Various enzymes such as lipases, proteases and laccases have been extracted for use in various industrial applications. However, most natural enzymes possess characteristics that make them unsuitable for the harsh conditions often associated with industrial processes. To overcome these limitations, various methods and techniques have been developed to enhance the suitability of enzymes as industrial biocatalysts, making them a viable alternative to chemical catalysts. One of the most effective approaches is enzyme immobilization, which improves enzyme properties such as thermal stability, organic solvent stability, enhanced efficiency, catalytic performance, prolonged storage, operational stability, and reusability. These improved characteristics lower manufacturing costs and provide more effective catalysts, making them essential for industrial applications. Enzyme immobilization typically involves attaching the enzyme to a solid support, and the microenvironment including the pH of the binding solution and the nature of the support often influences the immobilization rate. Immobilization techniques also play a crucial role in the success of the process. The adsorption method is being widely used due to its simplicity and minimal impact on enzyme structure. Through hydrogen bonds, ionic interactions, Van der Waals forces, and hydrophobic interactions, this method preserves the enzyme's active site, making it the preferred choice in industrial settings.
Keywords: Adsorption method; Biocatalysts; Immobilization; Molecular interactions; Thermostability.
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