Abstract
A specific nicotinamide adenine dinucleotide(NAD)-linked d-xylose dehydrogenase was first demonstrated in the d-xylose-grown cells of Arthrobacter sp. This enzyme was specifically induced by d-xylose. No other effective sugar was found for the production of this enzyme by growing culture. This enzyme catalyzes the following reaction: d-Xylose + NAD+−d−-xylonolactone + NADH + H+ This enzyme was purified 186-fold in specific activity from the extracts of d-xylose-grown cells by the procedures including chromatographies on DEAE-cellulose, DEAE-Sephadex and Sephadex G-100. The enzyme is specific on the dehydrogenation of d-xylose with NAD. Seven pentoses, 5 hexoses, and 7 polyols were not substrates with NAD or NADP. NAD was active coenzyme of this enzyme. The Km values were 17.4 mm for d-xylose and 0.27 mm for NAD. The pH optimum was at pH 10.4, but the enzyme activity was most stable at neutral pH, 7.0 to 7.5. The molecular weight of the enzyme was calculated as 62,000±2000 and isoelectric point was pH 5.58. These evidences clearly indicated the presence of a novel dehydrogenase specific on d-xylose, d-xylose dehydrogenase in Arthrobacter sp.
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