*Corresponding author; E-mail: rksaxena@bol.net.in, rksmicro@hotmail.com, rksmicro@yahoo.co.in. Tel: 91(11)26886559, 91(11)24678876, Extn.169. Fax: 91(11)26885270, 91(11)26886427.
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Microbial lipases today occupy a place of prominence among biocatalysts owing to their ability to catalyze a wide variety of reactions in aqueous and non-aqueous media. The chemo-, regio- and enantio-specific behaviour of these enzymes has caused tremendous interest among scientists and industrialists. Lipases from a large number of bacterial, fungal, plant and animal sources have been purified to homogeneity. This has enabled the determination of their sequence and three dimensional structure, which has provided an understanding of their unique structure-function relationships during various hydrolytic and synthetic reactions. This article presents a critical review of different strategies, which have been employed for the purification of yeast and fungal lipases. Since protein purification is normally done in a series of sequential steps involving a combination of different techniques, the effect of sequence of steps and the number of times each step is used is analyzed. This has proved to be of immense help while planning enzyme purification from yeast and fungal sources.
Lipases, immuno-purification, aqueous two phase purification, fungi, yeast
