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Interactions between carnosine and the different redox states of myoglobin
- Decker, E.A., Chan, W.K.M., Livisay, S.A., Butterfield, D.A., Faustman, C.
- Journal of food science 1995 v.60 no.6 pp. 1201-1204
- meat, myoglobin, lipid peroxidation, redox reactions, carnosine
- To better understand the mechanism by which carnosine inhibits myoglobin oxidation in salted ground pork, interactions of carnosine with ferrylmyoglobin (ferMb), metmyoglobin (metMb) and oxymyoglobin (oxyMb) were investigated Carnosine (0-50 mM; pH 5.0-7.5) accelerated the conversion of metMb to oxyMb at pH greater than or equal to 7.0 and carnosine concentrations greater than or equal to 25 mM. Carnosine (1-50 mM) also accelerated the conversion of oxyMb to metMb with its formation rates increasing with decreasing pH and increasing carnosine concentrations. Carnosine (1-25 mM) inhibited ferMb catalyzed oxidation of phosphatidylcholine liposomes 16-76% and reduced the ferMb electron paramagnetic resonance signal 24-43%. Results suggested that the color stabilizing effects of carnosine were related to its antioxidant activity.