Purification and Some Properties of New Coccine (NC)-Reductase fromBacillus cereusT-105 Strain

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Abstract
Intracellular distribution of NADPH-dependent New Coccine (NC)-reductase from Bacillus cereus T-105 strain was examined. It was found that most parts of the enzyme existed in a cytoplasmic fraction. The enzyme was purified to homogeneity from the cell- free extract about 200-fold by a procedure involving ammonium sulfate fractionation, heat treatment, ion-exchange chromatographies on DEAE-cellulose and DEAE-Sephadex A-50, and Sephadex G-200 gel filtration, and its properties were examined. The visible absorption spectrum of the purified enzyme showed maxima at 375 and 448 nm. The prosthetic group seemed to be a flavin, but has not been identified yet. The optima of pH and temperature for the enzyme activity were pH 7.0 and 40°C, respectively. The enzyme was stable up to 60°C, and 55% of the initial activity remained after heat treatment for 10 min at 80°C. The enzyme was stable in a pH range between 6.0 and 8.0 for 7 days at 5°C. The enzyme activity was strongly inhibited by Ag+, Hg2+ , Cu2+, Fe2+ , Fe3+, and SDS, but was activated slightly by Mg2+. Sulfhydryl reagents such as NEM, PCMB, or IAA, did not inhibit the enzyme activity.

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