ABSTRACT
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 and a few plant and animal sources have been purified to homogeneity. This has enabled their successful sequence determination and their three-dimensional structure leading to a better 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 bacterial, 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 will prove to be of immense help while planning lipase purification. Novel purification technologies now available in this field are also reviewed.
