Enzymatic Production of Glyoxal from Ethylene Glycol Using Alcohol Oxidase from Methanol Yeast

概要

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A new oxidative reaction of ethylene glycol was found with two alcohol oxidases from methanol yeast, Candida sp. and Pichia pastoris. Both alcohol oxidases oxidized ethylene glycol to glyoxal via glycolaldehyde. The optimum pHs for the oxidation of ethylene glycol and glycolaldehyde by the Candida alcohol oxidase were around 8.5 and 5.5, respectively, and their apparent K_ms were 2.96 M and 28.6 mM, respectively. The optimum temperature was 40℃ at pH 7.0. The optimum pHs for the oxidation of ethylene glycol and glycolaldehyde by the Pichia alcohol oxidase were around 8.0 and 6.0, respectively, and their optimum temperatures were 50 and 45℃, respectively, at pH 7.0. The apparent K_m for glycolaldehyde was found to be 83.3mM. For the accumulation of glyoxal, addition of catalase was effective, and a higher amount of glyoxal was obtained at a much lower temperature than the optimum for the alcohol oxidase. When 0.1 M ethylene glycol and glycolaldehyde were incubated with 80 units of the Pichia enzyme at 10℃, both substrates were almost completely converted to glyoxal after 10 and 3h of incubation, respectively.
社団法人日本農芸化学会の論文
1994-01-23