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Enzyme Encapsulation in Mesoporous Metal–Organic Frameworks for Selective Biodegradation of Harmful Dye Molecules
Author(s) -
Gkaniatsou Effrosyni,
Sicard Clémence,
Ricoux Rémy,
Benahmed Linda,
Bourdreux Flavien,
Zhang Qi,
Serre Christian,
Mahy JeanPierre,
Steunou Nathalie
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201811327
Subject(s) - mesoporous material , biocatalysis , chemistry , methyl orange , catalysis , metal organic framework , immobilized enzyme , selectivity , biodegradation , combinatorial chemistry , metal , enzyme , organic chemistry , reaction mechanism , adsorption , photocatalysis
Microperoxidase‐8, a small, peroxidase‐type enzyme was immobilized into nanoparticles of the mesoporous and ultra‐stable metal–organic framework (MOF) MIL‐101(Cr). The immobilized enzyme fully retained its catalytic activity and exhibited enhanced resistance to acidic conditions. The biocatalyst was reusable and showed a long‐term stability. By exploiting the properties of the MOF′s framework, we demonstrated, for the first time, that the MOF matrix could act in synergy with the enzyme (Microperoxidase‐8) and enhance selectivity the oxidation reaction of dyes. The oxidation rate of the harmful negatively charged dye (methyl orange) was significantly increased after enzyme immobilization, probably as a result of the pre‐concentration of the methyl orange reactant owing to a charge matching between this dye and the MOF.