Dearomatization of lignin derivatives by fungal protocatechuate 3,4‐dioxygenase immobilized on porosity glass

Abstract

Protocatechuate 3,4-dioxygenase (see protocatechuate: oxygen 3,4-oxidoreductase, EC 1.13.11.3) was isolated from the mycelium of Pleurotus ostreatus (induced with p-hydroxybenzoic acid) and immobilized on controlled porosity glass beads. Four fractions of Na-lignosulfonates (varying in M(r), after chromatography on Sephadex G-50) were treated with the immobilized enzyme. The products after incubation showed the same M(r) as the untreated fractions, but their light absorption at 280 nm considerably decreased. These studies indicate that dioxygenase causes partial dearomatization of lignin macromolecule.