A novel and efficient oxidative functionalization of lignin by layer-by-layer immobilised Horseradish peroxidase

Bioorg Med Chem. 2011 Jan 1;19(1):440-7. doi: 10.1016/j.bmc.2010.11.009. Epub 2010 Nov 10.

Abstract

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.

MeSH terms

  • Enzymes, Immobilized / metabolism*
  • Horseradish Peroxidase / metabolism*
  • Lignin / metabolism*
  • Microscopy, Electron, Scanning
  • Oxidation-Reduction

Substances

  • Enzymes, Immobilized
  • Lignin
  • Horseradish Peroxidase