| Summary: | The objective of this study was to investigate the effect of pork oxidation through modified atmosphere packaging (MAP) on gel characteristics of myofibrillar proteins (MP) during the heat-induced gelation process. The pork <i>longissimus thoracis</i> (LT) was treated by MAP at varying oxygen concentrations (0, 20, 40, 60, and 80% O<sub>2</sub>) with a 5-day storage at 4 °C for the detection of MP oxidation and gel properties. The findings showed the rise of O<sub>2</sub> concentration resulted in a significant increase of carbonyl content, disulfide bond, and particle size, and a decrease of sulfhydryl content and MP solubility (<i>p</i> < 0.05). The gel textural properties and water retention ability were significantly improved in MAP treatments of 0–60% O<sub>2</sub> (<i>p</i> < 0.05), but deteriorated at 80% O<sub>2</sub> level. As the concentration of O<sub>2</sub> increased, there was a marked decrease in the α-helix content within the gel, accompanied by a simultaneous increase in β-sheet content (<i>p</i> < 0.05). Additionally, a judicious oxidation treatment (60% O<sub>2</sub> in MAP) proved beneficial for crafting dense and uniform gel networks. Our data suggest that the oxidation treatment of pork mediated by O<sub>2</sub> concentration in MAP is capable of reinforcing protein hydrophobic interaction and disulfide bond formation, thus contributing to the construction of superior gel structures and properties.
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