Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/256521
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Title

Angiotensin I-converting enzyme inhibitory activity of peptides derived from egg white proteins by enzymatic hydrolysis

AuthorsMiguel, Marta CSIC ORCID ; Recio, Isidra CSIC ORCID ; Gómez-Ruiz, José Ángel CSIC; Ramos González, María Mercedes CSIC ; López-Fandiño, Rosina CSIC ORCID
Issue Date1-Sep-2004
PublisherInternational Association for Food Protection
CitationJournal of Food Protection 67(9): 1914-1920 (2004)
AbstractThe hydrolysis of crude egg white with pepsin, trypsin, and chymotrypsin produced peptides with angiotensin-converting enzyme (ACE) inhibitory properties. These peptides were mainly derived from the proteolysis of ovalbumin. The most active hydrolysates were obtained after treatment with pepsin (50% inhibitory concentration [IC50], 55.3 μg/ml), with the fraction having a molecular mass lower than 3,000 Da giving the highest ACE inhibitory activity (IC50, 34.5 μg/ml). Nine subfractions were collected from the fraction with a molecular mass lower than 3,000 Da using semipreparative reversed-phase high-performance liquid chromatography. Considerable ACE inhibitory activity (IC50 < 40 μg/ml) was found in three of them. These subfractions were analyzed by reversed-phase high-performance liquid chromatography–tandem mass spectrometry, and 14 peptides were identified. These sequences were synthesized, and their ACE inhibitory activities were measured. Among the identified peptides, two novel sequences with potent ACE inhibitory activity were found. The amino acid sequences of these inhibitors were identified as Arg-Ala-Asp-His-Pro-Phe-Leu and Tyr-Ala-Glu-Glu-Arg-Tyr-Pro-Ile-Leu and showed IC50 values of 6.2 and 4.7 μM, respectively.
Publisher version (URL)https://doi.org/10.4315/0362-028X-67.9.1914
URIhttp://hdl.handle.net/10261/256521
DOI10.4315/0362-028X-67.9.1914
Identifiersdoi: 10.4315/0362-028X-67.9.1914
issn: 0362-028X
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