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Effect of heating oxyhemoglobin and methemoglobin on microsomes oxidation

Bou, Ricard, Hanquet, Nicolas, Codony, Rafael, Guardiola, Francesc, Decker, Eric A.
Meat science 2010 v.85 no.1 pp. 47-53
raw meat, cooked foods, heme iron, oxidation, antioxidants, hemoglobin, meat protein, water solubility, protein value, free radical scavengers, iron, lipid peroxidation, thermal stability
Hemoglobin (Hb) has been proposed to be a major pro-oxidant in raw and cooked meats. To understand the mechanisms and differentiate between the pro-oxidant and antioxidant potential of oxyhemoglobin (OxyHb) and methemoglobin (MetHb), their pro-oxidant activity, protein solubility, radical scavenging capacity, iron content and contribution of non-chelatable iron on lipid oxidation were determined as a function of thermal treatments. The ability of native OxyHb and MetHb to promote lipid oxidation was similar and higher than their corresponding OxyHb or MetHb heated at 68 and 90°C but not different from those at 45°C. The pro-oxidant activity of MetHb heated at 68 and 90°C were similar whereas the pro-oxidant activity of OxyHb heated at 68°C was higher than that heated at 90°C. The decreased pro-oxidant activity of heat-denatured Hb was associated with a decrease in the solubility of heme iron while free iron showed little impact on the lipid oxidation.