Val-tyr, an Angiotensin I Converting Enzyme Inhibitor from Sardines that have Resistance to Gastrointestinal Proteases

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

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

Abstract

The NH2-terminal residue of a dipeptide is an important determinant of the resistance to peptidases of porcine small mucosa. NH2-terminal Val or Ile, and COOH-terminal Trp or Tyr dipeptides had higher angiotensin I converting enzyme(ACE)inhibitory activity and digestive resistance than other dipeptides. We defined Val-Tyr as a main inhibitor in alkaline protease hydrolyzates from sardines. Attempts to isolate and measurement of Val-Tyr were done from the short chain peptides that reduced blood pressure. The content of Val-Tyr was 51 mg per 100 g of the short chain peptides, represented 1.3% of the total ACE inhibitory activity of the short chain peptides. Isolated Val-Tyr was resistant to gastrointestinal proteases. The primary structures of fragments formed from Arg-Val-Tyr by digestive proteases were considerably different, and it was confirmed that the main peptide, Val-Tyr, was formed by intestinal proteases after digestion. The content of Val-Tyr formed from the short chain peptides by intestinal proteases after digestion was less than 10 percent of the original.

Original languageEnglish
Pages (from-to)1013-1020
Number of pages8
JournalNippon Nogeikagaku Kaishi
Volume69
Issue number8
DOIs
Publication statusPublished - Jan 1 1995

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Chemistry (miscellaneous)
  • Medicine (miscellaneous)

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