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 language | English |
|---|---|
| Pages (from-to) | 1013-1020 |
| Number of pages | 8 |
| Journal | Nippon Nogeikagaku Kaishi |
| Volume | 69 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Jan 1 1995 |
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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 journal › Article
}
TY - JOUR
T1 - Val-tyr, an Angiotensin I Converting Enzyme Inhibitor from Sardines that have Resistance to Gastrointestinal Proteases
AU - Seki, Eiji
AU - Osajima, Katsuhiro
AU - Matsufuji, Hiroshi
AU - Matsui, Toshiro
AU - Osajima, Yutaka
PY - 1995/1/1
Y1 - 1995/1/1
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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U2 - 10.1271/nogeikagaku1924.69.1013
DO - 10.1271/nogeikagaku1924.69.1013
M3 - Article
AN - SCOPUS:85010481102
VL - 69
SP - 1013
EP - 1020
JO - Nippon Nogeikagaku Kaishi
JF - Nippon Nogeikagaku Kaishi
SN - 0002-1407
IS - 8
ER -