Glycerol Dehydrogenase from Cellulomonas sp. NT3060: Purification and Characterization

Abstract

NAD+-dependent glycerol dehydrogenase from Cellulomonas sp. NT3060 was purified by a procedure of 10 steps involving crystallization. Dihydroxyacetone was identified as the oxidation product of glycerol with the enzyme. The purified enzyme did not lose activity on heating below 60°C. The enzyme oxidized other alcohols such as 1,2-propanediol, 2,3-butanediol and glycerol-α-monochlorohydrin, beside glycerol. The enzyme activity was inhibited by p-chloromercuribenzoate, Zn2+, Cu2+ and Cd2+. Oxidation of glyberol was activated by Na+ and reduction of dihydroxyacetone was activated by K+ at pH 7.5. © 1982, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.