Highly efficient enantioselective hydrolysis of short chain N-acetyl amino acid p-nitrophenyl esters catalysed by esterase models

An enantioselectivity (L/D) of 167 ± 21 (pH 7.68; ionic strength = 0.01; 298 K) has been achieved for the hydrolysis of the short chain substrate, N-acetylphenylalanine p-nitrophenyl ester in the catalytic vesicular system of Nα-(N-benzyloxycarbonyl-L-Ieucyl)-L-histidine (Z-L-Leu-L-His) and N,N-ditetradecyl-N,N-dimethylammonium bromide.