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Updated: Sep 11, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Non-enzymatic glycation modifies the functional properties and extends the application of poultry egg proteins
Rui Wang1,2,3, Shuping Chen1,2,3, Yao Yao1,2,3
1Jiangxi Key Laboratory of Natural Products and Functional Food, Jiangxi Agricultural University, Nanchang, China.
Abstract:
Poultry eggs represent a globally prevalent and nutritious protein source and are regarded as excellent raw materials for food products. However, their persistent allergenicity and instability of functional properties during processing, severely limit their deep-processing applications. Non-enzymatic glycation emerges as an energy-efficient and food-safe chemical modification method that affects the proteins' structures and then regulates their functional properties, suggesting its potential to simultaneously mitigate allergenicity and enhance functionalities in egg-based products. The review systematically overviews the methods and the influencing factors of glycation. Subsequently, it carefully summarizes the change induced by glycation in structures and functional properties, involving processing performance and biological activities, of egg proteins, and demonstrates that glycation improves the functional properties. Particularly, the review highlights emerging applications of glycated egg proteins in precision nutrient delivery systems and intelligent antimicrobial packaging matrices. And current research limitations and the perspectives for the future development of glycated egg proteins are further proposed. The review deepens the understanding of glycated egg proteins and provides theoretical foundations for egg protein derivatives with tailored functionalities.
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