Galactose Oxidase in Stereospecific Oxidation of Primary Alcohols

摘要

The stereospecificity of oxidation of several polyols and substituted polyols by the enzyme galactose oxidase was studied. An enzymatic method involving aldehyde dehydrogenase, D- and L-lactate dehydrogenase, and alcohol dehydrogenase, for the determination of optical purity of the oxidation product was used. Polyols and substituted polyols of three, four, five, and six carbons were tested as substrated using a horseradish peroxidase-chromagen coupled assay. A minimum structure required for polyol substrates of galactose oxidase was developed. Galactose oxidase was used in an attempt to synthesize D-threose, L-xylose, L-galactose, and L-glucose. Reasons for poor yields in three of four syntheses were discussed.