PLE catalyzed hydrolyses of α-substituted α-hydroxy esters: The influence of the substituents
The enzymatic hydrolyses of a variety of α-substituted mandelic and lactic esters using pig liver esterase (PLE) have been investigated. High to moderate enantioselectivity was found for various α-substituted mandelic esters, whereas PLE showed low to no enantioselectivity for α-substituted lactic esters. We observed that the enantioselectivity of PLE depends strongly on the length and nature of the substituent at the α-position. Some sequences for an active site model of PLE are discussed.