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Identification of a novel angiotensin‐I‐converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β‐lactoglobulin
Author(s) -
Mullally Margaret M,
Meisel Hans,
FitzGerald Richard J
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01503-7
Subject(s) - chemistry , peptide , pepsin , trypsin , chymotrypsin , chromatography , biochemistry , enzyme , proteolysis , angiotensin converting enzyme , biology , endocrinology , blood pressure
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 C 18 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 IC 50 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.