Session: Undergraduate Research at the Frontiers of Inorganic Chemistry:

Enzymes are attractive for use as biocatalysts for their high specificity towards substrates, lower energy requirements, and contribution to sustainable chemistry. However, free enzymes tend to be relatively unstable in industrial conditions. Immobilizing enzymes onto solid supports can increase their stability and provide additional benefits such as enhanced catalytic activity and increased recyclability. Crosslinking is one method of enzyme immobilization, where two molecules are linked together by covalently binding to a crosslinking reagent. This study focuses on using the crosslinking method to immobilize enzymes – horseradish peroxidase (HRP), glucose oxidase (GO_x), and chloroperoxidase (CPO) – on metal-organic frameworks (MOFs) – UiO-66-NH₂ and NH₂-MIL-68(Al). Metal-organic frameworks were chosen as solid supports due to their high surface areas and tunable porosity, and UiO-66-NH₂ and NH₂-MIL-68(Al) in particular were chosen due to their amine group, which could be used as a site for covalent linkage to crosslinking reagents. Infrared spectroscopy was used to compare the effectiveness of crosslinker reagents glutaraldehyde,1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC), and disuccinimidyl glutarate (DSG), and enzymatic assays were performed to confirm the enzymatic activity of the immobilized enzymes.

Sydnie Rizaldo

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