Abstract
The angiotensin-I-converting enzyme (ACE) inhibitory activity of a tryptic digest of bovine β-lactoglobulin (β-lg) was investigated. Intact β-lg essentially did not inhibit ACE while the tryptic digest gave an 84.3% inhibition of ACE. Peptide material eluting between 20 and 25% acetonitrile during C18 solid-phase extraction of the β-lg tryptic digest inhibited ACE by 93.6%. This solid-phase extraction fraction was shown by mass spectroscopy to contain β-lg f(142-148). This peptide had an ACE IC50 value of 42.6 μmol/l. The peptide was resistant to further digestion with pepsin and was hydrolysed to a very low extent with chymotrypsin. The contribution of specific amino acid residues within the peptide to ACE inhibitory activity and the potential application of this peptide as a nutraceutical is discussed.
Original language | English (Ireland) |
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Pages (from-to) | 99-101 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 402 |
Issue number | 2-3 |
DOIs | |
Publication status | Published - 27 Jan 1997 |
Keywords
- β-Lactoglobulin
- Bioactive peptide
- Gastric digestion
- Nutraceutical
- Pancreatic digestion