Inhibition of low-density lipoprotein oxidation, antioxidative and bile acid-binding capacities of hydrolyzed proteins from carbohydrase-treated oat bran.

This study investigated the valorization of oat bran and the use of its proteins to generate polypeptides with antioxidant and bile acid-binding properties. Ten protein hydrolysates were prepared by treating cellulase (CPI) or Viscozyme (VPI) protein isolates with five proteases. VPI-pepsin was the best peroxyl radical scavenger (497 ± 6-μM Trolox equivalents [TE]/g) while VPI-Flavourzyme quenched hydroxyl radicals (28 ± 0.6) and VPI-pepsin superoxide anion radicals (45.3 ± 6.6%). Hydrolysates, except those produced with pepsin, dose-dependently chelated iron whereas VPI-Protamex had the best copper-chelating capacity (59.83 ± 1.40%). These antioxidative capacities were important in preventing by 50% in vitro copper-induced oxidation of human low-density lipoprotein. Furthermore, due to their aromatic amino acid contents and hydrophobicity, the hydrolysates bound up to 46.3% the bile acids taurodeoxycholate and taurocholate. PRACTICAL APPLICATIONS: The presence of oxidants in foods can damage food molecules and decrease their quality. They are also known to increase the risk of developing chronic conditions like cardiovascular disease. Finding new antioxidant molecules are therefore useful in the management of chronic diseases. Data from this work showed that hydrolyzed oat bran proteins can be useful in stabilizing commercial oil as they reduced the oxidation of peanut oil. Additionally, the protein hydrolysates not only prevented the oxidation of linoleic, a common component of both vegetable oils and biological cell membranes, they also inhibited the oxidation of human LDL cholesterol and chelated bile acids. These hydrolysates can then be further explored as multifunctional ingredients for the development of stable functional food products with potential beneficial effects on the cardiovascular system.