Bilal_2021_Int.J.Biol.Macromol__

Lipases belong to alpha/beta hydrolases that cause hydrolytic catalysis of triacylglycerols to release monoacylglycerols, diacylglycerols, and glycerol with free fatty acids. Lipases have a common active site that contains three amino acid residues in a conserved Gly-X-Ser-X-Gly motif: a nucleophilic serine residue, an acidic aspartic or glutamic acid residue, and a basic histidine residue. Lipase plays a significant role in numerous industrial and biotechnological processes, including paper, food, oleochemical and pharmaceutical applications. However, its instability and aqueous solubility make application expensive and relatively challenging. Immobilization has been considered as a promising approach to improve enzyme stability, reusability, and survival under extreme temperature and pH environments. Innumerable supporting material in the form of natural polymers and nanostructured materials is a crucial aspect in the procedure of lipase immobilization used to afford biocompatibility, stability in physio-chemical belongings, and profuse binding positions for enzymes. This review outlines the unique structural and functional properties of a large number of polymers and nanomaterials as robust support matrices for lipase immobilization. Given these supporting materials, the applications of immobilized lipases in different industries, such as biodiesel production, polymer synthesis, additives, detergent, textile, and food industry are also discussed.