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.