Abstract
The enzymatic resolutions of two racemic ethyl hydroxyalkane(P-phenyl)phosphinates were performed by both esterification and hydrolysis approaches. The first reaction was performed in anhydrous diisopropyl ether with triethylamine or pyridine as additives by using lipases from three different sources (Candida cylindracea, Aspergillus niger, and Mucor javanicus). The increase in enantioselectivity was observed when NEt3 was applied. The second reaction—lipase-catalysed hydrolysis of ethyl butyryloxyalkane(P-phenyl)phosphinates—was carried out by Candida cylindracea lipase in diisopropyl ether saturated with water or in aqueous solutions containing MgCl2, LiCl, or Triton X-100. The usefulness of biphasic systems consisting of diisopropyl ether and water or aqueous solution of MgCl2, LiCl, or Triton X-100 also were tested. The use of biphasic system in the presence of Triton X-100 resulted in the higher conversion of the substrates.