapidly by enterbacter cloacae MG 82 at initial reaction time. The spheroplast showed higher activity of triphenylmentane decolorization than that of intact cell suspension. The outer part of the bacterial cell envelope and the peptidoglycan are important for the function of transport barrier of triphenylmethane. In intact cell, decolorization activity was higher at 37$\circ $C than at $\circ $C, indicating that triphenylmethane decolorization is due to the enzyme reaction. Culture filtrate showed no decolorization activity, while cell-free extract appeared high activity of 1.45 units, clearly showing that decolorization activity was due to the cell-free extract. Comparing decolorization activities of cell fractions, it was found that decolorization activity was located at the compartment of cytoplasmic membrane. The enzyme activity was also shown to be Mg$^{++}$-dependent. The optimum pH and temperature of enzyme activity were 7.0 and 50$\circ $C, respectively. The thermostability of this enzyme at 35$\circ $C was kept to 58% for 3 hours.

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