| Literature DB >> 30307095 |
Effrosyni Gkaniatsou1, Clémence Sicard1, Rémy Ricoux2, Linda Benahmed1, Flavien Bourdreux1, Qi Zhang1,3, Christian Serre4, Jean-Pierre Mahy2, Nathalie Steunou1.
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.Entities:
Keywords: biocatalysis; enzymes; immobilization; metal-organic frameworks (MOFs); oxidation
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Year: 2018 PMID: 30307095 DOI: 10.1002/anie.201811327
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336