Purification of angiotensin converting enzyme inhibitory peptides from sunflower protein hydrolysates by reverse-phase chromatography following affinity purification

The purification of a peptidic fraction with angiotensin converting enzyme (ACE) inhibitory activity from sunflower protein hydrolysates by affinity chromatography was recently described. We now describe that reverse-phase HPLC fractionation of this product yields several fractions with IC50 one order of magnitude higher than those previously purified by reverse-phase HPLC following gel filtration chromatography, showing that affinity chromatography is much more effective than gel filtration chromatography as a first step for purification of ACE inhibitory peptides. The amino acid composition of these fractions is presented, but attempts to determine their amino acid sequence failed, showing that these fractions contained more than one peptide.