Correlating the Electrochemical Kinetics of Myoglobin‐Films to pH Dependent Meat Color

We report here for the first time application of electrochemical kinetics to understand the myoglobin redox‐properties at three relevant meat pH conditions. We investigated the kinetics of oxymyoglobin formation electrochemically using films of myoglobin coated on high‐purity graphite electrodes. Three pH conditions corresponding to the physiological state (pH 7.4), stressed animal muscle (pH 6.4), and post‐mortem meat (pH 5.6) were examined in this study. Our findings show that slower metmyoglobin reduction rate and diminished oxygen‐affinity cause the discoloration of red‐meat at low acidic pH‐conditions in comparison to the physiological pH 7.4.