The stereochemical resolution of enantiomeric free and derivatized amino acids using and hplc chiral stationary phase based on immobilized α‐chymotrypsin: Ciral separation due to solue structure or enzyme activity

The stereochemical separation of free and derivatized amino acids on active alpha-chymotrypsin bonded to silica is governed by two mechanisms based on the structure of the solutes or on the enzymatic activity of the enzyme. The deactivation of the hydrolytically active site of the enzyme demonstrated that a significant portion of the retention on this support is due to hydrophobic interactions at other sites. These sites appear to be stereoselective for the ester derivatives of amino acids but not for the other studied solutes.