Antioxidant and Calcium Binding Activities of Hydrolyzed Oat Bran Proteins and Chromatographic Fractions
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Interest in peptides as bioactive agents has gained attention. Oats are a source of dietary fibers and phenols with demonstrated health benefits. However peptides have received little attention. In this research, oat bran treated with viscozyme and digested with protamex. The hydrolysates separated on RP-HPLC to eight fractions. The fractions were assayed for their ability to scavenge radicals, chelate metals, inhibit peroxide and bind calcium. In ORAC assay, F7 had the highest peroxyl quenching activity compared to OPH and other fractions. In the superoxide radical assay F3 and F6-F8 had higher activities while in the hydroxyl radical assay, F4, F7, F8 were the highest (14-16%).In the metal chelation assay F1 and OPH had the best iron chelating in comparison to the RP-HPLC derived peptides (1.22–22.8%). The calcium binding activity of OPH and peptides F5 and F7 was weak. Spectrums/MS charged peaks in F5 and F7 revealed a number peptides.
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Copyright © 2015 the author(s). Theses may be used for non-commercial research, educational, or related academic purposes only. Such uses include personal study, research, scholarship, and teaching. Theses may only be shared by linking to Carleton University Institutional Repository and no part may be used without proper attribution to the author. No part may be used for commercial purposes directly or indirectly via a for-profit platform; no adaptation or derivative works are permitted without consent from the copyright owner.
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- 2015
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