Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle

Hiroshi Matsufuji, Toshiro Matsui, Masatoshi Nakashima, Yutaka Osajima, Eiji Seki, Katsuhiro Osajima

Research output: Contribution to journalArticle

213 Citations (Scopus)

Abstract

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 100μM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 μm). 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[l]-angiotensin I.

Original languageEnglish
Pages (from-to)2244-2245
Number of pages2
JournalBioscience, biotechnology, and biochemistry
Volume58
Issue number12
DOIs
Publication statusPublished - Jan 1 1994

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle'. Together they form a unique fingerprint.

  • Cite this