Purification and Characterization of a Ribitol Dehydrogenase from Enterobacter agglomerans Strain 221e
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概要
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Ribitol dehydrogenase (EC 1.1.1.56) of Enterobacter agglomerans strain 221e was purified to homogeneity by polyetheylene glycol precipitation, anion exchange chromatography on diethylaminoethyl (DEAE)-Toyopearl 650 M, hydrophobic chromatography on Phenyl-Toyopearl 650 M and gel filtration on Sephadex G-150. The enzyme was specific for NAD^+ but showed a broad substrate specificity for various polyols. Among those tested ribitol exhibited the highest affinity for the enxyme followed by allitol, L-arabitol, L-mannitol, xylitol, L-sorbitol, L-talitol, L-iditol, D-sorbitol, galactitol and erythritol. The enzyme showed maximum activity at pH 9-10 and was stable in the pH range of 9-11. The native enzyme exhibited an isoelectric point of about 4.9 and was estimated to have an apparent M_r of 92,000 as determined by sephadex G-150 gel filtration. SDS-PAGE data suggested that ribitol dehydrogenase of strain 221e has a subunit M_r of 25,000.
- 1995-05-25
著者
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Izumori Ken
Department Of Biochemistry And Food Science Faculty Of Agriculture And Rare Sugar Research Center Ka
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Muniruzzaman Syed
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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KUNIHISA YASUTAKA
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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ICHIRAKU KENJI
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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Kunihisa Yasutaka
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Ichiraku Kenji
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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