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Dearomatization of lignin derivatives by fungal protocatechuate 3,4‐dioxygenase immobilized on porosity glass
Author(s) -
WojtaśWasilewska M.,
Luterek J.,
Leonowicz A.,
Dawidowicz A.
Publication year - 1988
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260320413
Subject(s) - chemistry , lignin , pleurotus ostreatus , sephadex , lignosulfonates , mycelium , dioxygenase , porous glass , chromatography , enzyme , porosity , organic chemistry , food science , botany , biology , mushroom
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.