Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine ß-lactoglobulin
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CitationMullally, M., Meisel, H. and FitzGerald, R. Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β-lactoglobulin. FEBS Letters, 1998, 402(2-3), 99-101. doi: https://doi.org/10.1016/S0014-5793(96)01503-7
AbstractThe 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.
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