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Updated: Jul 29, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Cysteine and dialysis mediated inhibition of dynamic changes in glycosylated egg white protein during storage
Lulu Guo1, Wanqiu Zhang1, Fan Zhang1
1State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi, Jiangsu 214122, China.
Abstract:
Glycosylation is commonly used to improve the solubility and functionality of egg white protein (EWP), but glycosylated EWP is prone to quality deterioration during storage. To enhance its storage stability, cysteine (Cys) addition and dialysis-based desugar treatment were applied to xylo-oligosaccharide (XOS) glycosylated EWP (GEW) in accelerated storage examinations. Both Cys addition and dialysis minimized changes in soluble protein content, color difference, and particle size during storage. Further, they inhibited the Maillard reaction and the accumulation of its intermediate products. Cys addition effectively maintained protein structures and prevented protein crosslinking. However, dialysis lost the filling and protective effect of free sugars, lowering the denaturation temperature of ovalbumin. Cys and dialysis effectively maintained the stability of emulsifying properties, while Cys better preserved gelation. Overall, both Cys addition and dialysis markedly enhanced the storage stability of GEW, with Cys proving to be more effective.
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