Mass spectrometry characterization for N-glycosylation of immunoglobulin Y from hen egg yolk.

Immunoglobulin Y (IgY) is a new therapeutic antibody that exists in hen egg yolk. It is a glycoprotein, not much is known about its N-glycan structures, site occupancy and site-specific N-glycosylation. In this study, purified protein from hen egg yolk was identified as IgY based on SDS-PAGE and MALDI-TOF/TOF MS.

The impact of N-glycosylation on conformation and stability of immunoglobulin Y from egg yolk.

Immunoglobulin Y (IgY) is a new therapeutic antibody, and its applications in industry are very broad. To provide insight into the effects of N-glycosylation on IgY, its conformation and stability were studied. In this research, IgY was extracted from egg yolk and then digested by peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine-amidase.

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

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).

A simple method for isolating chicken egg yolk immunoglobulin using effective delipidation solution and ammonium sulfate.

Chicken egg yolk immunoglobulin (IgY) is a superior alternative to mammalian immunoglobulin. However, the practical application of IgY in research, diagnostics, and functional food is limited due to complex or time-consuming purification procedures. The objective of this study was to develop a simple, safe, large-scale separation method for IgY from egg yolk.