Pressure Induced Structural Changes of Proteins Affecting the Ice Nucleation Temperature of Pork Loins

This study investigated the effects of pressure-mediated protein changes on the ice nucleation temperature of pork loins. To variate chemical state of meat proteins, pork loin was pressurized at varying pressure levels (100–500 MPa) for 3 min, and moisture content, expressible moisture (EM) and differential scanning calorimetry (DSC) were analyzed. Although, all treatments showed similar moisture content, EM and degree of protein unfolding of pork loin showed different features as of 300 MPa. At moderate pressure treatments (100–200 MPa), all protein fractions were detected in DSC experiments, and pork loin had lower EM than control (p<0.05). Meanwhile, myosin and actin of pork loin treated at greater than 300 MPa were completely unfolded, and the treatments showed high EM compared to control (p<0.05). Unfolding of meat proteins was a factor suppressing ice nucleation, and the ice nucleation temperature tended to decrease with increasing applied pressure level. The ice nucleation characteristics of pressurized pork loin exhibited a potential application in freezing storage of pressurized meat with less tissue damage comparing to freeze fresh meat, and further exploration regarding the quality change after freezing of fresh and pressurized meat was warranted.