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

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.