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Enhanced rehydration of egg white powder by high-pressure homogenization: A quantitative proteomic perspective
Jinwen Zhai1, Zahra Batool2, Guofeng Jin3
1Institute for Egg Science and Technology, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, Sichuan, China.
Abstract:
This study investigates how high-pressure homogenization (HPH) pretreatment influences the properties of spray-dried and freeze-dried egg white powder (EWP). HPH treatment significantly reduced particle size and increased surface charge, enhancing protein solubility and dispersibility. Structural analysis revealed HPH induced partial protein unfolding, evidenced by increased surface hydrophobicity and exposed sulfhydryl groups, while maintaining secondary structure stability. These modifications improved functional properties, notably increasing emulsifying activity by 20-59% and gel strength by 15-41%. HPH markedly enhanced powder rehydration, reducing turbidity by 32% and increasing solubility to 97-98%. Quantitative proteomics of rehydrated precipitates revealed that HPH selectively reduced aggregation-prone proteins while enriching structure-stabilizing ones. These findings demonstrate that HPH pretreatment optimizes fluid-solid transitions during drying through controlled protein modifications, offering new insights for improving protein powder processing.
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