ABSTRACT
Introduction Lipases (E.C.3.1.1.3) catalyze the hydrolysis of ester linkages in long-chain triacylglycerols with concomitant release of the constituent acid and alcohol moieties. ey act at the interface between an insoluble substrate phase and an aqueous phase in which the enzyme is dissolved. Lipases are ubiquitously produced by plants (Bhardwaj et al. 2001), animals (Carriere et al. 1994) and microorganisms (Olempska-Beer et al. 2006). Microbial lipases are the preferred potent sources due to several industrial potentials (Hasan et al. 2006). e world market for lipases has been estimated at approximately US $20 million of the industrial enzyme market (Rahman et al. 2005). Lipases have been intensively investigated for their multiplexity of catalysis with unique specicities (Villeneuve and Foglia, 1997), which have multifold applications in oleochemistry, organic synthesis, detergent formulations and nutrition (Saxena et al. 2003). Also, lipases display useful properties related to their stability as organic solvent-tolerant (Rahman et al. 2005) and thermostable (Li and Zhang, 2005) enzymes. erefore, microbial lipases have been of recent research interests and a number of lipases have been identied, puried and characterized to date.
