In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium.
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.
Wariishi
H
H
Dept. of Chemical & Biological Sciences, Oregon Graduate Institute of Science & Technology, Beaverton 97006-1999.
Valli
K
K
Gold
M H
MH
D001487:Basidiomycota / Q000201:enzymology*; D002250:Carbon Radioisotopes; D002850:Chromatography, Gel; D007700:Kinetics; D008031:Lignin / Q000302:isolation & purification / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D011865:Radioisotope Dilution Technique; D013379:Substrate Specificity
D002250:Carbon Radioisotopes; D008031:Lignin; D010544:Peroxidases; C051129:manganese peroxidase