Abstract
Ribitol dehydrogenase (EC 1.1.1.56) of Enterobacter agglomerans strain 221e was purified to homogeneity by polyethylene 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 enzyme 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.
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