Effects of unfolding treatment assisted glycation on the IgE/IgG binding capacity and antioxidant activity of ovomucoid

• Published in: Food & function 2024-01, Vol.15 (1), p.196-27
• Main Authors: Xia, Xian, Li, Jiangdong, Liang, Rui, Li, Yi, Ma, Xiaojuan, Yang, Ying, Lozano-Ojalvo, Daniel
• Format: Article
• Language: English
• Subjects: Allergenicity; Allergens; Binding; Carbohydrates; Chelation; Digestive system; Disulfide bonds; Epitopes; Food allergies; Gastrointestinal tract; Glycosylation; Immunoglobulin E; Immunoglobulin G; Maillard reaction; Maltose; Reduction; Saccharides; Scavenging
• ISSN: 2042-6496; 2042-650X
• DOI: 10.1039/d3fo04035f

Ovomucoid is the immune-dominant allergen in the egg white of hens. Due to its structure based on nine disulfide bonds as well as its resistance to heat and enzymatic hydrolysis, the allergenicity of this food protein is difficult to decrease by technological processes. We sought to reduce its allergenicity through the Maillard reaction. The unfolding of ovomucoid with l -cysteine-mediated reduction was used to increase accessibility to conformational and linear epitopes by modifying the secondary and tertiary structures of the allergen. Glycation with different saccharides revealed the beneficial effect of maltose glycation on the IgG-binding capacity reduction. By determining the better glycation conditions of unfolded ovomucoid, we produced ovomucoid with reduced IgE binding capacity due to the glycation sites (K17, K112, K129, and K164) on epitopes. Moreover, after simulated infant and adult gastrointestinal digestion, the unfolded plus glycated ovomucoid showed higher ABTS&z.rad; + scavenging activity, O2&z.rad; − scavenging activity, &z.rad;OH scavenging activity, Fe 2+ chelating activity, and a FRAP value; in particular, for &z.rad;OH scavenging activity, there was a sharp increase of more than 100%. The IgE binding ability of ovomucoid was sharply reduced by unfolding assisted glycation.