Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates,D-fructose to 5-keto-D-fructose,and D-psicose to 5-keto-D-psicose |
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| Authors: | Yoshitaka Ano Roque A Hours Yoshihiko Akakabe Naoya Kataoka Toshiharu Yakushi Kazunobu Matsushita |
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| Institution: | 1. Department of Bioscience, Graduate School of Agriculture, Ehime University, Matsuyama, Japan;2. CINDEFI, School of Science, La Plata National University, La Plata, Argentina;3. Faculty of Agriculture, Department of Biological Chemistry, Yamaguchi University, Yamaguchi, Japan |
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| Abstract: | A novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with Gluconobacter thailandicus NBRC 3258. D-Pentonate 4-dehydrogenase activity in the membrane fraction was readily inactivated by EDTA and it was reactivated by the addition of PQQ and Ca2+. D-Pentonate 4-dehydrogenase was purified to two different subunits, 80 and 14 kDa. The absorption spectrum of the purified enzyme showed no typical absorbance over the visible regions. The enzyme oxidized D-pentonates to 4-keto-D-pentonates at the optimum pH of 4.0. In addition, the enzyme oxidized D-fructose to 5-keto-D-fructose, D-psicose to 5-keto-D-psicose, including the other polyols such as, glycerol, D-ribitol, D-arabitol, and D-sorbitol. Thus, D-pentonate 4-dehydrogenase was found to be identical with glycerol dehydrogenase (GLDH), a major polyol dehydrogenase in Gluconobacter species. The reaction versatility of quinoprotein GLDH was notified in this study. |
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| Keywords: | acetic acid bacteria glycerol dehydrogenase 4-keto-D-arabonate production 4-keto-D-pentonate oxidative fermentation |
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