pH shifting treatment of egg yolk granules /salted ovalbumin mixed gels: Reassembled of egg yolk granules effects on heat-induced amorphous aggregates

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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Publication Details

Journal
Food Chemistry
Published
2025-04-21
DOI
https://doi.org/10.1016/j.foodchem.2025.144450
Citations
7
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
8.14
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article

pH shifting treatment of egg yolk granules /salted ovalbumin mixed gels: Reassembled of egg yolk granules effects on heat-induced amorphous aggregates

Hanyu Li, Ahmed M. Rayan, Chaogeng Xiao, Huajiang Zhang et al.
7 citations
Food Chemistry
Proteins in Food Systems
8.14
article

pH shifting treatment of egg yolk granules /salted ovalbumin mixed gels: Reassembled of egg yolk granules effects on heat-induced amorphous aggregates

Hanyu Li, Ahmed M. Rayan, Chaogeng Xiao, Huajiang Zhang, Mohamed Ghamry, Ning Xia, Jiaqi Wang, Xueying Wang, Dekun Meng, Nan Zhang, Lina Xu
article en
7 citations

Abstract

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.

Food ChemistryVol. 484
Suez Canal University (EG), Northeast Agricultural University (CN), Benha University (EG), ZheJiang Academy of Agricultural Sciences (CN)
Zero hunger
Openalex Percentile: Top 3%
Proteins in Food Systems
8.14
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