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Angew Chem Int Ed Engl ; 57(49): 16141-16146, 2018 12 03.
Article in English | MEDLINE | ID: mdl-30307095

ABSTRACT

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.


Subject(s)
Coloring Agents/chemistry , Metal-Organic Frameworks/chemistry , Peroxidases/chemistry , Coloring Agents/metabolism , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Hydrogen-Ion Concentration , Metal-Organic Frameworks/metabolism , Models, Molecular , Molecular Structure , Nanoparticles/chemistry , Nanoparticles/metabolism , Particle Size , Peroxidases/metabolism , Porosity , Surface Properties
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