Porcine pancreas lipase: a versatile biocatalyst.

Abstract

Porcine pancreatic lipase, a 1, 3-regioselective lipase, is one of the most widely used biocatalyst in academic as well as industrial processes. This lipase showed remarkable catalytic performance, often outclassed other types of lipases in producing valuable products through varieties of reactions. During hydrolysis of vegetable oil to fatty acid, mono and diacylglycerol, porcine pancreas lipase outclassed Candia rugosa and Thermomyces lanuginosus lipase. Porcine pancreas lipase efficiently catalyzed transesterification of vegetable oil to biodiesel as well. This lipase catalyzed esterification of organic acid and alcohol, glycerol and fatty acid, sugar and fatty acid resulting in organic ester, monoacylglycerol and sugar and fatty acid ester, respectively; outperformed Candia rugosa and Rhizopus niveus lipase. Porcine pancreas lipase manifested catalytic promiscuity by conversion of 4-hydroxycoumarin and aromatic aldehyde to Bis-4-hydroxycoumarin through Knoevenagel condensation; of aromatic or heteroaromatic aldehyde and ketone to aldol through aldol condensation. It outweighed lipases from Aspergillus niger, Pesudomonas fluorescens and Candia rugosa during Michael addition between 4-hydroxycoumarin and α, β-unsaturated enones to warfarin. It outperformed Mucor javanicus lipase during cascade reaction involving aldehyde and indole to Bis(indolyl)alkanes; and Candida cylindracea lipase during enantioselective acylation between amino alcohol and acetate ester to amide and amido-ester. This lipase also catalyzed multicomponent synthesis leading to Pyrido[2,3-d]pyrimidine derivatives from aromatic aldehyde, malononitrile and 6-amino-1,3-dimethyl uracil. This lipase has potential application value as it could catalyze these reactions under milder conditions.