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Updated: Jul 30, 2025

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Glycosylation modification: A promising strategy for regulating the functionalities of myofibrillar proteins
Yujuan Xu1,2, Xinglian Xu3, Baocai Xu1,2
1School of Food and Biological Engineering, Hefei University of Technology, Hefei, China.
Abstract:
Myofibrillar proteins (MPs), the most important proteins in muscle, play a vital role in the texture, flavor, sensory and consumer acceptance of final muscle-based food products. Over the past several decades, conjugation of carbohydrates to MPs via glycosylation is of particular interest due to the substantial enhancement in MPs characteristics. Studying the covalent interactions between carbohydrates and MPs under various processing conditions and molecular mechanisms by which carbohydrates affect the functionalities of MPs can introduce new perspectives for design and production of muscle-based foods. However, there is no insightful and comprehensive summary of the structural, physicochemical and functional characteristics changes of MPs induced by glycosylation modification and how these changes can be adopted to potentially promote the science-based development of tailor-made muscle foods. Based on this, the functionalities of MPs as well as their practical limiting issues are initially highlighted. A comprehensive overview of fabrication strategies is then introduced. Additionally, changes in the structural and functional properties of MPs regulated by glycosylation have also been carefully summarized. On this basis, the research limitations to be solved and our perspectives for the future development of muscle-based foods are put forward.
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