Xu_2025_Int.J.Biol.Macromol_302_140486

With the rapid development of industrialization and modern science, lipase has garnered pervasive attention. Lipases (EC 3.1.1.3) are enzymes exhibiting strong substrate specificity, high stereoselectivity, and solvent stability, which renders them a crucial biocatalyst. However, natural lipases often cannot meet the requirements of application and research in terms of activity, enantioselectivity, or thermal stability. With the continuous advancement of genetic engineering and protein engineering technologies, exploring efficient enzyme molecular modification techniques is a major task of enzyme engineering. We here review the current research status and progress of molecular modification techniques for lipases, including directed evolution, rational design, semi-rational design, and immobilization. Additionally, this article analyses lipase application prospects in food processing, environment, medical and pharmaceutical, cosmetics, and other fields. This article provides comprehensive information for the molecular modification and application research of lipases and contributes to providing reference for researchers in relevant fields.