Free radicals attack to biological molecules can initiate their oxidation and contribute to the development of several chronic diseases. Oxidation of low density lipoprotein, as well as a higher concentration of cholesterol, have been implicated in the development of atherosclerotic lesions and increased risks of cardiovascular diseases. Strategies to decrease the risks then include scavenging of free radicals and the reduction of cholesterol (e.g. binding of bile acids). In this regard, 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 chelating capacities as well as their ability to inhibit low density lipoprotein oxidation (LDL). Medium oat bran samples were treated with two cell wall polysaccharide degrading enzymes (cellulase and viscozyme) to generate two protein isolates named CPI and VPI respectively. Ten hydrolysates were subsequently prepared by treating CPI or VPI with five proteases protamex, alcalase, flavourzyme, pepsin and pepsin+pancreatin. The two highest degrees of hydrolysis (26.4 ± 0.5 and 22.0 ± 0.1%) were obtained under simulated gastrointestinal digestion with pepsin and pancreatin. Intrinsic absorbance showed that CPI-alcalase and CPI-pepsin/pancreatin had a higher content of aromatic amino acids. In the antioxidant oxidant assays, VPI-pepsin better scavenged ROO • radicals (496.77±5.83 μM Trolox Equivalents (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. In the metal