Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Jilin Provincial Key Laboratory of Nutrition and Functional Food and College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Int J Biol Macromol. 2022 Mar 1;200:263-272. doi: 10.1016/j.ijbiomac.2021.12.185. Epub 2022 Jan 7.
This study aims to evaluate the structure of ions-regulated gelation of egg white protein (EWP) via aggregation kinetics model, which was built by monitoring turbidity. Results showed that compared with NaCl and KCl, the addition of NaSO increased free sulfhydryl content, surface hydrophobicity and particle size of EWP significantly, while weakened the order of secondary structure. Hence, strengthened gel network structure was observed with higher porosity, which improved the texture profiles and rheological properties of EWP gels. Based on these phenomena above, the relationship between aggregation behavior and gelling properties with ions was further investigated by aggregation kinetics model and principal component analysis. Because of the enhancement of protein interactions, the aggregation growth rate with NaSO was much faster than the samples with NaCl, which reflected over-aggregation due to the accelerated nucleation process and resulted in firmed gel network structure.
本研究旨在通过浊度监测，利用聚集动力学模型评估离子调控的蛋清蛋白（EWP）胶凝结构。结果表明，与 NaCl 和 KCl 相比，添加 NaSO4 可显著增加 EWP 的游离巯基含量、表面疏水性和粒径，同时削弱二级结构的有序性。因此，观察到增强的凝胶网络结构具有更高的孔隙率，从而改善了 EWP 凝胶的质构特性和流变学特性。基于这些现象，通过聚集动力学模型和主成分分析进一步研究了离子与聚集行为和胶凝特性之间的关系。由于蛋白质相互作用的增强，与 NaCl 相比，NaSO4 样品的聚集生长速率要快得多，这反映出由于成核过程的加速而导致的过度聚集，从而形成了更坚固的凝胶网络结构。
