In Situ Enzyme Immobilization by Covalent Organic Frameworks

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.

Automated summary

Enzyme immobilization is a method to enhance enzyme stability and re-usability. In this study, researchers successfully encapsulated enzymes within covalent organic frameworks, demonstrating high enzyme loading, catalytic activity, and stability.