Controllable regulations on the enzyme conformation to optimize catalytic performance are highly desired for the immobilized biocatalysts yet remain challenging. Covalent organic frameworks (COFs) possess confined channels with finely tunable pore environment, offering a promising platform for enzyme encapsulation. Herein, we covalently immobilized the cytochrome c (Cyt c) in the size‐matched channels of COFs with different contents of anchoring site, and significant enhancement of the stability and activity (≈600 % relative activity compared with free enzyme) can be realized by optimizing the covalent interactions. Structural analyses on the immobilized Cyt c suggest that covalent bonding could induce conformational perturbation resulting in more accessible active sites. The effectiveness of the covalent interaction modulation together with the tailorable confined channels of COFs offers promise to develop high‐performance biocatalysts.

Pore environment and aggregated structure play a vital role in determining the properties of porous materials, especially regarding the mass transfer. Reticular chemistry imparts covalent organic frameworks (COFs) with well-aligned micro/mesopores, yet constructing hierarchical architectures remains a great challenge. Herein, we reported a COF-to-COF transformation methodology to prepare microtubular COFs. In this process, the C 3 -symmetric guanidine units decomposed into C 2 -symmetric hydrazine units, leading to the crystal transformation of COFs. Moreover, the aggregated structure and conversion degree varied with the reaction time, where the hollow tubular aggregates composed of mixed COF crystals could be obtained. Such hierarchical architecture leads to enhanced mass transfer properties, as proved by the adsorption measurement and chemical catalytic reactions. This selftemplate strategy was successfully applied to another four COFs with different building units.

Controllable regulations on the enzyme conformation to optimize catalytic performance are highly desired for the immobilized biocatalysts yet remain challenging. Covalent organic frameworks (COFs) possess confined channels with finely tunable pore environment, offering a promising platform for enzyme encapsulation. Herein, we covalently immobilized the cytochrome c (Cyt c) in the size‐matched channels of COFs with different contents of anchoring site, and significant enhancement of the stability and activity (≈600 % relative activity compared with free enzyme) can be realized by optimizing the covalent interactions. Structural analyses on the immobilized Cyt c suggest that covalent bonding could induce conformational perturbation resulting in more accessible active sites. The effectiveness of the covalent interaction modulation together with the tailorable confined channels of COFs offers promise to develop high‐performance biocatalysts.

Pore environment and aggregated structure play a vital role in determining the properties of porous materials, especially regarding the mass transfer. Reticular chemistry imparts covalent organic frameworks (COFs) with well‐aligned micro/mesopores, yet constructing hierarchical architectures remains a great challenge. Herein, we reported a COF‐to‐COF transformation methodology to prepare microtubular COFs. In this process, the C3‐symmetric guanidine units decomposed into C2‐symmetric hydrazine units, leading to the crystal transformation of COFs. Moreover, the aggregated structure and conversion degree varied with the reaction time, where the hollow tubular aggregates composed of mixed COF crystals could be obtained. Such hierarchical architecture leads to enhanced mass transfer properties, as proved by the adsorption measurement and chemical catalytic reactions. This self‐template strategy was successfully applied to another four COFs with different building units.