Synthesis of enantiomerically pure glycidol via a fully enantioselective lipase-catalyzed resolution

Abstract

The efficient enzymatic synthesis of enantiopure 2,3-epoxypropanol (glycidol) has been achieved. The racemic glycidyl butyrate was successfully resolved by enzymatic hydrolysis using a strategy that combines different immobilization protocols and different experimental reaction conditions. A new enzyme (25 kDa lipase)—which is a lipase-like enzyme purified from the pancreatic porcine lipase (PPL) extract—immobilized on DEAE–Sepharose was selected as the optimal biocatalyst. The optimal results were obtained at pH 7, 25 °C and 10% dioxane using this biocatalyst and a very high enantioselectivity for the enzyme was displayed, obtaining both ( R)-(−)-glycidyl butyrate and ( R)-(+)-glycidol with enantiomeric excesses >99% ( E >100). The hydrolysis of ( R)-(−)-glycidyl butyrate produced pure ( S)-(−)-glycidol.