Replication data for: Wheat gluten structure and (non-)covalent network formation during deep-fat frying

The aim of this work was to investigate wheat gluten protein network structure throughout the deep-frying process and evaluate its contribution to frying-induced microstructure development. Gluten polymerization, gluten-water interactions, and molecular mobility were assessed as a function of the deep-frying time (0 – 180 s) for gluten-water model systems of differing hydration levels (40 – 60 % moisture content). Results showed that protein extractability decreased considerably upon deep frying (5 s) due to glutenin polymerization by disulfide covalent cross-linking. Stronger protein-protein interactions were attributed to the breaking of hydrogen bonds and evaporation of water interacting with protein chains. Longer deep-frying resulted in progressively lower protein extractabilities in part due to gliadin co-polymerization by thiol-disulfide exchange reactions. The molecular mobility of gluten polymers was substantially reduced and gluten proteins gradually transitioned from the rubbery to the glassy state. The findings of this work demonstrate that the extent of gluten structural expansion as a result of deep-frying is dictated by the polymerization of the proteins and reduction in their molecular mobility.