Food science, Food chemistry, Speciation, Hydroperoxides, Lipid oxidation, Antioxidant free thiols, Aromatic amino acids, UV absorptionTransition metals play an important role in a wide variety of biological processes, but their functions are dependent on the quantity and the type of species present. Specific forms of arsenic (As) and chromium (Cr) are associated with oxidative stress, cellular damage and inflammation. The aim of this research was to test in a food system whether, in the presence of hydrolyzed oat proteins, arsenic or chromium will exist predominantly in a specific oxidative state, and to evaluate the potential implication of promoting or decreasing oxidative stress. Eight hydrolyzed proteins with different degrees of radical scavenging activities were produced by combining two extraction methods and four proteases. The addition of hydrolysates to ground chicken meat decreased lipid hydroperoxides by up to 50% when stored at 4 °C but had no effect at -20 °C. The ratio of pentavalent arsenic (As(V)) to arsenobetaine (AsB) in meat was about 2:1 but in the presence of the hydrolysates, meanwhile, the amount of AsB detected was 3-fold higher depending on the storage condition. This was due to better extraction of AsB in the presence of hydrolysates rather than to the conversion of other species. Data on chromium showed that Cr(VI) contents decreased from 14.3 ± 0.1 to 6.3 ± 0.5 μg/g while concentrations of Cr(III) increased from 2.8 ± 0. 2 to 8.6 ± 0.7 μg/g. In summary, the addition of hydrolyzed oat proteins to chicken meat enhanced the extraction of AsB, and had little effect on arsenic speciation during storage meanwhile, there was a reduction of Cr(VI) to Cr(III) which was in part due to the relative content of thiol groups. Additionally, there was a reduction of lipid oxidation in meats that contained the oat protein hydrolysates.

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Department of Chemistry

Shittu, A. (Adenike), Esfandi, R. (Ramak), & Tsopmo, A. (2020). Chromium and arsenic speciation analysis in meats by HPLC-ICP-MS in the presence of hydrolyzed oat proteins with radical scavenging activities. Heliyon, 6(3). doi:10.1016/j.heliyon.2020.e03654