Sructural features of lignin determining its biodegradation by oxidative enzymes and related systems
| Autor: | M.J. Martinez-inigo, I. Artaud, Christelle Lequart, Bernard Kurek, Bernard Monties, Bonnie Hames |
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| Přispěvatelé: | Unité de physicochimie et biotechnologie des polymères, Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
0106 biological sciences
Polymers and Plastics Ether macromolecular substances complex mixtures 01 natural sciences Enzyme catalysis chemistry.chemical_compound 010608 biotechnology Oxidative enzyme [SDV.IDA]Life Sciences [q-bio]/Food engineering Materials Chemistry Lignin Organic chemistry [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering ComputingMilieux_MISCELLANEOUS Laccase 010405 organic chemistry fungi technology industry and agriculture food and beverages Biodegradation Condensed Matter Physics 0104 chemical sciences chemistry Mechanics of Materials Lignin network Macromolecule |
| Zdroj: | Polymer Degradation and Stability Polymer Degradation and Stability, Elsevier, 1998, 59, pp.359-364 |
| ISSN: | 0141-3910 1873-2321 |
| Popis: | Peroxidases and laccases are key enzymes in the lignin biodegradation process. They oxidize phenolic and non-phenolic lignin model compounds into their phenoxy and cation radicals, respectively. Further non-enzymatic evolution lead then to various C-C and ether bond cleavages. Nevertheless, almost no information on the structural alterations undergone in vitro or in situ by lignin after enzymatic catalysis is available. We report here on the molecular structure of lignin oxidized by various (per)oxidasic systems. The oxidizability of phenolic and non-phenolic structures of the guaiacyl and syringyl type in the lignin network will be discussed as well as the modification of the macromolecular properties of the polymer oxidized in situ or in isolated state. |
| Databáze: | OpenAIRE |
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