Purification and Some Properties of Lignostilbene-α, β-dioxygenase Responsible for the Cα-Cβ Cleavage of a Diarylpropane Type Lignin Model Compound from Pseudomonas sp. TMY1009
1989 Volume 53 Issue 10 Pages 2757-2761
Details
1989 Volume 53 Issue 10 Pages 2757-2761
A novel dioxygenase, lignostilbene-α, β-dioxygenase (LSD), which catalyzes cleavage of the interphenyl double bond of lignin-derived stilbenes, was isolated. Four isozymes of LSD were separated from cell-free extracts of Pseudomonas sp. TMY1009 by ion-exchange chromatography on a DEAE-Toyopearl column. The major isozyme, LSD-I, was purified to electrophoretic homogeneity and characterized.
LSD-I cleaved the interphenyl double bond of 1, 2-bis(4'-hydroxy-3'-methoxyphenyl)ethylene with the optimum pH at 8.5. The Km of LSD-I was 11 μM for the stilbene and 110 μM for oxygen. The molecular weight of LSD-I, which is composed of two identical subunits, was estimated to be 94, 000. LSD-I contained 1 g atom of iron per 1 mol of enzyme protein.
This article cannot obtain the latest cited-by information.
