蛋黄
卵清蛋白
化学
食品科学
鸡蛋过敏
色谱法
生物
免疫球蛋白E
免疫学
免疫系统
抗体
作者
Xueying Wang,Dekun Meng,Jiaqi Wang,Huajiang Zhang,Hanyu Li,Lina Xu,Chaogeng Xiao,Ning Xia,Nan Zhang,Ahmed M. Rayan,Mohamed Ghamry
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2025-04-21
卷期号:484: 144450-144450
被引量:8
标识
DOI:10.1016/j.foodchem.2025.144450
摘要
In this study, we propose three methods of acidic pH shifting of egg yolk granules (EYGs) to investigate effects of EYGs structure on properties of EYGs-salted ovalbumin (SO) gels. Different pH parameters affect protein unfolding behavior, as well as assembly of high-density lipoprotein (HDL) and phosvitin during acidification. The main mechanism was a change in the microenvironment of hydrophobic amino acid residues and new hydrogen bonds, which induced the reassembly. Besides, low-content EYGs increased the mixed gel network structure density, cohesiveness (0.12-0.14) and chewiness (29.46-49.11). While mixed gels with high content EYGs had higher hardness and recovery rate, and were more tightly bound to water molecules. EYGs-4-6 exhibited greater hydrogen bonding forces, which could lead to a more rigid network and greater potential for use as an active filler. Our study tracked the trajectory of pH-shifting preparations of reassembled EYGs while providing new insight into nutritional value of SO gel.
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