Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field.

The application of a high-voltage electrostatic field (HVEF) is a novel method for thawing. To determine the effects of HVEF thawing (voltage range: -25kV to 0kV) on myofibrillar protein oxidation and/or denaturation and to provide a theoretical understanding of this process, pork tenderloin was thawed by traditional and HVEF methods. Based on the total sulfhydryl and carbonyl contents, further protein oxidation did not occur during HVEF thawing. It was proposed that the free radical-mediated oxidation of myofibrillar proteins was hindered by HVEF. The results of dynamic rheological analysis, protein aggregation and gel texture studies showed that HVEF thawing, especially -10kV HVEF thawing, led to better indicators than those achieved under air thawing. A higher abundance of proteins extracted from -10kV HVEF-thawed samples compared with air-thawed samples was found. Finally, this study showed that thawing under -10kV conditions did not affect the structure of myofibrillar proteins.