Reduction of hexavalent chromium by digested oat bran proteins

Hexavalent chromium (Cr(VI)) is associated with an increase in oxidative stress, such as DNA, lipid and protein oxidations. This study investigated, for the first time, the ability of digested food proteins to reduce Cr(VI) and scavenge free radicals. Protamex, an endopeptidase was used to digest oat bran protein isolates for 1, 2, 3, and 4 h. The hydrolysates (1 mg/ml) showed a maximum Cr(VI)-reducing activity of 5.4 ± 0.4% and 44.6% at pH 7.4 and 3.0, respectively. The difference might be due to charge or conformation changes depending on the pH. The 2 h hydrolysate possessed the highest O 2 - inhibition activity (57.4 ± 5.1%), while the 1 h hydrolysate had the highest HO inhibition (11.6 ± 0.6%). A correlation (R2 = 0.82) was observed between the O 2 - scavenging activities of hydrolysates and their Cr(VI)-reducing activities at pH 3.0 only. Further investigations of the digested oat bran proteins are required to determine their ability to reduce Cr(VI) oxidative stress damage in vivo.