ANGIOTENSIN I-CONVERTING ENZYME-INHIBITORY PEPTIDES IN AN ALKALINE PROTEASE HYDROLYZATE DERIVED FROM SARDINE MUSCLE

The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC50 = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100 mu M of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 mu M). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des Asp[1]-angiotensin I.