Lipases (EC 3.1.1.3) belong to the serine hydrolase family that act on carboxylic ester bonds and their natural function is to hydrolyze TAGs in diglycerides (DAG), monoglycerides (MAG), fatty acids (FA) and glycerol. Lipases primarily act at the water-oil interface with a kinetic model that involves two distinctive equilibria: the first equilibrium implicates a reversible adsorption of the enzymes to the interface, the second equilibrium involves the formation of an enzyme-substrate complex and it is characterized by a typical Michaelis-Menten kinetic (Verger, et al., 1973; Verger and Haas, 1976). Lipases also catalyze other reactions in addition to hydrolysis such as esterification and transesterification with high enantioselectivity and regioselectivity on TAGs and other substrates also in unconventional media. In light of these features, commercially produced microbial lipases find applications in various industrial processes.