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 journalArticle

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

Fingerprint

valyltyrosine
enzyme inhibitors
peptidyl-dipeptidase A
sardines
Angiotensin-Converting Enzyme Inhibitors
Peptide Hydrolases
proteinases
peptides
dipeptides
Dipeptides
Peptides
Enzyme activity
Peptidyl-Dipeptidase A
digestion
Digestion
peptidases
Blood pressure
mucosa
blood pressure
Mucous Membrane

All Science Journal Classification (ASJC) codes

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

Cite this

Val-tyr, an Angiotensin I Converting Enzyme Inhibitor from Sardines that have Resistance to Gastrointestinal Proteases. / Seki, Eiji; Osajima, Katsuhiro; Matsufuji, Hiroshi; Matsui, Toshiro; Osajima, Yutaka.

In: Nippon Nogeikagaku Kaishi, Vol. 69, No. 8, 01.01.1995, p. 1013-1020.

Research output: Contribution to journalArticle

Seki, Eiji ; Osajima, Katsuhiro ; Matsufuji, Hiroshi ; Matsui, Toshiro ; Osajima, Yutaka. / Val-tyr, an Angiotensin I Converting Enzyme Inhibitor from Sardines that have Resistance to Gastrointestinal Proteases. In: Nippon Nogeikagaku Kaishi. 1995 ; Vol. 69, No. 8. pp. 1013-1020.
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N2 - 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.

AB - 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.

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