Enzyme immobilization has been widely studied to enhance enzymatic stability while retaining functionality. However, the flexibility and activity of the immobilized enzymes are usually compromised after immobilization processes. In this work, through the capable post-synthetic strategy of metal-organic frameworks (MOFs), an enzyme/MOFs composite system was developed to mimic natural environments for the encapsulated enzymes. Correlating to the kinetic studies of hydrogen peroxide (H2O2) degradation to the fluorescence shifts of urea unfolded catalases, the encapsulated catalases exhibited the recovered bioactivity with the increased enzymatic flexibility, which demonstrates the limited biofunctionality by external MOFs materials. The higher Michaelis-Menten constant (KM) and maximum rate conversion (Vmax) of the encapsulated catalases after reducing confinement indicate the restored biofunctionality compared to the fully confined catalases. Overall, this enzyme/MOFs system provides a new approach to study the confinement effect in enzyme immobilization and reveal the significant correlation between enzymatic flexibility and activity.

Enzyme immobilization with reduced confinement in metal-organic frameworks

2019 Fall National Meeting

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