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Chain reactions of temperature-induced egg white protein amorphous aggregates: Formation, structure and material
Xin Liu1, Ziwei Zhang1, Yujie Chen1
1Key Laboratory for Animal Food Green Manufacturing and Resource Mining of Anhui Province/ Engineering Research Center of Bio-process, Ministry of Education/ School of Food and Biological Engineering, Hefei University of Technology, Hefei 230601, China.
Abstract:
Egg white protein is widely used in food, chemical, medical and other fields due to its excellent thermal gel properties. However, the regularity of egg white thermal gel (EWTG) by temperature influence is still unknown. In this study, we investigated the potential mechanism of temperature (75-95 °C, 15 min) gradient changes inducing thermal aggregation and gel formation of EWTG. The results showed that changes in textural characteristics and water holding capacity (WHC) of EWTGs depended on switching in protein aggregation morphology (spherical shape - chain shape - regiment shape) and gel network structure differences ("irregular bead-like" - "regular lamellar structure"). In addition, proteomics indicated that the generation of amorphous protein aggregates at 95 °C might be related to Mucin 5B as the aggregation core. The research revealed the EWTG formation from "whole egg white protein" to "single molecules", aiming to provide a reference for quality control in gel food processing.
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