催化学报

催化学报 ›› 2011, Vol. 32 ›› Issue (11): 1663-1666.DOI: 10.1016/S1872-2067(10)60277-X

• 研究快讯 • 上一篇    下一篇

Ligninolytic Peroxidase-Like Activity of a Synthetic Metalloporphine Immobilized onto Mercapto-Grafted Crosslinked PVA Inspired by the Active Site of Cytochrome P450

Paolo ZUCCA1,*, Antonio RESCIGNO1,2, Enrico SANJUST1,2   

  1. 1Dipartimento di Scienze e Tecnologie Biomediche, Università di Cagliari, Monserrato 09042, Italy; 2Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, Sesto Fiorentino 50019, Italy
  • 收稿日期:2011-08-02 修回日期:2011-09-13 出版日期:2011-11-14 发布日期:2015-03-30

Ligninolytic Peroxidase-Like Activity of a Synthetic Metalloporphine Immobilized onto Mercapto-Grafted Crosslinked PVA Inspired by the Active Site of Cytochrome P450

Paolo ZUCCA1,*, Antonio RESCIGNO1,2, Enrico SANJUST1,2   

  1. 1Dipartimento di Scienze e Tecnologie Biomediche, Università di Cagliari, Monserrato 09042, Italy; 2Consorzio per lo Sviluppo dei Sistemi a Grande Interfase, Sesto Fiorentino 50019, Italy
  • Received:2011-08-02 Revised:2011-09-13 Online:2011-11-14 Published:2015-03-30

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摘要： 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 imidazole- and 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.

关键词: porphine, porphyrin, lignin peroxidase, cytochrome P450, biomimetic

Abstract: 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 imidazole- and 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.

Key words: porphine, porphyrin, lignin peroxidase, cytochrome P450, biomimetic