Embedding an enzyme within aMOF as exoskeleton (enzyme@MOF) offers new opportunities to improve the inherent fragile nature of the enzyme,but also to impart novel biofunctionality to the MOF.D espite the remarkable stability achieved for MOF-embedded enzymes,e mbedding patterns and conversion of the enzymatic biofunctionality after entrapment by aM OF have only received limited attention. Herein, we reveal howe mbedding patterns affect the bioactivity of an enzyme encapsulated in ZIF-8. The enzyme@MOF can maintain high activity when the encapsulation process is driven by rapid enzyme-triggered nucleation of ZIF-8. When the encapsulation is driven by slow coprecipitation and the enzymes are not involved in the nucleation of ZIF-8, enzy-me@MOF tends to be inactive owing to unfolding and competing coordination caused by the ligand, 2-methyl imidazole.T hese two embedding patterns can easily be controlled by chemical modification of the amino acids of the enzymes,modulating their biofunctionality.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

Cell‐free enzymatic catalysis (CFEC) is an emerging biotechnology that enable the biological transformations in complex natural networks to be imitated. This biomimetic approach allows industrial products such as biofuels and biochemical to be manufactured in a green manner. Nevertheless, the main challenge in CFEC is the poor stability, which restricts the effectiveness and lifetime of enzymes in sophisticated applications. Immobilization of the enzymes within solid carriers is considered an efficient strategy for addressing these obstacles. Specifically, putting an “armor‐like” porous metal–organic framework (MOF) exoskeleton tightly around the enzymes not only shields the enzymes against external stimulus, but also allows the selective transport of guests through the accessible porous network. Herein we present the concept of this biotechnology of MOF‐entrapped enzymes and its cutting‐edge applications.

This work reports a new protein-directed, hydrogen-bonded assembly strategy to organize proteins and organic linkers into robust hybrid frameworks. The pconjugated carboxylate linkers are feasible to be anchored on the peptide backbone of proteins through hydrogen-bonded interaction and then by

Rationally tailoring ar obust artificial coating can enhance the lifetime of fragile biomacromolecules.H owever, the coating also can restrain the activity of the guest because of the decreased substrate accessibility.H erein, we report ap eptide-directed strategy that enables in situ tailoring of the MOFshrouded biohybrids into controllable nanoarchitectures.T he MOF biohybrid can be shaped from different 3D microporous architectures into a2 Dm esoporous layer by ap eptide modulator.U sing this mild strategy,w es how that the nanoarchitectures of the MOF coatings significantly affect the biological functions of the contained biomacromolecules.The biomacromolecules entrapped within the novel 2D mesoporous spindle-shaped MOFs (2D MSMOFs) have significantly increased bioactivity compared to when encased within the hitherto explored 3D microporous MOFs.T he improvement results from the shortened diffusion path and enlarged pore channel in 2D MSMOFs.M eanwhile,t he thin 2D MSMOF layer also can providee xcellent protection of the hosted biomacromolecules or protein-scaffolded biominerals through structural confinement.