In Situ Enzyme Immobilization by Covalent Organic Frameworks

Abstract Enzyme immobilization is a widely reported method to favor the applicability of enzymes by enhancing their stability and re‐usability. Among the various existing solid supports and immobilization strategies, the in situ encapsulation of enzymes within crystalline porous matrices is a powerful tool to design biohybrids with a stable and protected catalytic activity. However, to date, only a few metal–organic frameworks (MOFs) and hydrogen‐bonded organic frameworks (HOFs) have been reported. Excitingly, for the first time, Y. Chen and co‐workers expanded the in situ bio ‐ encapsulation to a new class of crystalline porous materials, namely covalent organic frameworks (COFs). The enzyme@COF materials not only exhibited high enzyme loading with minimal leaching, high catalytic activity and selectivity, chemical and long‐term stability and recyclability but could also be scaled up to a few grams. Undoubtedly, this work opens new striking opportunities for enzymatic immobilization and will stimulate new research on COF‐based matrices.