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Journal of Chemistry
Volume 2016 (2016), Article ID 8216378, 8 pages
Research Article

Pepsin Digested Oat Bran Proteins: Separation, Antioxidant Activity, and Identification of New Peptides

1Food Science and Nutrition Program, Carleton University, 1125 Colonel By Drive, Ottawa, ON, Canada K1S 5B6
2National Institute of Higher Education in Agronomy, Food and Environmental Sciences, 26 Boulevard Docteur-Petitjean, BP 87999, Dijon, France
3Institute of Biochemistry, Carleton University, 1125 Colonel By Drive, Ottawa, ON, Canada K1S 5B6

Received 16 September 2015; Revised 31 December 2015; Accepted 3 January 2016

Academic Editor: Somdet Srichairatanakool

Copyright © 2016 Ariane Vanvi and Apollinaire Tsopmo. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The aim of this study was to determine pepsin hydrolysis conditions to produce digested oat bran proteins with higher radical scavenging activities and separate and identify peptides. Isolated proteins were then digested with different concentrations of pepsin and incubation times. Hydrolysates produced with 1 : 30 enzyme substrate (E/S) ratio and 2 h possessed the highest peroxyl radical scavenging activity, 608 ± 17 µM TE/g (compared to 456–474 µM TE/g for other digests), and was therefore subsequently fractionated into eight fractions (F1–F8) by high performance liquid chromatography (HPLC). F1 and F2 had little activity because of their low protein contents. Activities of F3–F8 were 447–874 µM TE/g, 20–36%, and 10–14% in the peroxyl, superoxide anion, and hydroxyl radical tests, respectively. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify a total of fifty peptides that may have contributed to the activity of F3, a fraction that better scavenged radicals.