Suppressive effect of ATP on autoxidation of tuna oxymyoglobin to metmyoglobin

Abstract

The discoloration of tuna meat proceeds during frozen storage at around −20 °C. On the other hand, the discoloration of highly fresh tuna meat could effectively be suppressed even if stored at −20 °C. However, the suppressive mechanism of the discoloration is not well understood. Here the effects of ATP on the autoxidation rate and molecular structure of tuna myoglobin are reported. The autoxidation rate of southern bluefin tuna Thunnus maccoyii myoglobin at 25 °C was suppressed in the presence of ATP especially in acidic pH range. Mixing ATP with myoglobin induced a spectral perturbation in the soret region of myoglobin. This spectral perturbation was observed as a function of the ATP concentration. Quenching of myoglobin fluorescence was also caused by ATP, saturating at around 0.5 mM ATP. According to dynamic light-scattering measurements, the molecular weights of tuna Mb changed from 15.5 to 11.3 kDa with ATP and zeta-potential measurements gave also a negative surface charge without ATP and a positive one with ATP, respectively. The above results indicate that ATP-induces changes in the conformational structure of myoglobin. The effects of ATP on myoglobin could thus provide a possible mechanism to regulate the autoxidation of myoglobin.