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 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...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1994, Vol.58 (12), p.2244-2245
Main Authors: Matsufuji, H. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture), Matsui, T, Seki, E, Osajima, K, Nakashima, M, Osajima, Y
Format: Article
Language:English
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
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Summary: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
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.58.2244