Alcohol oxidase from the yeast Pichia pastoris – a potential catalyst for organic synthesis

Abstract

Alcohol oxidase (AO) from the methylotropic yeast Pichia pastoris was isolated and investigated. Wide substrate specificity is characteristic for this enzyme. Unbranched primary alcohols are effectively oxidized by AO to aldehydes, including propargyl alcohol, 2-chloroethanol, 2-cyanoethanol, leading to important synthetic intermediates. AO was immobilized by covalent linking to macroporous cellulose activated by glutaraldehyde, yield of immobilization 80%. Presence of two izoenzymes of AO was suggested from the pH activity dependence.