Chain reactions of temperature-induced egg white protein amorphous aggregates: Formation, structure and material composition of thermal gels

• Published in: Food chemistry 2024-12, Vol.460 (Pt 3), p.140785, Article 140785
• Main Authors: Liu, Xin, Zhang, Ziwei, Chen, Yujie, Zhong, Mengzhen, Lei, Yuqing, Huo, Jiaying, Ma, Lulu, Li, Shugang
• Format: Article
• Language: English
• Subjects: Amorphous aggregates; Animals; Chickens; egg albumen; Egg Proteins - chemistry; Egg white; Egg White - chemistry; food chemistry; gels; Gels - chemistry; Hot Temperature; mucins; Ovomucin; Protein Aggregates; proteomics; quality control; temperature; Temperature induction; Thermal gel mechanism
• ISSN: 0308-8146; 1873-7072; 1873-7072
• DOI: 10.1016/j.foodchem.2024.140785

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. [Display omitted] •Temperature-induced changes in the morphology of egg white aggregates followed the “spherical - chain - regiment” shape rule.•The EWTG network structure followed the changing rule from “irregular bead-like” to “regular lamellar structure”.•Amorphous aggregates of EWTGs disrupted the ordering and continuity of gel networks.•Amorphous aggregates based on Mucin 5B as an “aggregation core” were the main reason for the impaired texture of EWTG at 95 °C.