ABSTRACT
Lipases can catalyze other reactions, including acyl exchange and acyl transfer, and may catalyze the hydrolysis of a range of different carboxylate esters. Therefore, the distinction between lipases and other members of the carboxylic ester hydrolase family (EC 3.1.1) is not always clear. In kinetic terms, it was shown that an esterase enzyme (e.g., horse liver esterase) was active only against monomeric substrates, while the activity of a lipase (e.g., porcine pancreatic lipase) was significantly enhanced when the substrate was increased above its solubility limit [1], although this generalization did not always apply when tested across a range of lipases and esterases [2]. Instead, a more classical definition was suggested, whereby esterases are enzymes that act on watersoluble neutral esters and lipases act on water-insoluble neutral esters [2]. Lipases are, therefore, a special group of esterases that are active predominantly at a lipid-water interface.
