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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.
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Yamada et al. (1982) studied this question.
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