Zeolitic imidazolate frameworks as effective crystalline supports for aspergillus-based laccase immobilization for the biocatalytic degradation of carbamazepine.

In this study, zeolitic imidazolate frameworks (ZIF) were employed as effective porous supports for laccase enzyme attachment and further explored synergistic adsorption and biocatalytic degradation of carbamazepine (CBZ) in aqueous solutions. Characterization results from FTIR and NMR analysis confirmed successful incorporation of the laccase enzyme onto ZIF particles. Further analyses from SEM and TEM revealed rhombic dodecahedral morphologies of ZIF crystals with crusts of the enzyme observed on the particles' surface. The carbamazepine degradation results showed that immobilization of the laccase improved its stability and resistance at various pH's, in comparison to the free enzyme. The immobilized laccase also exhibited relatively higher activities across the studied temperature range compared to the free form. Kinetic studies revealed a negligible decline in velocity, Vmax after immobilization, evaluated to be 0.873 and 0.692 mg L h for the free and immobilized laccase, respectively. The immobilized laccase demonstrated improved stabilities towards organic solvents, which qualifies the composite's application in real wastewater samples. In which case, the laccase-ZIF composite proved effective in CBZ decontamination with an efficiency of ∼92%. Furthermore, the immobilized laccase exhibited appreciable storage stabilities (∼70% residual activity) for up to 15 days before any significant loss in activity.