Bacterial lipases play an important role in biotechnology-based industries as hydrolases for detergent additives, as synthases catalyzing kinetic resolution of racemic compounds and for performing esteriWcation reactions. Amongst bacteria very few extra-cellular lipases have been isolated, characterized, and studied for their activities in aqueous or organic media. Amongst Bacillus spp., B. coagulans NCIMB 9365 and B. circulans possess intracellular lipases while a recently reported thermophilic B. coagulans BTS-3 isolate possessed an extra-cellular (31 kDa) alkalophilic lipase. In contrast, lipase with very high molecular weight (112 kDa) has been reported from a mesophilic Bacillus sp.. Thermostable lipases from many Bacillus species have been found to possess a molecular mass of 43–45 kDa . Recently, a 62-kDa lipase from Geotrichum marinum has been reported. To exploit lipases of Bacillus spp. for performing hydrolysis reaction in aqueous or esteriWcation and trans-esteriWcation reactions in organic system(s), respectively, it is important to biochemically characterize these enzymes. Most of these lipases were not studied for their applications in organic synthesis