Confinement of biomolecules in porous material offers long-term chemical/thermal stability, tunable catalytic performance, and enhanced cost-efficiency. Of particular importance is the confinement of proteins, the most sophisticated biocatalysts in life-sustaining biological processes with catalytic efficiency, specificity, and selectivity often far exceeding artificial catalysts. The primary driving force of protein confinement is the physical interaction with the supporting matrix, which is crucial to protein industrialization and restoring bio-functionality/structural integrity under unnatural conditions. However, only limiting proteins with suitable dimensions were successfully immobilized into the instinct pores of novel porous materials like MOFs, COFs, and HOFs; the undersized cavities/apertures inhibited proteins' infiltration into porous matrices. Thus, the template-growth porous matrices could provide sufficient space (&gt;50 nm) for accommodating proteins with an extensive range of dimensions and efficiently integrate these bio functions, which are usually carried out under natural/mild conditions, in those matric materials. Furthermore, the properties of the classic materials are often difficult to fine-tune, thus leading to heterogeneous, uncontrollable protein-host materials interactions. The surface modifications of hollow porous materials are targeted to overcome these barriers, resulting in higher loading capacity, abundant protein-matrix interactions, and more friendly microenvironments.

Encapsulating large biomolecules in hierarchically- ordered porous materials

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ACS Fall 2022

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