Abstract
Lipases have large differences with respect to the source (animal, plant or microbial cells) and the cheapest preparation commercially available is isolated from porcine pancreas. Although it has been used to lesser extent when comparing with microbial lipases, porcine pancreatic lipase (PPL) has high stability and activity in anhydrous media as demonstrated in esterification and transesterification reactions. In addition, studies have recommended the utilization of this lipase preparation for synthetic applications in which stereoselectivity and cost are considered to be critical factors. Therefore, there is a growing interest in applying PPL to produce not only fine chemicals but also commodities. This review focuses on the isolation and purification, structural features, and biochemical properties of PPL. Immobilization techniques which improve its catalytic activity, storage, operational, and thermal-stability properties are briefly discussed. This review also describes the extensive biotechnological applications for PPL.
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