Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic digest of bovine b-lactoglobulin

Richard Fitzgerald, Margaret M. Mullally, Hans Meisel

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (Ireland)
Pages (from-to)99-101
Number of pages3
JournalFEBS Letters
Volume402
Issue number2-3
DOIs
Publication statusPublished - 27 Jan 1997

Keywords

  • β-Lactoglobulin
  • Bioactive peptide
  • Gastric digestion
  • Nutraceutical
  • Pancreatic digestion

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