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Updated: Jun 18, 2025

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Effect of glycation with three polysaccharides on the structural and emulsifying properties of ovalbumin
Yaxue Hu1,2, Qiqi Bian1,2, Lijia Chen1,2
1Medical Food Laboratory, Shanghai Key Laboratory of Pediatric Gastroenterology and Nutrition, Shanghai Institute for Pediatric Research, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200092, China.
Abstract:
Herein, three types of ovalbumin (OA)-polysaccharide conjugates were prepared with three polysaccharides (XG: xanthan gum; GG: guar gum; KGM: konjac glucomannan) for the fish oil emulsion stabilization. The glycation did not change the spectra bands and secondary structure percentages of OA, whereas it decreased the molecular surface hydrophobicity of OA. The initial emulsion droplet sizes were dependent on the polysaccharide types, OA preparation concentrations, polysaccharide: OA mass ratios, and glycation pH. The emulsion stability was mainly dependent on the polysaccharide types, polysaccharide: OA mass ratios, and glycation pH. However, it was minorly dependent on the OA preparation concentrations. The emulsions stabilized by conjugates with high polysaccharide: OA mass ratios (e.g., ≥3:5 for OA-GG) or appropriate glycation pH (e.g., 5.0-6.1 for OA-XG) showed no obvious creaming during the room temperature storage. This work provided basic knowledge on the structural modification and functional application of a protein.
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