Authors
Lan Liu, Jiahui Bi, Jingnan Zang, Mingmin Qing, Ying Zhao, Yanqiu Ma, Yujie Chi, Yuan Chi
Published in
Food chemistry. Volume 525. Issue Pt 3. Pages 150571. Jul 27, 2026. Epub Jul 27, 2026.
Abstract
This paper focused on egg yolk plasma (EYP) and systematically analyzed the critical factors underlying heat-induced EYP instability. 76 °C is the key temperature for phase behavior transformation of EYP, and 72 °C marks the rheological transition point of thermal aggregation rate. Heat induction caused particle size of EYP increase by 6.20 times and emulsifying activity decrease by 6.90%, corresponding to larger and more aggregated emulsion droplets. Protein structure became more compact, with β-sheet content increasing by 32.48% and reduced fluorescence intensity. SDS-PAGE revealed that β-livetin, γ-livetin and apo-LDL were the key proteins involved in heat-induced EYP aggregation. Betaine altered hydrogen bond and water binding to suppress particle growth of EYP proteins, yet lost its protective effect on key proteins at 76 °C. The results clarify the thermal aggregation rules of EYP and liquid egg yolk, and lay a theoretical foundation for the production of thermally stable liquid egg products.
PMID:
42531638
Bibliographic data and abstract were imported from PubMed on 31 Jul 2026.
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