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. 1991 Apr 15;176(1):269-75.
doi: 10.1016/0006-291x(91)90919-x.

In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium

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In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium

H Wariishi et al. Biochem Biophys Res Commun. .

Abstract

Homogeneous manganese peroxidase catalyzed the in vitro partial depolymerization of four different 14C-labeled synthetic lignin preparations. Gel permeation profiles demonstrated significant depolymerization of 14C-sidechain-labeled syringyl lignin, a 14C-sidechain-labeled syringyl-guaiacyl copolymer (angiosperm lignin), and depolymerization of 14C-sidechain- and 14C-ring-labeled guaiacyl lignins (gymnosperm lignin). 3,5-Dimethoxy-1,4-benzo-quinone, 3,5-dimethoxy-1,4-hydroquinone, and syringylaldehyde were identified as degradation products of the syringyl and syringyl-guaiacyl lignins. These results suggest that manganese peroxidase plays a significant role in the depolymerization of lignin by Phanerochaete chrysosporium.

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