Abstract
The enzymatic hydrolysis of a series of carboxylic esters by carboxylesterase NP has been investigated in order to determine the scope and limitations of this enzyme. 2‐Substituted propionates were hydrolyzed with high enantioselectivity when an aromatic moiety was part of the 2‐substituent. Enantioselective hydrolysis could be accomplished with several 2‐arylpropionates, 2‐(aryloxy)propionates and N‐arylalanine esters. The propionate esters yielded propionic acids as (S) enantiomers, whereas the alanine esters yielded the (R) enantiomers. Without a 2‐aryl substituent, the enzymatic hydrolysis of the propionates occurred at a lower rate without acceptable enantioselectivity. In addition to 2‐substituted propionates, only a few other esters were hydrolyzed with high enantioselectivity by carboxylesterase NP, such as some prochiral disubstituted malonates. 1‐Phenylethyl acetate was the only substrate with chirality in the alcohol part of the ester that was found to be hydrolyzed enantioselectively.
Carboxylesterase NP proved to be a powerful enzyme for kinetic resolution of propionate esters with an aromatic ring containing a 2‐substituent.