title: Identification of peptides, metal binding and lipid peroxidation activities of HPLC fractions of hydrolyzed oat bran proteins.
abstract: The aim of this study was to evaluate metal binding and antioxidant activities of hydrolyzed oat bran proteins followed by the determination of peptide sequences. Protamex oat bran protein hydrolysates (OBPH) were separated by reverse-phase HPLC into eight peptide fractions (F1-F8) and their abilities to either chelate metals (Fe2+, Ca2+) or prevent the oxidation of lipids were investigated. In the Fe2+chelation assay, OBPH had significantly (p< 0.05) higher activity (39.7 %) than the best performed fraction F7 (22.8 %). The second most active was F5 with 12.1 % chelating activity and this was higher than the activity of the tripeptide glutathione (5.8 %) used as control. The two most Fe2+chelating fractions (F5, F7) however had weak calcium binding (0.6-1.0 %) properties at peptide concentration ranging from 0.2 to 1.0 mg/mL. In the lipid peroxidation assay, OBPH and all HPLC fractions prevented the oxidation of linoleic acid. More than 60 peptides mainly derived from globulin and avenin proteins were identified using tandem mass spectrometry.
authors: Food Science and Nutrition Program, Carleton University, 1125 Colonel By Drive, Ottawa, ON K1S 5B6 Canada.
authors: Morooj M
authors: MM
authors: Baakdah
authors: Food Science and Nutrition Program, Carleton University, 1125 Colonel By Drive, Ottawa, ON K1S 5B6 Canada ; Institute of Biochemistry, Carleton University, 1125 Colonel By Drive, Ottawa, ON K1S 5B6 Canada.
authors: Apollinaire
authors: 0000-0002-7062-0833
authors: A
authors: Tsopmo
keywords: Calcium binding; Mass spectrometry; Metal chelation; Oat bran; Protein hydrolysate