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Chemical and Pharmaceutical Bulletin
Vol. 26 (1978) No. 3 P 716-721



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.

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