Lipases are versatile green biocatalysts from the hydrolase family, valued for their high selectivity, specificity, and catalytic efficiency in diverse industrial applications, including pharmaceuticals, food, and bioenergy. Their activity and productivity are strongly influenced by a range of physicochemical and operational factors. This review summarizes the key parameters affecting lipase performance, including temperature, pH, metal ions, nitrogen sources, surfactants, agitation speed, and incubation time. The roles of substrate-related factors-such as concentration, derivative type, substrate ratio, and enzyme loading-are also described. In addition, recent methods and emerging techniques aimed at enhancing lipase activity and reducing product losses, such as lipase engineering, immobilization, bioimprinting, interfacial imprinting, the use of conventional organic co-solvents, additives, natural deep eutectic solvents, and multi-lipase systems, are outlined. By compiling and organizing current knowledge, this work serves as a practical reference for optimizing lipase-based processes in both research and industrial contexts.
Alhakimi et al. (Fri,) studied this question.