Page 36 - Natural Antioxidants, Applications in Foods of Animal Origin
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Mechanism of Oxidation in Foods of Animal Origin                15
  VetBooks.ir  increase the efficiency of iron as a catalyst for lipid oxidation, presumably


            by regenerating the active ferrous form (Sato & Hegarty, 1971).
               Kolakowska (2002) reported the effect of transition metals in lipid
            oxidation.  Hydroperoxides  formed  at  the  propagation  stage  of the  free
            radical oxidation, as well as those produced by photooxidation and enzyme-
            catalyzed oxidation, can disintegrate and yield alcoxy, alkyl, and peroxyl
            radicals, which reinitiate the oxidation of unsaturated fatty acid. Hydroper-
            oxide decomposition may be triggered by temperature and/or light, but most
            important in this respect is the activity of transition metals, mainly iron and
            copper.
               The Fe  ions are more reactive than Fe  ions and decompose hydrogen
                                                  3+
                     2+
            peroxide over 100 times faster (Girotti, 1998). Iron occurs in human and
            animal bodies, in up to 90% in a bound form in: hemoglobin, myoglobin,
            cytochromes, the storage protein ferritin and hemosiderin, the iron trans-
            port proteins, transferrins, and as prosthetic groups  of enzymes. A small
            amount of iron occurs in a “free” form, that is, primarily as LMW iron.
            It complexes with organic phosphates, inorganic phosphates, amino acids
            (histidine,  glycine,  and cysteine), and organic acids (citric  acid) (Decker
            & Hultin, 1992). LMW iron contributes between 2.5 and 3.8% to the total
            iron content in muscle tissue of lamb, pork, and chicken. Dark muscles of
            chicken, turkey, and mackerel contain twice as much LMW iron and more
            ferritin  than light muscles (Kanner, 1992). LMW iron acts as a catalyst.
            Protein-bound Fe and Cu are minimally catalytic in oxidation. Ascorbate,
            NAD(P)H, thiol compounds, reduced glutathione, cysteine, and protein thiol
            groups release iron, which can catalyze the Fenton reaction. This occurs post
            mortem during, for example, the storage of fish or turkey, but the amount of
            reductants is then also decreased (Kanner, 1992; Hultin, 1994).



            1.4.5  SODIUM CHLORIDE

            Sodium chloride is able to catalyze  lipid  oxidation  in muscle  tissue
            (Nambudiry, 1980; Love  & Pearson, 1971).  Alternatively, the  Na  may
                                                                         +
            replace iron from a cellular complex via an ion exchange reaction (Kanner
            & Kinsella, 1983). The displaced iron may then participate in the initiation
            of lipid oxidation. It is most likely that meat or meat products containing salt
            such as surimi and cured meat are susceptible to lipid oxidation (Chaijan,
            2008).
               Ladikos and Lougovois (1990) reported that sodium chloride induces
            rancidity in freezer-stored, cooked, cured meat, in cured pork and in raw
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