An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.

Abstract:

:An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide.

journal_name

Enzyme Microb Technol

authors

Linke D,Lehnert N,Nimtz M,Berger RG

doi

10.1016/j.enzmictec.2014.04.001

subject

Has Abstract

pub_date

2014-07-01 00:00:00

pages

7-12

eissn

0141-0229

issn

1879-0909

pii

S0141-0229(14)00074-X

journal_volume

61-62

pub_type

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