Abstract:Porcine longissimus muscles were used as the raw material to study changes in the molecular interactions of proteins, degree of oxidation of myofibrillar protein (the main components of pork), and changes in surface hydrophobicity and structure of myofibrillar proteins using a combination of ultra-high pressure and thermal treatment to determine their correlation. The results showed that hydrogen bonds, hydrophobic interactions, and disulfide bonds were the primary molecular forces maintaining the three-dimensional network structure of porcine proteins following a combination ultra-high pressure and thermal treatment. After combined treatment with ultra-high pressure and thermal process, the number of SH groups in myofibrillar proteins was significantly reduced (p < 0.01), whereas the number of S-S bonds, surface hydrophobicity, and carbonyl content in myofibrillar proteins significantly increased (p < 0.01). Secondary structure analyses confirmed that the content of helical structures decreased, while the content of disordered structures increased concomitantly.and Correlation analysis indicated a close relationship (p < 0.01) of the ultra-high pressure coupled with thermal treatment with the molecular interaction of proteins, carbonyl content, and protein structure. These findings will be useful for improving the understanding of changes in proteins after ultra-high pressure combined with thermal treatment, provide scientific guidance for the protein production process, and offer a theoretical basis for developing new meat products.
