| Literature DB >> 21130661 |
Raffaella Perazzini1, Raffaele Saladino, Melissa Guazzaroni, Claudia Crestini.
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. Copyright ÂEntities:
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Year: 2010 PMID: 21130661 DOI: 10.1016/j.bmc.2010.11.009
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641