Bioinspired versus enzymatic oxidation of some homologous thionine dyes in the presence of immobilized metalloporphyrin catalysts and ligninolytic enzymes

Cocco, Gianmarco
First
;
Sanjust, Enrico
Penultimate
;
Zucca, Paolo
Last
2017-01-01

Abstract

Thionines are recalcitrant and polluting textile dyes presenting various degrees of N-methylation. In this paper, a complete series of homologous thionines was used as the substrates for oxidation in the presence of a bioinspired commercial iron-porphyrin immobilized on to imidazoleand pyridine-functionalized fumed silica, to emulate the active site of ligninolytic peroxidases. The obtained catalytic adducts showed a remarkable ability to catalyze thionine dye oxidation in the presence of different oxidants such as potassium monopersulfate and hydrogen peroxide. Different oxidation patterns were obtained and mechanistically discussed, in comparison with those observed in the presence of some ligninolytic oxidizing enzymes.
2017
Biomimetic; Hydrogen peroxide; Metalloporphines; Metalloporphyrins; Monopersulfate; Peroxidase; Peroxygenase; Thionine; Catalysis; Molecular Biology; Spectroscopy; Computer Science Applications1707 Computer Vision and Pattern Recognition; Physical and Theoretical Chemistry; Organic Chemistry; Inorganic Chemistry
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