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Lipase A is an enzyme from Candida antarctica strain isolated from Lake vanda in Antarctica. The gene coding for Lipase A is CALA gene. Lipase A is the most thermostable lipase known and is used as a biocatalyst in food and pharmaceutical industry. Lipases (triacylglycerol acylhydrolases EC 126.96.36.199) are ubiquitous enzymes of considerable physiological significance and industrial potential. Lipases catalyze the hydrolysis of triacylglycerols to glycerol and free fatty acids. Lipases are serine hydrolases. Lipases display little activity in aqueous solutions containing soluble substrates.
Lipase A gene was from Candida antarctica was amplified using gene specific primers Xho1 restriction site. The gene was cloned unidirectionally into Xho1 site in pKLAC2 vector. pKLAC2 with lipase A gene insert was transformed into E.Coli TOP 10F’ strain and the transformed colonies were screened for positive transformants. Future prospects involve expressing lipase A gene in Kluveromyces lactis expression system and conducting expression studies in a fermenter.