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 erzyme activity was inhibited by p-chloromercuribenzoate, Zn²⁺, Cu²⁺ and Cd²⁺ . Oxidation of glycerol was activated by Na⁺ and reduction of dihydroxyacetone was activated by K⁺ at pH 7.5.