Lipid-controlled non-monotonic assembly and rheology of an egg yolk protein at a water–soybean oil interface
- 1Department of Physics, School of Natural Sciences, Shiv Nadar Institution of Eminence NH-91, Tehsil Dadri, Gautam Buddha Nagar Uttar Pradesh-201314 India
Abstract
Hen egg yolk is an essential component of food items such as mayonnaise and salad dressing. Phosvitin (PVT) is a phosphoprotein that exists in the granules of hen egg yolk and stabilizes food emulsions by preventing phase separation. Understanding how this protein is adsorbed at the interface of water and an edible oil in the presence and absence of lipids is essential. To monitor the kinetics of this adsorption, the dynamic interfacial tension was determined in the current investigation. The drop in interfacial tension over time indicates the adsorption of protein at the interface, which is enhanced upon increasing the concentration of protein in the water phase. However, at higher concentrations, the positive activation energy hinders the adsorption process, resulting in saturation of the interfacial tension. Dilational rheology of the macromolecular film at this oil–water interface shows the elastic nature of the film to be greater than its viscous nature, indicating the formation of a soft gel film. Low concentrations of the zwitterionic lipid 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) promote the adsorption of this protein at the interface. Interestingly, at high concentration, the lipid overtakes the interface, removing the protein from it. The lipid–protein composite film again shows a soft gel nature. AFM images provided evidence of PVT–POPC assembly, revealing distinct morphological features associated with lipid-induced reorganization of the protein at the interface. The non-monotonic effects of lipids on assembly of protein at the water–edible oil interface are an important observation for optimizing the composition of relevant food products.
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BibTeX
@article{jaglan2026lipidcontrolled,
title = {{Lipid-controlled non-monotonic assembly and rheology of an egg yolk protein at a water–soybean oil interface}},
author = {Nancy Jaglan and Rumal Singh and Sajal K. Ghosh},
journal = {RSC Advances},
year = {2026},
month = oct,
doi = {10.1039/d6ra06516c},
url = {https://doi.org/10.1039/d6ra06516c},
note = {CC BY-NC 3.0},
}
RIS
TY - JOUR
TI - Lipid-controlled non-monotonic assembly and rheology of an egg yolk protein at a water–soybean oil interface
AU - Nancy Jaglan
AU - Rumal Singh
AU - Sajal K. Ghosh
PY - 2026
DA - 2026/10/08
JO - RSC Advances
DO - 10.1039/d6ra06516c
UR - https://doi.org/10.1039/d6ra06516c
AB - Hen egg yolk is an essential component of food items such as mayonnaise and salad dressing. Phosvitin (PVT) is a phosphoprotein that exists in the granules of hen egg yolk and stabilizes food emulsions by preventing phase separation. Understanding how this protein is adsorbed at the interface of water and an edible oil in the presence and absence of lipids is essential. To monitor the kinetics of this adsorption, the dynamic interfacial tension was determined in the current investigation. The drop in interfacial tension over time indicates the adsorption of protein at the interface, which is enhanced upon increasing the concentration of protein in the water phase. However, at higher concentrations, the positive activation energy hinders the adsorption process, resulting in saturation of the interfacial tension. Dilational rheology of the macromolecular film at this oil–water interface shows the elastic nature of the film to be greater than its viscous nature, indicating the formation of a soft gel film. Low concentrations of the zwitterionic lipid 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) promote the adsorption of this protein at the interface. Interestingly, at high concentration, the lipid overtakes the interface, removing the protein from it. The lipid–protein composite film again shows a soft gel nature. AFM images provided evidence of PVT–POPC assembly, revealing distinct morphological features associated with lipid-induced reorganization of the protein at the interface. The non-monotonic effects of lipids on assembly of protein at the water–edible oil interface are an important observation for optimizing the composition of relevant food products.
SN - 2046-2069
ER -