The enzymatic hydrolyses of a variety of alpha-substituted mandelic and lactic esters using pig liver esterase (PLE) have been investigated. High to moderate enantioselectivity was found for various alpha-substituted mandelic esters, whereas PLE showed low to no enantioselectivity for alpha-substituted lactic esters. We observed that the enantioselectivity of PLE depends strongly on the length and nature of the substituent at the alpha-position. Some consequences for an active site model of PLE are discussed.
|Nummer van het tijdschrift||7|
|Status||Published - 1991|