Application of Lecitase® Ultra-Catalyzed Hydrolysis to the Kinetic Resolution of (E)-4-phenylbut-3-en-2-yl Esters

The possibility of using Lecitase (R) Ultra as a novel alternative biocatalyst for the kinetic resolution of model racemic allyl esters of (E)-4-phenylbut-3-en-3-ol: Acetate (4a) and propionate (4b) through their enantioselective hydrolysis was investigated. Reaction afforded (+)-(R)-alcohol (3) and unreacted ( -)-(S)-ester (4a or 4b). Hydrolysis of propionate 4b proceeded with higher enantioselectivity than acetate 4a. (R)-Alcohol (3) with highest enantiomeric excess (93-99%) was obtained at 20-30 degrees C by hydrolysis of propionate 4b, while the highest optical purity of unreacted substrate was observed for (S)-acetate 4a (ee = 34-56%). The highest enantioselectivity was found for the hydrolysis of propionate 4b catalyzed at 30 degrees C (E = 38). Reaction carried out at 40 degrees C significantly lowered enantiomeric excess of produced alcohol 3 and enantioselectivity in resolution. Lecitase (R) Ultra catalyzed the enantioselective hydrolysis of allyl esters 4a,b according to Kazlauskas' rule to produce (R)-alcohol 3 and can find application as a novel biocatalyst in the processes of kinetic resolution of racemic allyl esters.