Purification and some properties of glycerol dehydrogenase from Erwinia aroideae.

Abstract

Glycerol dehydrogenase was purified from Erwinia aroideae IFO 3830 by precipitation of acetone and ammonium sulfate, and chromatographies on diethylaminoethyl (DEAE)-cellulose, Sephadex G-200 and DEAE-Sephadex A-50. The purified enzyme was demonstrated to be homogeneous by disc electrophoresis. Optimum pH and temperature of this enzyme for glycerol oxidation was 10.5 and 50°, respectively. The glycerol dehydrogenase was stable over a pH between 6 and 9 at 5°for 15 hr, and showed more than 90% activity of the original under the conditions of pH 7.0 and 70°for 20 min. It was clarified that glycerol, glycerol-α-monochlorohydrin, 1, 2-propanediol and 2, 3-butanediol were good substrates for glycerol dehydrogenase from Erwinia aroideae. From the result of effect of sulfhydryl agents, it is suggested that this enzyme has a catalytic sulfhydryl group.