Abstract
Eight inhibitory peptides of angiotensin I converting enzyme (ACE) were isolated from the hydrolysate of soybean broth. The amino acid sequences of these peptides identified by Edman procedure were: Val-Thr-Val-Pro-Gln, Val- Val-Phe-Asp, Gly-Glu-Leu-Phe-Glu, Ile-Thr-Pro-Leu, Gln-Val-Val-Phe, Val-Gln- Val-Val-Phe, Ile-Val-Phe-Asp-Ala and Gly-Asp-Ala-Pro-Asn. The IC50 value of these peptides for ACE from bovine lung were: 6.3, 3.9, 2.3, 5.2, 4.6, 3.4, 4.1 and 2.8 x 10-5 M, respectively. These peptides contained hydrophobic and aromatic amino acids. This characteristic, was considered to be highly related to their inhibitory effect on ACE activity.
| Translated title of the contribution | Peptides with angiotensin I converting enzyme inhibitory activity in pepsin-digests of soybean broth |
|---|---|
| Original language | Chinese (Traditional) |
| Pages (from-to) | 435-444 |
| Number of pages | 10 |
| Journal | Nutritional Sciences Journal |
| Volume | 22 |
| Issue number | 4 |
| Publication status | Published - 1997 |
Keywords
- Angiotensin I converting enzyme
- Peptide
- Soybean
- Soybean protein
ASJC Scopus subject areas
- Food Science
- Medicine (miscellaneous)