Enzymatic Studies on the Oxidation of Sugar and Sugar Alcohol I. Purification and Properties of Particle-bound Fructose Dehydrogenase*

Publisher Website
Google Scholar
Abstract
An enzyme, fructose dehydrogenase which catalyzes the oxidation of D-fructose to 5-keto-D-fructose was obtained from fructose-grown cells of Gluconobacter cerinus. The enzyme present in particulate fraction was solubilized by deoxycholate-butanol extraction, and purified about 40–50 fold by acetone precipitation and DEAE-cellulose column chromatography. 2, G-Dichlorophenol indophenol was the most effective electron acceptor but neither NAD nor NADP was required. The optimal pH was 5.0 and Michaelis constant for D-fructose was 1.0 × 10−2M in the presence of 6.7 × 10−4M of 2, 6-dichlorophenol indophenol. P-Chloromercuribenzoate, phenylmercuric nitrate, as well as silver and mercuric ions inhibited most of the activity. L-Sorbose, sucrose and polyols were inactive as a substrate. The partially purified enzyme preparation still has an activity toward D-glucose, D-gluconate, and several aldoses. It was proved, however, that this fructose dehydrogenase was different from either glucose or gluconate dehydrogenase. It was, therefore, proposed that the enzyme is a new type of the so-called Bertrand-Hudson enzyme.

This publication has 1 reference indexed in Scilit: