Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

TLDR

Chemical modification and immobilization of enzymes are typically viewed as separate strategies, yet numerous studies demonstrate that combining them can synergistically improve biocatalyst performance. This review surveys strategies that enable such synergistic coupling to enhance enzyme activity and stability. It examines how chemical modification can strengthen immobilization through reinforced adsorption or multipoint covalent attachment, improve enzyme stability and guide immobilization conditions, and how solid‑phase chemistry benefits already immobilized enzymes, while also exploring diverse modification targets such as cross‑linking, one‑point modification, and artificial microenvironments.

Abstract

Abstract Chemical modification and immobilization of enzymes have been usually considered unrelated tools to improve biocatalyst features. However, there are many examples where a chemically modified enzyme is finally used in an immobilized form, and that exemplifies how both tools may be complementary resulting in a synergism in the final results. In this review we present some of the strategies that may give that result. For example, the chemical modification of soluble enzymes may be used to improve their immobilization (reinforcing adsorption or improving multipoint covalent attachment), or just to improve enzyme stability and facilitate the selection of the immobilization conditions. Chemical modification of previously immobilized enzymes benefits from solid‐phase chemistry due to the nature of enzymes (e.g., prevention of inactivation, aggregation, etc.). The use of different targets for chemical modifications with small molecules or multifunctional polymers are also discussed: intramolecular or intersubunit cross‐linking, one‐point modification, generation of artificial microenvironments, etc.