Solubilization, Purification and Properties of Membrane-bound Glycerol Dehydrogenase from Gluconobacter industrius
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概要
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Membrane-bound glycerol dehydrogenase was solubilized and purified about 100-fold from the membrane of Gluconobacter industrius IFO 3260 grown on a glycerol-glutamate medium. Solubilization of the enzyme was successfully achieved by use of 0.5% dimethyldodecylamineoxide in 0.05M Tris-HCl, pH 8.0. Alcohol dehydrogenase and D-glucose dehydrogenase, which were abundantly formed in the same bacterial membrane, were eliminated on Solubilization. Glycerol dehydrogenase was further purified through fractionation with polyethylene glycol 6000. The enzyme showed a broad substrate specificity and various kinds of polyhydroxyl alcohols, in addition to glycerol, were rapidly oxidized in the presence of 2, 6-dichlorophenolindophenol and phenazine methosulfate as the electron acceptor but NAD and NADP were inert. The enzyme was proved to be a quinoprotein in which pyrroloquinoline quinone functioned as the prosthetic group.
- 社団法人 日本農芸化学会の論文
著者
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Adachi Osao
Laboratory Of Applied Microbiology Department Of Biological Chemistry Faculty Of Agriculture Yamaguc
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SHINAGAWA Emiko
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Faculty of Agriculture, Ya
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Ameyama Minoru
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Faculty Of Agriculture Yamag
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Matsushita Kazunobu
Laboratory Of Applied Microbiology Department Of Biological Chemistry Faculty Of Agriculture Yamaguc
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