Oxymyoglobin oxidation and membrane lipid peroxidation initiated by iron redox cycle: prevention of oxidation by enzymic and nonenzymic antioxidants.

Abstract

The red color of muscle is principally due to the presence of oxymyoglobin. Oxidation of heme iron from the ferrous to the ferric state produces a brownish color, which consumers find undesirable. The aim of this study was to use enzymic and nonenzymic antioxidants to simulate in situ muscle antioxidation reactions in order to understand better the mechanism by which the iron redox cycle catalyzes membrane lipid peroxidation and oxymyoglobin oxidation. The inclusion of superoxide dismutase (SOD) in the model system decreased oxymyoglobin oxidation by 10% without affecting lipid peroxidation. Addition of catalase decreased oxymyoglobin oxidation by approximately 40% but not lipid peroxidation. Increasing the ceruloplasmin concentration inhibited lipid peroxidation but increased oxymyoglobin oxidation, which was inhibited by SOD and catalase. Conalbumin (50 microM), a specific iron chelator, inhibited peroxidation and oxymyoglobin oxidation by almost 50%. The addition of the antioxidant catechin (500 microM) decreased lipid peroxidation by 90% but oxymyoglobin oxidation by only 50%. Feeding turkeys with vitamin E at several levels significantly increased the alpha-tocopherol level of membranes, thus preventing oxymyoglobin and lipid oxidation. In conclusion, oxymyoglobin stability in the model system was affected by two pathways: (a) oxygen active species, such as O(2)*(-), H(2)O(2), HO*, and ferryl, generated during autoxidation of myoglobin and oxidation of ferrous ions and ascorbic acid; and (b) lipid radicals, such as ROO*, RO*, and hydroperoxides, generated during lipid peroxidation. Maximum inhibition could be achieved only by introducing inhibitors of both pathways into the system.