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Monitoring glycation-induced structural and biofunctional changes in chicken immunoglobulin Y by different monosaccharides.

Posted by on in 2016
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He Z1Tong C1Sheng L1Ma M1Cai Z22016. Poult Sci. 95(11):2715-2723. Epub 2016 Jul 14.

1National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, P. R. China.
2National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, P. R. China caizhaoxia@mail.hzau.edu.cn.

 

Abstract

Chicken IgY has been applied in the food industry as an important supplement. Glycation of IgY is of special interest due to its possible influence on the structure and functionality of IgYIgY was subjected to in vitro glycation with 4 different monosaccharides, including glucose (Glu), mannose (Man), fucose (Fuc), and fructose (Fru). The objective of this paper was to characterize the formation of IgY-sugar conjugates using ultraviolet spectra, fluorescence spectra, circular dichroism spectra, Fourier transform infrared spectra, and SDS-PAGE and differential scanning calorimetry analysis. The antigen epitopes of native and glycated IgY was determined by enzyme-linked immunosorbent assay (ELISA). The existence of broad bands in stacking gel and sample well demonstrated that reducing monosaccharides covalently bound to IgY. The secondary structure of IgY was altered from a well-defined β-sheet structure to a random coil structure. Fluorescence spectra showed that IgY was more hydrophilic after glycation. Thermal stability of glycated IgY was remarkably increased over that of native IgY. However, ELISA results would suggest that the antigen epitopes recognized by the polyclonal antibody and overall conformation changed in the IgY molecule due to a decrease in polyclonal antibody binding to glycated IgY. Data suggested that glycation induced by reducing sugars significantly affects the structure and antigen-binding ability of IgY, which could reduce the utility of IgY in certain applications.

KEYWORDS:

Chicken Immunoglobulin Y; Glycation; Molecular structure stability; Protein structure; Reducing monosaccharides

PMID:
 
27418665
 
DOI:
 
10.3382/ps/pew223
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