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Molecules 2016, 21(8), 1044; doi:10.3390/molecules21081044

Catalytic Oxidation of Phenol and 2,4-Dichlorophenol by Using Horseradish Peroxidase Immobilized on Graphene Oxide/Fe3O4

College of Resources and Environmental Science, South Central University for Nationalities, Wuhan 430074, China
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Academic Editor: Roberto Fernandez-Lafuente
Received: 12 April 2016 / Revised: 30 July 2016 / Accepted: 3 August 2016 / Published: 10 August 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
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Abstract

Graphene oxide/Fe3O4 (GO/Fe3O4) nanoparticles were synthesized by an ultrasonic-assisted reverse co-precipitation method, and then horseradish peroxidase (HRP) was covalently immobilized onto GO/Fe3O4 with 1-ethyl-3-(3-dimethyaminopropyl)carbodiimide (EDC) as a cross-linking agent. In order to enhance the phenol removal efficiency and prevent the inactivation of the enzyme, the polyethylene glycol with highly hydrophilicity was added in this reaction, because the adsorption capacity for the polymer by degradation was stronger than the HRP. The results showed that the immobilized enzyme removed over 95% of phenol from aqueous solution. The catalytic condition was extensively optimized among the range of pH, mass ratio of PEG/phenol as well as initial concentration of immobilized enzyme and H2O2. The HRP immobilized on GO/Fe3O4 composite could be easily separated under a magnetic field from the reaction solution and reused. View Full-Text
Keywords: graphene oxide; magnetite; phenol; immobilized enzyme; catalytic oxidation graphene oxide; magnetite; phenol; immobilized enzyme; catalytic oxidation
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Chang, Q.; Huang, J.; Ding, Y.; Tang, H. Catalytic Oxidation of Phenol and 2,4-Dichlorophenol by Using Horseradish Peroxidase Immobilized on Graphene Oxide/Fe3O4. Molecules 2016, 21, 1044.

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