Issue 17, 2023

Removal of trichloroethene by glucose oxidase immobilized on magnetite nanoparticles

Abstract

To overcome the safety risks and low utilization efficiency of H2O2 in traditional Fenton processes, in situ production of H2O2 by enzymatic reactions has attracted increasing attention recently. In this study, magnetite-immobilized glucose oxidase (MIG) was prepared to catalyze the heterogeneous Fenton reaction for the removal of trichloroethene from water. The successful immobilization of glucose oxidase on magnetite was achieved with a loading efficiency of 70.54%. When combined with substrate glucose, MIG could efficiently remove 5–50 mg L−1 trichloroethene from water with a final removal efficiency of 76.2% to 94.1% by 192 h. This system remained effective in the temperature range of 15–45 °C and pH range of 3.6–9.0. The removal was slightly inhibited by different cations and anions (influencing degree Ca2+ > Mg2+ > Cu2+ and H2PO4 > Cl > SO42−) and humic acid. Meanwhile, the MIG could be recycled for 4 cycles and was applicable to other chlorinated hydrocarbons. The results of reactive oxidative species generation monitoring and quenching experiments indicated that H2O2 generated by the enzymatic reaction was almost completely decomposed by magnetite to produce ·OH with a final cumulative concentration of 129 μM, which played a predominant role in trichloroethene degradation. Trichloroethene was almost completely dechlorinated into Cl, CO2 and H2O without production of any detectable organic chlorinated intermediates. This work reveals the potential of immobilized enzymes for in situ generation of ROS and remediation of organic chlorinated contaminants.

Graphical abstract: Removal of trichloroethene by glucose oxidase immobilized on magnetite nanoparticles

Supplementary files

Article information

Article type
Paper
Submitted
21 Feb 2023
Accepted
10 Apr 2023
First published
18 Apr 2023
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2023,13, 11853-11864

Removal of trichloroethene by glucose oxidase immobilized on magnetite nanoparticles

M. Wang, Y. Huang and H. Liu, RSC Adv., 2023, 13, 11853 DOI: 10.1039/D3RA01168B

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