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Updated: Feb 11, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Glycosylation engineering in protein modification: Mechanistic insights, food applications, and potential health
Chenxu Xue1, Jiaxin Guo1, Wanjun He1
1College of Biosystems Engineering & Food Science, Zhejiang University, Hangzhou, 310058, China.
Abstract:
In recent years, natural proteins have increasingly failed to meet modern food industry demands for multifunctional performance under advanced processing conditions. Glycosylation, as an eco-friendly and safe protein modification strategy, has emerged to improve protein functional characteristics. This review systematically summarizes three predominant glycosylation approaches, that is, Maillard reaction-based glycation, enzymatic glycosylation, and physically-assisted glycosylation techniques. Furthermore, the study comprehensively illustrates process characteristics of dry-heating, wet-heating, enzymatic, and physically-assisted methods in glycoconjugate preparation. Moreover, critical reaction parameters are emphasized, including saccharide type selection, thermal processing conditions protein-to-carbohydrate mass ratios, pH, and temporal control. Comparative analyses demonstrate that glycated proteins exhibit superior physicochemical properties versus native counterparts: enhanced solubility, optimized emulsifying activity, strengthened gelation capacity, and improved foaming stability. Besides, industrial applications are multifaceted. Glycosylated proteins can serve as emulsifiers or gelling agents for the preparation of emulsion/gel systems. These systems function as fat replacers in baked goods and meat products, encapsulate bioactive compounds for the development of functional foods, and demonstrate emerging potential in 3D food printing by improving rheological properties. Notably, glycoconjugates exhibit intrinsic antimicrobial effects and allergenicity reduction properties, significantly expanding their commercial viability and safety profile in food applications. Finally, this review critically analyzes the potential health risks associated with protein glycosylation and proposes potential solutions. It provides critical insights into the structure-function relationships of glycosylated proteins and provides a summary of the inherent limitations of this process. These comprehensive discussions establish a conceptual framework that paves the way for future developments in food technology trends.
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