Wheat gluten structure and (non–)covalent network formation during deep-fat frying.

[Display omitted] • Gluten proteins polymerize mainly by disulfide cross-linking during deep-frying. • Deep-frying results in a denser gluten protein network. • Molecular mobility and protein polymerization contribute to structure expansion. • The gluten network structure does not depend on the initial hydration level. 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 micro- and macrostructure 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 gluten protein extractability decreased considerably upon deep frying (5 s) mainly due to glutenin polymerization by disulfide covalent cross-linking. Stronger gliadin and glutenin protein–protein interactions were attributed to the formation of covalent linkages and evaporation of water interacting with protein chains. Longer deep-frying (> 60 s) resulted in progressively lower protein extractabilities, mainly due to the loss in gliadin protein extractability, which was associated with gliadin co-polymerization with glutenin by thiol-disulfide exchange reactions. The mobility of gluten polymers was substantially reduced during deep-frying (based on the lower T 2 relaxation time of the proton fraction representing the non-exchanging protons of gluten) and gluten proteins gradually transitioned from the rubbery to the glassy state (based on the increased area of said protons). The sample volume during deep-frying was strongly correlated to the reduced protein extractability (r = –0.792, p < 0.001) and T 2 relaxation time of non-exchanging protons of gluten proteins (r = –0.866, p < 0.001) thus demonstrating that the extent of gluten structural expansion as a result of deep-frying is dictated both by the polymerization of proteins and the reduction in their molecular mobility. [ABSTRACT FROM AUTHOR]