Effects of isochoric freezing on myofibrillar protein conformational structures of chicken breasts

Abstract

This study investigated the myofibrillar protein conformational structures during the isochoric freezing of chicken breasts at three different temperatures of −4, −8, and −12 °C. Experiments conducted using 2.5% NaCl solution revealed that samples treated at −4 °C (25 MPa) showed no significant (P > 0.05) effect in the myofibrillar protein structure, while those treated at −8 °C (60 MPa) showed significant changes (P < 0.05) in protein properties including dityrosine, solubility, and sulfhydryl, suggesting the partial recovery of the samples. However, samples treated at −12 °C (85 MPa) indicated complete destruction of the myofibrillar protein structure. Results of the myofibrillar sarcomeres evaluation further verified that freezing at −4 °C was able to maintain chicken breast meat protein structure. Insights on the possibilities of preserving meat under isochoric freezing in the food industry are envisaged to be gained from the current study.