Majumder_2025_Arch.Microbiol_207_166

Lipases play a pivotal role in biocatalysis, particularly in industrial and pharmaceutical applications, due to their exceptional regio- and enantioselectivity. However, their inherent limitations, including low stability, substrate specificity constraints, and suboptimal catalytic efficiency, hinder broader utilization. Genetic modifications have emerged as a powerful strategy to enhance lipase performance, offering significant improvements in enzyme activity, thermal stability, and substrate adaptability. This study presents a comprehensive investigation into the molecular engineering of lipases, leveraging site-directed mutagenesis and computational modelling to optimize structural and functional attributes. Key advancements in protein engineering, including rational design and directed evolution, are explored to elucidate their impact on catalytic efficiency and industrial viability. Experimental validation confirms that the genetically modified lipases exhibit superior stability under extreme pH and temperature conditions, along with enhanced catalytic turnover rates. Comparative analyses with wild-type enzymes underscore the potential of engineered lipases in diverse biotechnological applications, ranging from biofuel synthesis to pharmaceutical drug development. Furthermore, the study examines the mechanistic insights underlying these modifications, offering a theoretical framework for future enzyme engineering efforts. The findings underscore the transformative potential of genetically enhanced lipases in industrial biotechnology, paving the way for more sustainable and cost-effective biocatalytic processes. Future research should focus on integrating machine learning and advanced computational tools to further refine enzyme optimization strategies.