Immobilization of a Bienzymatic System via Crosslinking to a Metal-Organic Framework

A leading biotechnological advancement in the field of biocatalysis is immobilization enzymes on solid supports to create more stable and recyclable systems. Metal-organic frameworks (MOFs) are porous materials that have been explored as for enzyme immobilization. Composed organic linkers inorganic nodes, MOFs feature empty void space with large surface areas ability be modified post-synthesis. Our target system glucose oxidase (GOx) chloroperoxidase (CPO). Glucose catalyzes oxidation used many applications biosensing, biofuel cells, food production. Chloroperoxidase a fungal heme peroxide-dependent halogenation, oxidation, hydroxylation. These two work sequentially this by GOx producing peroxide, which activates CPO reacts suitable substrate. This study focuses using zirconium-based MOF, UiO-66-NH2, immobilize via crosslinking MOF’s amine group MOF. investigates different crosslinkers: disuccinimidyl glutarate (DSG) 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC)/N-hydroxysuccinidimide (NHS), providing MOF enzymes. The crosslinkers covalently bond onto comparison recyclability enzymatic activity single doubly immobilized discussed through assays characterization analyses. DSG-crosslinked composites displayed enhanced relative free enzyme, all crosslinked enzyme/MOF demonstrated recyclability, at least 30% being retained after four catalytic cycles. results report will aid researchers utilizing biocatalyst active has greater recyclability.