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Updated: Jun 12, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Cyclic Continuous Glycation Enhanced Dispersibility of Myofibrillar Protein: Reaction Efficiency and Sites
Jiale Chai1, Xue Zhao1, Weiyi Zhang1
1State Key Lab of Meat Quality Control and Cultured Meat Development, Ministry of Science and Technology, Key Laboratory of Meat Processing, Ministry of Agriculture, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, Jiangsu, China.
Abstract:
Reaction efficiency in glycation lacks sufficient attention, leading to the waste of process costs. Cyclic continuous glycation (CCG) is an effective approach to accelerate covalent binding between myofibrillar protein (MP) and glucose. This study elucidated that CCG promoted the exposure of reactive glycated sites in MP with full unfolding of secondary and tertiary structures. Notably, the glycation rate was significantly increased by 65.43%. Physicochemical properties indicated that MP-glucose conjugates with high graft degree exhibited favorable solubility, dispersibility, and thermal stability. Furthermore, proteomics was applied to reveal the glycated sites and products in glycoconjugates of MP. Glycation preferentially acted on the tails of the myosin heavy chain. The glucosylation modification on the head region was enhanced by CCG contributing to the inhibition of the head-head interaction. Overall, this study systematically clarifies the mechanism of CCG, providing a theoretical basis for the application of glycation in innovative meat products.
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