Immobilization of laccase onto meso-MIL-53(Al) via physical adsorption for the catalytic conversion of triclosan

Abstract

Due to the abundant binding sites and high stability, a synthesized meso-MIL-53(Al) was selected as the backbone and used for immobilizing laccase (Lac-MIL-53(Al)) to catalytically degrade of TCS. XRD, BET and FTIR analyses proved that the carboxyl groups on PTA of meso-MIL-53(Al) could provide sufficient adsorption sites for physically immobilizing laccase through hydrogen bonds and electrostatic interactions. Although the catalytic efficiency of Vmax/Km slightly decreased from 785 to 607 min−1 due to the mass transfer limitation upon immobilized, Lac-MIL-53(Al) showed high activity recovery (93.8%) and stability. The conformational analysis indicated the laccase could partially enter into the MOF by conformational changes without impairing laccase, although the laccase molecular (6.5 nm × 5.5 nm × 4.5 nm) was larger than the mesopore sizes of the MOF (4 nm). The kinetics indicated that Lac-MIL-53(Al) could remove 99.24% of TCS within 120 min due to the synergy effect of the adsorption of meso-MIL-53(Al) and catalytic degradation of laccase. Meanwhile, Lac-MIL-53(Al) could remain approximately 60% of activity for up to 8 times reuse without desorption. The GC/MS and LC/MS/MS analyses further confirmed that TCS could be transformed to 2, 4-DCP by laccase via the breakage of the ether bond, or to passivated dimers, trimers and tetramers by the self-coupling and oxidization of the phenoxyl radicals, and finally removed by precipitation. In summary, enzyme-MOF composite might be a potential strategy to control the micropollutants in the wastewater.