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Title: Oxidation of wheat straw lignin by fungal lignin peroxidase, manganese peroxidase and laccase: A comparative study

Conference ·
OSTI ID:370063
;  [1]
  1. Laboratorie de Chimie Biologique, Thiverval-Grignon (France)

Lignin peroxidase (LiP), manganese peroxidase (MnP) from Phanerochaete chrysosporium and laccase from Pleurotus eryngii were separately used to degrade alkali wheat straw lignin (AL). In order to characterize the catalytic action of the different enzymes, the chemical structure and the hydrodynamic properties of the treated lignin were analyzed by thioacidolysis-gas chromatography and molecular size exclusion chromatography. The results confirmed that only LiP was able to degrade guiacyl (G) and syringyl (S) structures in non-phenolic methylated lignins. However, provided that some phenolic terminal structures are present, MnP and laccase were able to degrade the non-phenolic portion of the polymer linked by {beta}-O-4 alkyl aryl ether bonds. This suggested that the oxidative reactions catalyzed in alkali straw lignin could progress through bond cleavages generating phenoxy radicals. The molecular size distribution of both thioacidolysis products and the oxidized polymer showed that AL underwent condensation side-reactions regardless of the enzyme treatment, but only LiP oxidation led to the increase in the hydrodynamic volume of the recovered lignin. This indicated that modification of enzymes by bonding patterns in lignin is not always associated with alterations in the spatial network of the polymer.

OSTI ID:
370063
Report Number(s):
CONF-960376-; TRN: 96:003805-0114
Resource Relation:
Conference: Spring national meeting of the American Chemical Society (ACS), New Orleans, LA (United States), 24-28 Mar 1996; Other Information: PBD: 1996; Related Information: Is Part Of 211th ACS national meeting; PB: 2284 p.
Country of Publication:
United States
Language:
English