Abstract
Food processing conditions affect the structure, solubility, and therefore accurate detection of gluten proteins. We investigated the influence of dough, bread, and pretzel making on the composition of different wheat protein fractions obtained by Osborne fractionation. The albumin/globulin, gliadin, and glutenin fractions from flour, dough, crispbread, bread, and pretzel were analyzed using RP-HPLC, SDS-PAGE, and untargeted nanoLC-MS/MS. This approach enabled an in-depth profiling of the fractionated proteomes and related compositional changes to processing conditions (mixing, heat, and alkali treatment). Overall, heat treatment demonstrated the most pronounced effect. Label-free quantitation revealed significant changes in the relative abundances of 82 proteins within the fractions of bread crumb and crust in comparison to flour. Certain gluten proteins showed shifts or reductions in particular fractions, indicating their incorporation into the gluten network through SS and non-SS cross-links. Other gluten proteins were enriched, suggesting their limited involvement in the gluten network formation.