Methanol Oxidase of Phanerochaete chrysosporium

Abstract

Methanol oxidase catalyzes the oxidation of methanol and other low-molecular-weight primary alcohols to the corresponding aldehydes and H 2 O 2 . This chapter discusses the isolation and characterization of this enzyme from the mycelium of Phanerochaete chrysosporium , a basidiomycete. In addtion to the organism, several other basidiomycetes, including Polyporus obtusus, Polyporus versicolor, and Lenzites trabea, have also been demonstrated to produce this enzyme. However, the enzyme methanol oxidase is produced not only in basidiomycetes, but also in yeasts, such as Kloeckera sp. No. 2201 and Hansenula polymorpha. The chapter also discusses the properties of the enzyme. Methanol oxidase of Phanerochaete chrysosporium catalyzes the oxidation of several other simple primary alcohols but at varying rates: ethanol (91.9), n-propanol (34.4), and n-butanol (10.6). The figures in parentheses give relative activity toward primary alcohols. Toward higher alcohols, the activity is negligible.