The extracellular lignin peroxidase from the white-rot basidiomycete Phanerochaete chrysosporium is thought to play an important role in lignin biodegradation. However, the majority of lignin-derived preparations actually experience overall polymerization at the hands of the enzyme in vitro. It has now been found that, in the presence of H2O2 at pH 4.0, the monomeric lignin precursor coniferyl alcohol is polymerized quantitatively by a lignin peroxidase preparation which is uncontaminated with Mn(II)-dependent peroxidases. 13C NMR spectrometry of the resulting dehydropolymerisates from 13C-labeled monolignols confirms that the frequencies of different interunit linkages are very similar to those engendered through the action of horseradish peroxidase with H2O2. Indeed, lignin peroxidase does not ultimately seem to be a prerequisite for lignin degradation in vivo, yet its activity can still accelerate the conversion of lignin-derived preparations by P. chrysosporium to CO2. Consequently, lignin peroxidase can provisionally be expected to fulfill two important functions. On the one hand, the enzyme may detoxify lower molecular weight phenolic compounds released from lignins during their fungal decomposition. On the other hand, through the introduction of suitable functional groups, lignin peroxidase could indirectly enhance the susceptibility of macromolecular lignin structures toward depolymerization by another enzyme.
|Original language||English (US)|
|Number of pages||8|
|Journal||Journal of Biological Chemistry|
|State||Published - 1991|