title: Monitoring glycation-induced structural and biofunctional changes in chicken immunoglobulin Y by different monosaccharides.
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 IgY. IgY 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.
authors.affiliation: National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, P. R. China.
authors.forename: Zhenjiao
authors.initials: Z
authors.lastname: He
authors.affiliation: National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, P. R. China.
authors.forename: Chenyao
authors.initials: C
authors.lastname: Tong
authors.affiliation: National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, P. R. China.
authors.forename: Long
authors.initials: L
authors.lastname: Sheng
authors.affiliation: National Research and Development Center for Egg Processing, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, P. R. China.
authors.forename: Meihu
authors.initials: M
authors.lastname: Ma
authors.affiliation: National 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.
authors.forename: Zhaoxia
authors.initials: Z
authors.lastname: Cai
mesh_terms: D000818:Animals; D002645:Chickens / Q000502:physiology*; D000939:Epitopes / Q000737:chemistry*; D006031:Glycosylation; D007136:Immunoglobulins / Q000737:chemistry*; D009005:Monosaccharides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis / Q000662:veterinary; D013997:Time Factors
chemical_list: D000939:Epitopes; C016512:IgY; D007136:Immunoglobulins; D009005:Monosaccharides
keywords: Chicken Immunoglobulin Y; Glycation; Molecular structure stability; Protein structure; Reducing monosaccharides