Dependence of the synthetic activity of nine immobilized lipases on water activity

The advantages of carrying out enzymatic syntheses in organic media with water activity, a(w), control are now well recognized and a number of techniques for accomplishing this have been described in the literature. Recently, many of these ideas have been extended to allow the continuous control of water activity in reactor designs suitable for scaleup. For the proper design and operation of such devices, it is essential to have some knowledge regarding the water activity behavior of enzyme preparations suitable for use with them. This article describes the a(w) profiles of nine different lipases, adsorbed on a microporous polypropylene support, used for the synthesis of dodecyl decanoate from a solution of the corresponding acid and alcohol in hexane.