Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of ovalbumin: Tracing of advanced glycation end-products and immuno-active peptides

Abstract

Currently, the biological consequences of advanced glycation end-products (AGEs) and their link to the antigenicity of food allergens are largely unknown due to the uncertainty in their digestive fates within the body. In this study, the influence of glycation derived from α-dicarbonyl compounds (α-DCs), precursors of AGEs, on digestive behaviors of ovalbumin (OVA) was investigated in a two-step simulated gastrointestinal (GI) model. Methylglyoxal (MGO), glyoxal (GO), and 3-deoxyglucosone were selected as typical α-DCs to obtain glycated OVA with different AGE-modifications (AGE-Ms). It was unveiled that α-DC-glycation reduced the digestibility of OVA via blocking tryptic cleavage sites and inducing steric hindrance, especially seen in the GO- and MGO-OVA groups. The formed AGE-Ms, depending on the precursor type, showed masking effects on the epitopes of OVA, which counteracted the negative effects of reduced digestibility on its antigenicity. Substantial changes in the peptide release patterns were also noted in glycated OVA, including alterations in the sequences and structures of several known protease-resistant epitopes of OVA. This study provides new insights into the nutritional and healthy effects of MRPs in heat-processed foods, as well as their potential connection to the modulation of egg allergy.

Keywords: Advanced glycation end-products; Digestibility; Glycated structure; Immuno-active epitopes; Ovalbumin; α-dicarbonyls.