Abstract
The photolysis mechanism of riboflavin (RF) in milk serum was studied. When milk serum was light-illuminated, the decomposition of RF in the serum was accelerated. Superoxide anion and hydrogen peroxide (H2O2) were found to form during the illumination, while superoxide dismutase (SOD) activity could not be detected in the milk serum. The decomposition of RF was significantly inhibited by the addition of tryptophan or mannitol which are scavengers of the hydroxyl radical. Conversely, addition of Fe3+ or lactoferrin promoted the decomposition.These results strongly suggest the direct participation of the hydroxyl radical in the RF decomposition in milk serum during light-illumination. It was also suggested that the hydroxyl radical was formed via the iron catalyzed Haver-Weiss reaction in which iron reacts with and H2O2, although it is still unknown how and H2O2 were generated by illumination.
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