PURIFICATION AND CHARACTERIZATION OF DIHYDROGEODIN OXIDASE FROM A FUNGAL STRAIN OF ASPERGILLUS TERREUS PRODUCING (+)-GEODIN

Abstract

Dihydrogeodin oxidase (DHGO), an enzyme catalyzing regio- and stereo-specific intramolecular phenol oxidative coupling reaction of dihydrogeodin to give (+)-geodin, was purified up to homogeneity. DHGO was shown to be a blue copper protein with an absorption maximum at 600 nm. The presence of copper atoms was confirmed by atomic absorption analysis. A molecular weight of 153, 000 was estimated for the oxidase and it was composed of two equal molecular weight subunits. DHGO had no phenolase activity and showed strict substrate specificity.