Enantioselective Transesterification of Allyl Alcohols with (E)-4-Arylbut-3-en-2-ol Motif by Immobilized Lecitase™ Ultra

Abstract

Lecitase™ Ultra was immobilized on four different supports and tested for the first time as the biocatalyst in the kinetic resolution of racemic allyl alcohols with the (E)-4-arylbut-3-en-2-ol system in the process of transesterification. The most effective biocatalyst turned out to be the enzyme immobilized on agarose activated with cyanogen bromide (LU-CNBr). The best results (E > 200, ees and eep = 95–99%) were obtained for (E)-4-phenylbut-3-en-2-ol and its analog with a 2,5-dimethylphenyl ring whereas the lowest ee of kinetic resolution products (90%) was achieved for the substrate with a 4-methoxyphenyl substituent. For all substrates, (R)-enantiomers were esterified faster than their (S)-antipodes. The results showed that LU-CNBr is a versatile biocatalyst, showing high activity and enantioselectivity in a wide range of organic solvents in the presence of commonly used acyl donors. High operational stability of LU-CNBr allows it to be reused in three subsequent reaction cycles without negative effects on the efficiency and enantioselectivity of transesterification. This biocatalyst can become attractive to the commercial lipases in the process of the kinetic resolution of allyl alcohols.