Low-voltage electrostatic field enhances the frozen force of-12 degree celsius to suppress oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing

The effect of low-voltage electrostatic field (LVEF) assisted -9 degrees C (LVEF-9) and -12 degrees C (LVEF-12) frozen, non-LVEF-assisted -9 degrees C (NLVEF-9) and -12 degrees C (NLVEF-12) frozen, and conventional frozen (CF-18, -18 degrees C) storage on the muscle microstructure and the oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing was investigated. Compared with NLVEF-9, LVEF-9, and NLVEF-12, LVEF-12 maintained the better integrity of muscle microstructure, demonstrated by smaller holes, more complete Z-line and M-line, and no significant difference with CF-18 (P > 0.05). Furthermore, LVEF-12 effectively inhibited protein oxidative denaturation as shown by the lower carbonyl content, surface hydrophobicity, and higher total/active sulfhydryl groups and Ca2+-ATPase activity. Moreover, LVEF-12 effectively maintained the integrity of the secondary and tertiary structure of proteins, reduced cross-linking aggregation of proteins, and sustained better functional properties, as shown by higher alpha-helix content, fluorescence intensity, protein solubility, and lower R-value, disulfide bonds.

Automated summary

This study investigated the effects of low-voltage electrostatic field (LVEF) assisted -9°C and -12°C frozen storage, as well as non-LVEF-assisted -9°C and -12°C frozen storage, and conventional frozen storage (-18°C) on muscle microstructure and the oxidative denaturation of lamb protein. The results showed that LVEF-12 demonstrated better preservation of muscle microstructure and inhibition of protein oxidative denaturation compared to other freezing methods.