College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Kexin College, Hebei University of Engineering, Handan, Hebei 056038, China.
Food Chem. 2021 Nov 15;362:130222. doi: 10.1016/j.foodchem.2021.130222. Epub 2021 May 27.
The synergistic effect of pH and heating on the structure, aggregation behaviour and gel properties of myofibrillar protein (MP) in mirror carp (Cyprinus carpio) was evaluated. The surface hydrophobicity of the control at pH 5.0 (143.6 ± 0.3 μg) was significantly higher than that of other samples (P < 0.05). Under the same pH conditions, the decrease in total sulfhydryl content of all samples during the heating process demonstrated that covalent/non-covalent cross-linking occurred between proteins due to heat input. Moreover, the decrease in solubility and the increase in turbidity of all samples verified the fact of MP aggregation, and the changes in the elasticity index (EI) and macroscopic viscosity index (MVI) also indicated a decrease in MP fluidity upon heating treatment. Therefore, the aggregation of MP was affected by pH and heating, and the optimal three-dimensional network structure and gel properties could be formed at pH 6.0 and above 70 °C.
研究了 pH 值和加热协同作用对鲤鱼肌原纤维蛋白（MP）结构、聚集行为和凝胶特性的影响。在 pH 值为 5.0 时（143.6±0.3μg），对照组的表面疏水性显著高于其他样品（P<0.05）。在相同 pH 值条件下，所有样品在加热过程中总巯基含量的减少表明，由于热输入，蛋白质之间发生了共价/非共价交联。此外，所有样品的溶解度降低和浊度增加证实了 MP 聚集的事实，弹性指数（EI）和宏观粘度指数（MVI）的变化也表明 MP 流动性在热处理过程中下降。因此，MP 的聚集受到 pH 值和加热的影响，在 pH 值为 6.0 以上和 70°C 以上可以形成最佳的三维网络结构和凝胶特性。
