Purification and some properties of glycerol dehydrogenase from Erwinia aroideae
| Autor: | Kazuyuki Hirano, Hiroshi Shimizu, Fumio Hirata, Tsutomu Oikawa, Mamoru Sugiura |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Glycerol
chemistry.chemical_classification Ammonium sulfate Chromatography biology General Chemistry General Medicine Erwinia biology.organism_classification Alcohol Oxidoreductases chemistry.chemical_compound Enzyme chemistry Biochemistry Sephadex Drug Discovery Acetone Glycerol dehydrogenase Aroideae |
| Zdroj: | Chemical and Pharmaceutical Bulletin. 26:716-721 |
| ISSN: | 1347-5223 0009-2363 |
| DOI: | 10.1248/cpb.26.716 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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