Lipases (triacylglycerol hydrolase, EC 3.1.1.3.) are en­zymes that catalyze the breakdown of carboxylic ester link in the triacylglycerol molecule to form FFAs, di — and monoglycerides and glycerol. Although their pur­pose is to catalyze hydrolysis of ester links, they can also catalyze the esterification, the conception of this link between alcohol hydroxyl groups and carboxyl groups of carboxylic acids. Therefore, they can catalyze hydrolysis, alcoholysis, esterification and transesterifi­cation and they have a wide spectrum of biotechnolog­ical applications (Kirk et al., 2002). Lipases are also highly specific as regio, chemo and enantioselective cat­alysts. Thanks to protein engineering, it is possible to enhance catalytic potential of lipases and "tailor" them to exact application and process situation, enabling further expansion of their industrial applications (B van Beilen and Li, 2002). Among lipases from animal, plant and microbial origins, the most commonly used are microbial lipases. They have abundant advantages over lipases from animal and plant sources. Using mi­crobes it is possible to achieve a higher yield of enzymes, and to genetically control the strain in obtaining a low — cost lipase with preferred properties for the conversion of fats and oils into biodiesel. In addition, the enzymatic yield is independent of potential seasonal variations and it is possible to achieve rapid growth of microbes in low — cost media (Gupta et al., 2004).