Abstract
Moisture migration, protein oxidation, microstructure, and the physicochemical qualities of Atlantic mackerel during storage at 4 °C and 0 °C were explored in this study. Three proton components were observed in mackerel muscle using low-field nuclear magnetic resonance relaxation, which were characterized as bound water, immobilized water, and lipid. The relaxation peak of immobilized water shifted to a shorter relaxation time and its intensity decreased with the proceeding of the storage process. T1 and T2 weighted images obtained by magnetic resonance imaging showed a slightly continuous decrease in the intensity of water. The significant decrease in sulfhydryl (SH) content and the increase in carbonyl group (CP) content, disulfide bond content, and hydrophobicity revealed the oxidation of protein during storage. The contents of α-helixes in proteins decreased while that of random coils increased during storage, which suggested changes in the secondary structure of mackerel protein. The storage process also caused the contraction and fracture of myofibrils, and the granulation of endolysin protein. In addition, the drip loss, total volatile basic nitrogen (TVB-N), thiobarbituric acid-reactive substances (TBARS) value, and b* value increased significantly with the storage time.
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