On the ability of lactoperoxidase to catalyze the peroxidase-oxidase oxidation of a vitamin E water-soluble derivative (Trolox C).

The rapid-scan spectral technique has been applied to test conversion of the lactoperoxidase compounds during the peroxidase-oxidase catalyzed oxidation of Trolox. The results clearly indicate a normal peroxidatic pathway of Trolox degradation. Changes of spectral scan profiles were investigated to study directly the interaction of Trolox with lactoperoxidase compound III. Oxygen radicals were not involved in peroxidase-mediated oxidation of Trolox. The rate of the one-electron reduction of lactoperoxidase compound I to II was the same in the absence and presence of equal amounts of Trolox and ascorbic acid, which is also a good substrate for lactoperoxidase. The oxidation of Trolox by lactoperoxidase has potential physiological relevance. Since it could help maintain the catalytic cycles and activity of animal peroxidases, leading to detoxification of hydrogen peroxide as a main product of inflammation processes.