In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium

Journal Article · Mon Apr 15 00:00:00 EDT 1991 · Biochemical and Biophysical Research Communications; (USA)

DOI:https://doi.org/10.1016/0006-291X(91)90919-X· OSTI ID:5801598

Wariishi, H; Valli, K; Gold, M H ^[1]

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1. Oregon Graduate Institute of Science Technology, Beaverton (USA)

Homogeneous manganese peroxidase catalyzed the in vitro partial depolymerization of four different {sup 14}C-labeled synthetic lignin preparations. Gel permeation profiles demonstrated significant depolymerization of {sup 14}C-sidechain-labeled syringyl lignin, a {sup 14}C-sidechain-labeled syringyl-guaiacyl copolymer (angiosperm lignin), and depolymerization of {sup 14}C-sidechain- and {sup 14}C-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.

• OSTI ID: 5801598
• Journal Information: Biochemical and Biophysical Research Communications; (USA), Vol. 176:1; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
LIGNIN
DEPOLYMERIZATION
PEROXIDASES
BIOCHEMICAL REACTION KINETICS
CARBON 14 COMPOUNDS
FUNGI
IN VITRO
ISOTOPE DILUTION
METABOLISM
TRACER TECHNIQUES
CARBOHYDRATES
CHEMICAL REACTIONS
DECOMPOSITION
ENZYMES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PLANTS
POLYSACCHARIDES
REACTION KINETICS
SACCHARIDES
550501* - Metabolism- Tracer Techniques