Abstract
A new enzymatic method for glycolaldehyde production from ethylene glycol was investigated using alcohol oxidase from Pichia pastoris or glycerol oxidase from Aspergillus japonicus. Both alcohol and glycerol oxidases oxidize ethylene glycol to glyoxal via glycolaldehyde, but glycolaldehyde was remarkably accumulated using a high concentration of ethylene glycol. The glycolaldehyde formation was also affected by buffer species and reaction pH. Under the optimum conditions, 0.92 or 0.97 M glycolaldehyde was formed from 1.0 M ethylene glycol using alcohol oxidase or glycerol oxidase. This enzymatic method was superior to the chemical method in terms of conversion yields and selectivity of glycolaldehyde.
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