Multi-spectral and proteomic insights into the impact of proanthocyanidins on IgE binding capacity and functionality in soy 11S protein during alkali-heating treatment

Abstract

This study evaluated the impact of proanthocyanidins on immunoglobulin E (IgE) binding capacity, antioxidant, foaming and emulsifying properties in soy 11S protein following alkali treatment at 80 °C for 20 min. The formation of >180 kDa polymer was observed in the combined heating and proanthocyanidins-conjugation treatment sample (11S-80PC) rather than in the heating treated sample (11S-80) using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The structural analyzes demonstrated that 11S-80PC exhibited more protein unfolding than 11S-80. Heatmap analysis revealed that 11S-80PC had more alteration of peptide and epitope profiles in 11S than in 11S-80. Molecular docking showed that PC could well react with soy protein 11S. Liquid chromatography tandem MS analysis (LC/MS-MS) demonstrated that there was a 35.6 % increase in 11S-80, but a 14.5 % decrease in 11S-80PC for the abundance of total linear epitopes. As a result, 11S-80PC exhibited more reduction in IgE binding capacities than 11S-80 owing to more obscuring and disruption of linear and conformational epitopes induced by structural changes. Moreover, 11S-80PC exhibited higher antioxidant capacities, foaming properties and emulsifying activity than 11S-80. Therefore, the addition of proanthocyanidins could decrease allergenic activity and enhance the functional properties of the heated soy 11S protein.