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DOI 10.1016/j.ijbiomac.2025.146328

Медицинская библиотека · International journal of biological macromolecules · 2025

Multi-coupled field processing enhanced thermal stability of egg white protein condensates through hydration effect.

Li Shijun, Hu Gan, Lin Jia, Lei Yuqing, Liu Xin, Gao Ying, Ma Lulu, Huo Jiaying, Wu Jijun, Dong Shijian, Li Shugang

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Аннотация

The application of egg white protein in the food industry is limited due to its poor thermal stability. In this study, thermally stable egg white protein (EWP) micro-nano condensate (200-300 nm) was prepared through shear-assisted preheating. After sterilization (98 °C, 5 min), these condensates maintained stable soluble protein concentration and turbidity, while control EWP showed significant changes (soluble protein: 43.62 → 41.54 mg/mL; turbidity: 0.038 → 0.066). Meanwhile, these condensates exhibited enhanced absolute Zeta potential (-39.60 mV vs control's - 20.13 mV) and thermal transition temperature (112.07 °C vs 103.73 °C). Mechanistic studies revealed that shearing firstly optimized protein hydration by disrupting aggregates, while subsequent preheating guided protein refolding into stable conformations. This sequential treatment significantly improved thermal stability across broad pH (5.5-8.5) and extended heating periods (15-45 min). The experimental results demonstrated that shear-assisted preheating effectively enhanced EWP's thermal stability through modulating protein hydration networks, offering technical insights into expanding its functional applications.

Для цитирования: Li Shijun, Hu Gan, Lin Jia, Lei Yuqing, Liu Xin, Gao Ying, Ma Lulu, Huo Jiaying, Wu Jijun, Dong Shijian, Li Shugang. Multi-coupled field processing enhanced thermal stability of egg white protein condensates through hydration effect.. International journal of biological macromolecules. 2025. DOI: 10.1016/j.ijbiomac.2025.146328.

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