A new extracellular lipase (Lip2p) from the yeast Yarrowia lipolytica was used for the resolution of 2-bromo-arylacetic acid esters, an important class of chemical intermediates for the pharmaceutical industry. Its efficiency for the transesterification of racemic mixtures with 1-octanol in n-octane was compared with the most efficient lipases described to date, lipases from Burkholderia cepacia and Rhizomucor miehei. Resolution of 2-bromo-p-tolylacetic acid ethyl ester catalyzed by Y. lipolytica lipase showed an enantiopreference of 28, almost equal to that obtained with B. cepacia lipase (E = 30). Moreover, Y. lipolytica lipase presents a higher catalytic activity and an (S)-enantiopreference, while B. cepacia lipase is (R)-enantiomer selective. The most interesting result is that Y. lipolytica lipase has until now been the only enzyme able to catalyze the resolution of 2-bromo-o-tolylacetic acid ethyl ester (E = 27).