One biotechnological advancement in the field of biocatalysis is the immobilization of enzymes onto solid supports to create more stable and recyclable systems. Metal-organic frameworks (MOFs) are nanocomposite materials that have been explored as solid supports to facilitate enzyme immobilization. MOFs are composed of  organic linkers and inorganic nodes that form porous structures with large surface areas and have the ability to be modified postsynthetically. Our target enzyme system for immobilization is glucose oxidase (GOx) and chloroperoxidase (CPO). Glucose oxidase is a commercially available enzyme that catalyzes the oxidation of glucose used for many applications in biosensing, biofuel cells, and food production. Chloroperoxidase is a fungal heme enzyme that catalyzes peroxide-dependent halogenation, oxidation, and hydroxylation. These two enzymes work sequentially in this enzyme system by GOx producing peroxide which activates CPO that reacts with a suitable substrate. This study focuses on using a zirconium-based MOF, UiO-66-NH<sub>2</sub>, to immobilize the enzyme system, via crosslinking with the MOF’s amine group.  This study investigates the optimal conditions for enzyme loading, pH, and temperature to synthesize a more stable, and recyclable enzyme/MOF composite of the GOx/CPO enzyme biocatalytic system.

Optimizing enzyme immobilization via crosslinking to a metal-organic framework

ACS Spring Meeting 2021

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