Analysis of the changes in structural modification, physicochemical properties, and water distribution of porcine myofibrillar proteins induced by sub-freezing short storage (−6 °C and −12 °C, 7 d)

The changes in structure, oxidative denaturation, and moisture distribution of myofibrillar proteins (MP) stored at −6 °C or −12 °C for 7 d were analyzed using fresh meat (FM), chilling (4 °C) and freezing (−18 °C) for 7 d as controls. The results showed that the structures of MP under −12 °C treatment and −18 °C treatment were similar (P > 0.05). Furthermore, compared to 4 °C treatment, −12 °C treatment could inhibit the MP's denaturation and alleviate the MP's oxidation. Regarding the static rheology and water distribution results, −12 °C treatment was more beneficial for maintaining the rheology properties and water holding capacity than 4 °C treatment. Conversely, the oxidative denaturation and water leakage of MP at 4 °C for 7 d were severe, due to the structural destruction. Therefore, −12 °C sub-freezing short storage (7 d) could be considered an ideal alternative to −18 °C short storage (7 d) with low power consumption.