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Updated: Jul 8, 2026

Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs
Published on: January 27, 2021
pH-Shifting combined with heat treatment regulates the aggregate structure and interfacial functional properties of
Yating Wu1, Yicheng Guo1, Junhua Li1
1State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Wuxi, Jiangsu 214122, China.
Abstract:
Natural egg white protein (NEWP) exhibited inherent thermal instability, restricting its application in thermally processed liquid foods. This study investigated pH-shifting combined with heat treatment as a strategy to modulate EWPP properties, particularly the superior performance and molecular mechanisms of alkaline-treated N-EWPP. Molecularly, alkaline conditions trigger partial unfolding to form flexible molten-globule intermediates, self-assembling into hydrogen-bond-stabilized dispersed aggregates. This structural rearrangement increased molecular flexibility and exposed abundant hydrophilic groups, contributing to high absolute zeta potential and excellent hydration capacity. The micromorphology of N-EWPP featured low surface roughness and uniform dispersion, while its interfacial behavior showed balanced wettability and the highest interfacial protein load, facilitating the formation of a dense viscoelastic interfacial film. Functionally, compared with natural EWPP, N-EWPP increased EAI by 1.8-fold (from 0.32 to 0.89) and ESI by 2.2-fold (from 17.4 to 55.5), and reduced the heat-induced transmittance loss from 10.9 to 1.6 percentage points. These superior properties of N-EWPP were closely related to its unique aggregate structure, as well as the dominant role of hydrogen bonding in stabilizing aggregates. This work provided an experimental basis for converting thermosensitive globular proteins into high-performance food-grade emulsifiers with enhanced thermal stability.
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