A novel and efficient oxidative functionalization of lignin by layer-by-layer immobilised Horseradish peroxidase.
Horseradish peroxidase (HRP) was chemically immobilised onto alumina particles and coated by polyelectrolytes layers, using the layer-by-layer technique. The reactivity of the immobilised enzyme was studied in the oxidative functionalisation of softwood milled wood and residual kraft lignins and found higher than the free enzyme. In order to investigate the chemical modifications in the lignin structure, quantitative (31)P NMR was used. The immobilised HRP showed a higher reactivity with respect to the native enzyme yielding extensive depolymerisation of lignin.
Dipartimento di Scienze e Tecnologie Chimiche, Tor Vergata University, Via della Ricerca Scientifica, 00133 Rome, Italy.
Raffaella
R
Perazzini
Raffaele
R
Saladino
Melissa
M
Guazzaroni
Claudia
C
Crestini
D004800:Enzymes, Immobilized / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D008031:Lignin / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D010084:Oxidation-Reduction
D004800:Enzymes, Immobilized; D008031:Lignin; D006735:Horseradish Peroxidase