Enzyme immobilization is critical to boosting its application in various areas. Covalent organic frameworks (COFs) are ideal hosts for enzyme immobilization due to their porous and predesignable structures. Nevertheless, the construction of COFs-based enzyme immobilization systems with high activity via existing immobilization methods (including covalent linkages and channel entrapment) remains a considerable challenge. Herein, a versatile approach was introduced to encapsulate enzymes within hollow COF capsule (named enzyme@COF) using metal-organic frameworks (including ZPF-1(C8H11N4O4.5Zn), ZIF-8(C8H10N4Zn), and ZIF-90(C8H6N4O2Zn)) as sacrificial templates. The obtained porous COF capsule could not only facilitate the efficient mass transfer of enzymatic reactions but also protect enzymes against the incompatible conditions, resulting in enhanced activity and stability of the encapsulated enzymes. Moreover, this approach offered an opportunity to spatially organize multienzymes in COF capsule to construct enzyme cascade system. For instance, glucose oxidase (GOx) and cytochrome c (Cyt c) were coencapsulated within COF capsule to construct GOx-Cyt c cascade. The integration of GOx and Cyt c within COF capsule achieved ∼1.6-fold improvement in catalytic activity than that of free enzymes and the resultant GOx-Cyt c@COF was successfully adopted as a nanoreactor for the sensitive determination of glucose in serum. This work provided a new insight into the design of COFs-based enzyme immobilization systems.
Read full abstract