Laccase Immobilization on Copper-Magnetic Nanoparticles for Efficient Bisphenol Degradation

Abstract

The industrial applications of enzymes are primarily limited by their low stability, substrate or solvent tolerance, and reusability. Various strategies, such as enzyme engineering and immobilization, have been adopted to improve stability Despite the immense effort required in protein engineering, the results are undesirable and lead to only minor gains in enzyme stability Through immobilization, enzymes can enhance catalytic activity, stability, and reusability Several approaches for industrial enzyme immobilization have been reported, such as encapsulation within polymeric materials or metal-protein hybrids [5], adsorption on solid supports or membranes The additional treatment of glutaraldehyde on immobilized enzymes is beneficial to stabilize enzymes on solid supports, minimizing leaching and improving the structural stability of encapsulated enzymes Enzyme properties, such as residual activity, substrate specificity, and catalytic parameters, including turnover number, V max and K m , pH, temperature profiles, stability (storage, room temperature, or thermal), and reusability highly vary among the different immobilization procedures However, the selection of suitable approaches is essential for the successful immobilization of industrial enzymes. During adsorption, enzymes are attached to supports by weak bonds, such as van der Waals, hydrophobic, or ionic interactions In contrast, covalent procedures involve strong bonds, such as covalent interactions between support surfaces containing functional groups and various amino acids of the enzyme In addition, covalent methods more effectively minimize leaching, which is primarily associated with the adsorption of enzymes on the support surface The support capacity for maximum enzyme loading is also a crucial parameter determining the effectiveness of immobilization procedures. The amount of enzyme immobilized is essentially altered by support assets, such as morphology, functional groups on their surface, surface area, and porosity, as well as enzyme properties, such as the size and number of groups involved in binding hydrophilic or hydrophobic behaviors

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