A synthetic metalloporphine was immobilized onto a PVA-based and mercapto-grafted solid support, emulating the active site of cytochrome P450. Its ligninolytic peroxidase-like catalytic activity was studied. The coord...A synthetic metalloporphine was immobilized onto a PVA-based and mercapto-grafted solid support, emulating the active site of cytochrome P450. Its ligninolytic peroxidase-like catalytic activity was studied. The coordinated mercapto ligand significantly affected the catalytic features of the catalyst because the oxidation of lignin-model compounds was very slow by comparison with imidazoleand pyridine-coordinated immobilized metalloporphines. Conversely, the catalyst efficiently bleached several industrial dyes and thus demonstrated promising activity for this application. Based on this altered substrate specificity the oxygen-donor catalytic route seems to be more favorable than a single electron oxidation pathway.展开更多
基金supported by the Regione Autonoma Sardegna (PO Sardegna FSE 2007-2013, L.R.7/2007, Bando Giovani Ricercatori, Project CRP1_27)
文摘A synthetic metalloporphine was immobilized onto a PVA-based and mercapto-grafted solid support, emulating the active site of cytochrome P450. Its ligninolytic peroxidase-like catalytic activity was studied. The coordinated mercapto ligand significantly affected the catalytic features of the catalyst because the oxidation of lignin-model compounds was very slow by comparison with imidazoleand pyridine-coordinated immobilized metalloporphines. Conversely, the catalyst efficiently bleached several industrial dyes and thus demonstrated promising activity for this application. Based on this altered substrate specificity the oxygen-donor catalytic route seems to be more favorable than a single electron oxidation pathway.
