The aim of this project was; 1) to produce and characterize various hydrolyzed proteins from oat brans; 2) determine their antioxidant, metal binding and bile biding capacities as well their ability to inhibit low-density lipoprotein (LDL) oxidation. Medium oat bran samples treated with (cellulase and viscozyme) were digested with five proteases protamex, alcalase, flavourzyme, pepsin and pepsin+pancreatin. VPI-pepsin better scavenged ROO• radicals (496.77±5.83 μM(TE)/g) while VPI-flavourzyme and VPI-pepsin had better quenching for HO• (27.95 ±1.580 and and O2•- (45.31±6.6%) radicals, respectively. VPI-protamex exhibited the best Cu2+ chelating capacity (59.83±1.40%). All hydrolysates protected human LDL against Cu2+ mediated oxidation by reducing the concentration of hydroperoxides from 158.4 to 74.4-97.7 μMH2O2/mg. There was a binding of up to 46.3% for taurodeoxycholate and taurocholate. VPI alcalase proteins displayed the highest activity in the most assay and consequently separated into eleven fractions (F1-F11) (HPLC).