Journal of Biotechnology, 26 (1992) 111-142 © 1992 Elsevier Science Publishers B.V. All rights reserved 0168-1656/92/$05.00 111 BIOTEC 00791 Minireview Purification of lipases M.A. Taipa, M.R. Aires-Barros and J.M.S. Cabral Laborat6rio de Engenharia Bioqu{mica, Instituto Superior T&nico, Lisboa, Portugal (Received 9 September 1991; revision accepted 17 March 1992) Summary Interest on lipases from different sources (microorganisms, animals and plants) has markedly increased in the last decade due to the potential applications of lipases in industry and in medicine. Microbial and mammalian lipases have been purified to homogeneity, allowing the successful determination of their primary aminoacid sequence and, more recently, of the three-dimensional structure. The X-ray studies of pure lipases will enable the establishment of the structure-func- tion relationships and contribute for a better understanding of the kinetic mecha- nisms of lipase action on hydrolysis, synthesis and group exchange of esters. This article reviews the separation and purification techniques that were used in the recovery of microbial, mammalian and plant lipases. Several purification proce- dures are analysed taking into account the sequence of the methods and the number of times each method is used. Novel purification methods based on liquid-liquid extraction, membrane processes and immunopurification are also reviewed. Lipase; Purification Introduction Lipases (triacylglycerol hydrolase, EC 3.1.1.3) are enzymes widely distributed among animals, plants and microorganisms that catalyze the hydrolysis of glycerol- ester bonds at fat water interfaces. In anhydrous water-immiscible organic solvents they are also able to catalyze the reverse reactions of synthesis and group exchange Correspondence to: M.A. Taipa, Laborat6rio de Engenharia Bioquimica, Instituto Superior T6cnico, 1000 Lisboa, Portugal.