Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle

• Published in: Bioscience, biotechnology, and biochemistry Vol. 58; no. 12; pp. 2244 - 2245
• Main Authors: Matsufuji, H. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture), Matsui, T, Seki, E, Osajima, K, Nakashima, M, Osajima, Y
• Format: Journal Article
• Language: English
• Published: Tokyo Taylor & Francis 1994; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Amino Acid Sequence; Angiotensin-Converting Enzyme Inhibitors - isolation & purification; Angiotensin-Converting Enzyme Inhibitors - pharmacology; Animals; Biological and medical sciences; Biotechnology; Endopeptidases - chemistry; Fish and seafood industries; Fishes; Food industries; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; HYDROLYSAT DE PROTEINES; Hydrolysis; INHIBIDORES DE ENZIMAS; INHIBITEUR D'ENZYME; Molecular Sequence Data; MUSCLE; Muscles - enzymology; MUSCULOS; PEPTIDE; Peptides - isolation & purification; Peptides - pharmacology; PEPTIDOS; Peptidyl-Dipeptidase A - metabolism; PESCADO; POISSON (ALIMENT); PROTEASAS; PROTEASE; PROTEINAS HIDROLIZADAS; SARDINA; SARDINE; Sardine; Edible fish; Enzyme; Enzyme inhibitor; Biological activity; Tissue extract; Hydrolysate; Peptide fragment; Peptidyl-dipeptidase A; Hydrolases; Peptidyl-dipeptidases; Muscle; Proteinases
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.58.2244

The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastro-intestinal 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 inhabited 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