Abstract
Immobilization techniques are generally based on reusing enzymes in industrial applications to reduce costs and improve enzyme properties. These techniques have been developing for decades, and many methods for immobilizing enzymes have been designed. To find a better immobilization method, it is necessary to review the recently developed methods and have a clear overview of the advantages and limitations of each method. This review introduces the recently reported immobilization methods and discusses the improvements in enzyme properties by different methods. Among the techniques to improve enzyme properties, metal–organic frameworks, which have diverse structures, abundant organic ligands and metal nodes, offer a promising platform.
Highlights
Enzymes are biological macromolecules that are generally globular proteins [1]
We have summarized recent immobilization techniques, including adsorption, covalent bonding- and Metal–organic frameworks (MOFs)-based immobilization
Adsorption techniques based on van der Waals interactions and covalent bonding methods through covalent conjugation, which further affect the structure and substrate binding properties, may result in improvements in substrate selectivity
Summary
Enzymes are biological macromolecules that are generally globular proteins [1]. They are known to catalyze numerous chemical reactions [2,3] and are widely used in different areas, such as the food, agricultural, cosmetic and pharmaceutical industries [4]. The reusability or stability of enzymes used in industrial applications are key factors in reducing costs. To achieve this objective, immobilization techniques have been used for decades. We provide an update on studies from the past five years and discuss improvements in enzyme properties and the limitation of the application of immobilization
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