Abstract
Laccase, a so-called “blue-copper” oxidase, is able to oxidize a variety of organic compounds. Sol–gel derived silica glasses are frequently adopted as an immobilization method to improve the stability of enzymes and make them reusable. In this study, immobilization conditions were optimized to achieve improved embedding results. The thermal stability, reaction stability and storage stability were improved with the immobilized enzyme when compared to the free enzyme. 2,4-Dichlorophenol (DCP) and 2,4,6-trichlorophenol (TCP) were chosen as model compounds. The treatment of chlorophenols (CPs) by immobilized laccase demonstrated excellent removal and response stability. The affinity of TCP for immobilized laccase was higher than that of DCP. This finding leads to different removal efficiencies under variable conditions (reaction time, initial concentration, dosage of immobilized laccase and removal rate in mixed solution). By fitting the experimental data with the diffusion model of the degradation process, the degradation of CPs by immobilized laccase matches an intraparticle diffusion-controlled model.
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