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The influence of buffer type, co-solvent type, and acyl chain length was investigated for the enantioselective hydrolysis of racemic 4-arylbut-3-en-2-yl esters using Lecitase ™ Ultra (LU). Immobilized preparations of the Lecitase ™ Ultra enzyme had significantly higher activity and enantioselectivity than the free enzyme, particularly for 4-phenylbut-3-en-2-yl butyrate as the substrate. Moreover, the kinetic resolution with the immobilized enzyme was achieved in a much shorter time (24-48 h). Lecitase ™ Ultra, immobilized on cyanogen bromide-activated agarose, was particularly effective, producing, after 24 h of reaction time in phosphate buffer (pH 7.2) with acetone as co-solvent, both ( R )-alcohols and unreacted ( S )-esters with good to excellent enantiomeric excesses (ee 90-99%). These conditions and enzyme were also suitable for the kinetic separation of racemic ( E )-4-phenylbut-3-en-2-yl butyrate analogs containing methyl substituents on the benzene ring ( 4b , 4c ), but they did not show any enantioselectivity toward ( E )-4-(4'-methoxyphenyl)but-3-en-2-yl butyrate ( 4d ).

Free and Immobilized Lecitase™ Ultra as the Biocatalyst in the Kinetic Resolution of (E)-4-Arylbut-3-en-2-yl Esters