Tuning Pore Heterogeneity in Covalent Organic Frameworks for Enhanced Enzyme Accessibility and Resistance against Denaturants

Achieving high‐performance biocomposites requires knowledge of the compatability between the immobilized enzyme and its host material. The modular nature of covalent organic frameworks (COFs), as a host, allows their pore geometries and chemical functionalities to be fine‐tuned independently, permitting comparative studies between the individual parameters and the performances of the resultant biocomposites. This research demonstrates that dual pores in COFs have profound consequences on the catalytic activity and denaturation of infiltrated enzymes. This approach enforces a constant pore environment by rational building‐block design, which enables it to be unequivocally determined that pore heterogeneity is responsible for rate enhancements of up to threefold per enzyme molecule. More so, the enzyme is more tolerant to detrimental by‐products when occupying the larger pore in a dual‐pore COF compared to a corresponding uniform porous COF. Kinetic studies highlight that pore heterogeneity facilitates mass transfer of both reagents and products. This unparalleled versatility of these materials allows many different aspects to be designed on demand, lending credence to their prospect as next‐generation host materials for various enzyme biocomposites catalysts. The inimitable role of hierarchical pore structure on catalytic efficiency and robustness is delineated by comparing the enzymatic performance of biocomposites using covalent orgainc frameworks with similar pore environments yet different pore structures.