Interrelationship among myoglobin forms, lipid oxidation and protein carbonyls in minced pork packaged under modified atmosphere
2019
Zareian, Mohsen | Tybussek, Thorsten | Silcock, Patrick | Bremer, Phil | Beauchamp, Jonathan | Böhner, Nadine
Red meats such as pork contain pro-oxidative heme proteins that can act as initiators of protein oxidation. The present study investigated the interrelationships between different forms of myoglobin, lipid oxidation and protein carbonyls in minced pork packaged under modified atmosphere (30% CO2 and 70% O2) and stored at 4 °C for 12 days. Peroxides were correlated with metmyoglobin formation (r = 0.992; p < 0.01), non-heme iron content (r = 0.988; p < 0.05), ferryl myoglobin (r = 0.986; p < 0.05), autoxidation rate (r = 0.984; p < 0.05), and myoglobin denaturation rate (r = 0.978; p < 0.05). Storage did not significantly affect fatty acid composition, whereas secondary metabolites of lipid oxidation were associated with protein carbonyls (r = 0.994; p < 0.05). Total color differences indicated discoloration during storage. The present study provides information on the changing biochemical profile with insights on spoilage development during storage.
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