Abstract
On exposure to oxygen the purple ferrous haem pigment, myoglobin, forms the bright red covalent complex, oxymyoglobin. In fresh meat oxidation of oxymyoglobin to metmyoglobin, the unattractive brown pigment, is affected principally by the reducing capacity of the muscle, oxygen availability and temperature. In frozen meat, light is the major factor affecting the oxidation rate. Oxidation of nitric oxide myoglobin, the ferrous pigment in cured meats, is prevented by excluding oxygen but proceeds rapidly in light, if oxygen is present. Stress, pre-slaughter handling of the animal and post-slaughter treatment of the carcass affect the light scattering properties of the meat. Glycogen depletion in the live animal results in translucent, dark firm and dry (DFD) meat with high pH and high oxygen uptake. Rapid post-mortem glycolysis causes structural changes in muscle which becomes opaque, pale soft and exudative (PSE). Electrical stimulation of the carcass and the rate of chilling also affect light scattering of meat. On storage, increase in light scatter is accompanied by a decrease in colour stability.
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