Abstract
The use of the laccase enzyme from the fungus Trametes versicolor, coupled with the mediator 1-hydroxybenzotriazole (1-HBT) has been shown to be effective for the biocatalytic conversion of a hexameric lignin model compound containing three of the most common linkages found in native lignin. Cleavage of the model takes place over a 24 hours period predominantly at the β-O-4 ether linkage to give a previously known β-5 dimer intermediate which in turn was rapidly consumed to further degradation products. There is also mass spectrometric evidence of repolymerisation of the β-5 dimer and other degradation intermediates to form higher oligomers. Mechanistic pathways to account for the major catalytic processes are proposed.
Original language | English |
---|---|
Pages (from-to) | 10851–10858 |
Number of pages | 9 |
Journal | Green Chemistry |
Volume | 26 |
Early online date | 20 Jun 2024 |
DOIs | |
Publication status | Published - 21 Jun 2024 |
Keywords
- laccase enzyme
- Trametes versicolor
- mediator 1-hydroxybenzotriazole (1-HBT)
- biocatalytic conversion
- hexameric lignin model
- native lignin
- β-O-4 ether linkage
- oligomers
- catalytic processes