Insights into physical property changes of fish proteins during low-frequency electric field freezing

To elucidate the mechanism by which low-frequency electric field affect ice crystal formation, a comparative investigation was conducted to examine the effects of low-frequency electric field-assisted freezing (LF-EFAF) and air freezing (AF) on the physical properties of tilapia fish proteins. The LF-EFAF group exhibits a higher specific heat capacity, a lower enthalpy and a faster icing rate in comparison to the AF group, reduced the icing rate by 10.28 %. The dielectric constant of the LF-EFAF group remained closer to that of the fresh samples. Furthermore, LF-EFAF reduced fish protein conductivity by 5 %. A strong correlation was observed between alterations in the physical properties of fish proteins and changes in their protein characteristics. LF-EFAF was observed to reduce protein particles by 44 %, and enhance the dielectric loss of fish proteins. These effects resulted in a reduction in the size of the ice crystals.