超高压结合热处理对猪肉蛋白质相互作用力及结构的影响

以猪背最长肌为原料,研究超高压(100~600 MPa)结合热处理(25~55℃)条件下,蛋白质相互作用力的变化,猪肉主要组成部分肌原纤维蛋白氧化程度,表面疏水性及结构变化,并建立他们之间的相关性。研究结果表明:超高压结合热处理后稳定猪肉蛋白质的作用力主要是氢键、疏水性相互作用和二硫键。经超高压结合热处理的肌原纤维蛋白质巯基含量极显著下降(p0.01),二硫键含量、疏水性和羰基值极显著上升(p0.01)。二级结构发生重排,螺旋结构减少,无序结构增多。相关性分析结果表明超高压结合热处理与蛋白质相互作用力、蛋白质羰基值、蛋白质结构之间存在着极显著的相关关系(p0.01)。这些结果可以帮助我们全面认识超高压结合热处理过程中蛋白质的变化,科学指导其生产过程,为开发新型肉制品提供理论依据。

Effects of Ultra-high Pressure Combined with Thermal Treatment on Molecular Interaction and Structure of Pork Proteins

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.