KSBB Journal

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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Characteristics of Fumarate Reductase from Enterococcus faecalis RKY1

Enterococcus faecalis RKY1 이 생산하는 Fumarate Reductase의 특성

  • 박미란 (전남대학교 의공학 협동과정) ;
  • 김도만 (생물화학공학과, 촉매연구소) ;
  • 류화원 (생물화학공학과) ;
  • 이진하 (Hokkaido 대학교 농업대학원)
  • Published : 2000.06.01
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Abstract

An oxygen-sensitive fumarate reductase has been purified from the cytosol fraction of the Enterococcus faecalis RKY1 grown anaerobically on a defined medium containing glycerol and fumarate. A major portion of the purification was performed with employing Triton X-100 and reducing agents by Phenyl-sepharose CL-4B DEAE-sepharose and Dephadex G-150 The final activity was 0.42 unit/mg. The deduced molecular mass of active band was 66 kDa. The optimal pH and temperature for the activity were 7.0 and 38$^{\circ}C$ respectively. The enzyme activity was not affected by 1mM metal ions such as bacl2 $.$2H2O HgCl2 MnCl2$.$4H2O ZnCl2 CuCl2$.$2H2O Mgcl2$.$6H2O FeSo4$.$7H2O and by EDTA. Partially purified enzyme ws yellow in color ; spectroscopic study indicated the presence of flavins as a cofactor.

Keywords

References

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