• ACE inhibitory peptide;
  • hypertension;
  • wheat germ hydrolyzate;
  • alkaline protease


Reported is the preparation of wheat germ (WG) hydrolyzate with potent angiotensin I-converting enzyme (ACE) inhibitory activity, and the characterization of peptides responsible for ACE inhibition. Successful hydrolyzate with the most potent ACE inhibitory activity was obtained by 0.5 wt.%–8 h Bacillus licheniformis alkaline protease hydrolysis after 3.0 wt.%–3 h α-amylase treatment of defatted WG (IC50; 0.37 mg protein ml−1). The activity of WG hydrolyzate was markedly increased by ODS and subsequent AG50W purifications (IC50; 0.018 mg protein ml−1). As a result of isolations by high performance liquid chromatographies, 16 peptides with the IC50 value of less than 20 μm, composed of 2–7 amino acid residues were identified from the WG hydrolyzate. Judging from the high content (260 mg in 100 g of AG50W fraction) and powerful ACE inhibitory activity (IC50; 0.48 μm), Ile-Val-Tyr was identified as a main contributor to the ACE inhibition of the hydrolyzate. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd.