ISOLATION AND CHARACTERIZATION OF NAD(P)-DEPENDENT L-SORBOSONE DEHYDROGENASE FROM GLUCONOBACTER-MELANOGENUS UV10

NAD(P)-Dependent L-sorbosone dehydrogenase has been purified from the cytosol fraction of Gluconobacter melanogenus UV10. The enzyme was purified about 30-fold with an overall yield of 19% by column chromatographies on DEAE-Sepharose CL-6B, DEAE-Sephadex A-50, and Blue Sepharose CL-6B. The enzyme required NAD or NADP as a cofactor, and showed broad substrate specificity on various aldehyde compounds. Among them, L-sorbosone was the best substrate for the enzyme. In this respect, the enzyme is a kind of aldehyde dehydrogenase.