Abstract
1H NMR spectroscopy was used to determine first order rate constants at four temperatures (300, 304, 308, 312 K) and activation energies of the autoxidation reaction for oxymyoglobin. the haeminic pigment was purified from two bovine muscles with different colour stabilities (psoas major (PM) and longissimus lumborum (LL)) at 2h (day 0) and 192 h (day 8) post mortem. to characterize this autoxidation reaction, we have focused attention on the time‐temperature dependent disappearance of the Val‐E11 methyl group signal. This study showed that, whatever the time post mortem, although the myoglobin autoxidation rate was greater for PM than for LL muscle, the activation energies were similar. It was also worth noting that, in the range 300–312 K, the average ratio of autoxidation rate constants between day 8 and day 0 was near 1.6 for the two muscles studied. It is reasonable to think that oxidative processes developed during 8 days meat storage have led to a structural change within the cavity of the heme pocket of the myoglobins. Moreover, only one orientation of the porphyrin within the heme pocket was noted for the two muscles studied.
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