Structural characterization of peroxyl radical oxidative products of antioxidant peptides from hydrolyzed proteins
This work aimed to characterize oxidative products of five unique antioxidant peptides (P1: YFDEQNEQFR, P2: GQLLIVPQ, P3: SPFWNINAH, P4: NINAHSVVY, P5: RALPIDVL) from hydrolyzed oat proteins. Peptides were reacted with 2,2′-Azobis(2-amidinopropane) dihydrochloride, a common peroxyl radical generator...
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Published in | Heliyon Vol. 10; no. 9; p. e30588 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
15.05.2024
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | This work aimed to characterize oxidative products of five unique antioxidant peptides (P1: YFDEQNEQFR, P2: GQLLIVPQ, P3: SPFWNINAH, P4: NINAHSVVY, P5: RALPIDVL) from hydrolyzed oat proteins. Peptides were reacted with 2,2′-Azobis(2-amidinopropane) dihydrochloride, a common peroxyl radical generator. Chromatographic data showed that peptide P3 was the most oxidized (67 ± 4 %) while also displaying the most ability to scavenge radicals in the oxygen absorbance capacity assay (ORAC) with an activity of 2.16 ± 0.09 μM Trolox equivalents/μM peptide. Structural characterization using mass spectrometry showed the presence of four oxidative products of P3, three of which were mono-oxygenated and the fourth di-oxygenated. The identification of these oxidative products is new and provides an opportunity to investigate their biological function. A good correlation (r = 0.889) between the degree of oxidation and the ORAC data, demonstrates the usefulness of using oxidative peptide data to predict their radical scavenging activities. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2405-8440 2405-8440 |
DOI: | 10.1016/j.heliyon.2024.e30588 |