In Situ Enzyme Immobilization by Covalent Organic Frameworks

Sicard, C

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.

Keywords: Bio-Immobilization; Biocatalysis; Covalent Organic Frameworks; Enzyme; Porous Solid

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Covalent Organic Framework (COF) Materials

In situ enzyme immobilization of covalent organic frameworks (COFs) is an innovative biocatalytic technology. COF is a crystalline material composed of organic monomers connected by covalent bonds and has a highly ordered pore structure. In in situ enzyme immobilization, the surface of the COF is designed to interact with the enzyme and immobilize the enzyme molecules through covalent bonds or other specific chemical bonds. This approach takes advantage of the highly structured and tunable nature of COFs, allowing enzymes to be efficiently localized and stabilized within or on their surface. This helps improve the catalytic activity and stability of the enzyme, thereby enhancing the efficiency of the biocatalytic process. In addition, the pore structure of COF can also provide additional reaction sites to optimize the interaction between substrate and enzyme. In situ enzyme immobilization of COF has broad application prospects in the fields of biocatalysis, biosensing, and biopharmaceuticals. This technology provides a promising approach to the development of efficient and sustainable biocatalytic processes and opens new possibilities for customized catalytic systems. In the future, with an in-depth understanding of COF materials and biocatalytic mechanisms, more breakthroughs are expected in this field.