With the help of highly dynamic reverse micellar media, lipase-catalyzed esterification reactions can be carried out at ambient conditions without any agitation. Having low water contents in reverse micellar media, these reversible reactions favor the esterification direction instead of the normal hydrolysis catalyzed by lipases. A proposed enzyme kinetic model has successfully predicted the reaction mechanism of lauric acid with 1,3-propanediol in reverse micellar media. However, experiments conducted showed a likelihood of substrate inhibition at higher lauric acid concentrations (>70 mM) and a strong bonding effect among 1,3-propanediol, water, and AOT head groups. The effect of water concentration in the reaction media was shown to be important. The optimal W-0’s for achieving the greatest initial reaction rate and final conversion were 9 and 4 for Candida rugosa and Rhizopus delemar, respectively. For both lipases, reverse micellar media experiments showed a lipase localization possibility.