Chemical and Pharmaceutical Bulletin
Online ISSN : 1347-5223
Print ISSN : 0009-2363
Purification and Some Properties of Glycerol Dehydrogenase from Erwinia aroideae
MAMORU SUGIURATSUTOMU OIKAWAKAZUYUKI HIRANOHIROSHI SHIMIZUFUMIO HIRATA
Author information
Keywords: NAD
JOURNALS FREE ACCESS

1978 Volume 26 Issue 3 Pages 716-721

Details
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.

Information related to the author
© The Pharmaceutical Society of Japan
Previous article Next article
feedback
Top