Review examines enzyme immobilization's role in enhancing stability and performance across various applications, suggesting significant advancements.
Enzyme immobilization serves as a pivotal strategy for enhancing enzymatic stability, reusability, and operational performance, demonstrating significant potential across diverse fields including biocatalysis, biosensing, food processing, environmental remediation, and biomedicine. This review systematically examines recent advances in enzyme immobilization, with a focus on advanced carrier platforms such as covalent organic frameworks (COFs), metal‐organic frameworks (MOFs), natural and synthetic polymers, silica materials, magnetic materials, carbon materials, and corresponding composite materials. These materials provide robust support for constructing high‐performance and multifunctional immobilized enzyme systems, as their tunable porosity, rich surface chemistry, excellent biocompatibility, and unique physicochemical properties. The review critically analyzes how various immobilization strategies, such as covalent bonding, physical adsorption, coprecipitation, and encapsulation, regulate enzymatic activity, stability, and selectivity. Moreover, the characteristics of these enzyme immobilization systems such as loading capacity, operational conditions and recyclability are summarized. It highlights the remarkable performance of these systems in applications spanning chiral synthesis, sensitive biosensing, pollutant degradation, drug delivery, food and beverage processing and continuous‐flow bioprocessing. Finally, the review summarizes the current research landscape and highlights the most promising innovative prospects in this rapidly evolving field of enzyme immobilization.
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Wang et al. (2026) studied this question.
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