Heating of Chicken and Pork Meat Batters under Pressure Conditions: Protein Interactions

Abstract

Protein molecular interactions involved in the formation of the protein network of pork and chicken gels made by heating (70 °C) under pressure (200 and 400 MPa) were studied. Gel properties were influenced both by pressure treatment and by species. In both species, pressurization favored gels that had better water binding properties but were less hard and chewy. Nondenatured proteins were thermally detected in the batters after all of the combined pressure/heat processes. Heating-under-pressure conditions caused breakdown of myosin molecules, so that salt soluble protein content was higher than in nonpressurized samples.