The impact of disulfide bond dynamics in wheat gluten protein on the development of fermented pastry crumb

•Large, non-spherical gas bubbles are present in the separate fermented dough layers.•Fermented pastry crumb structure strongly depends on wheat gluten protein disulfide bond dynamics.•Steam entrapment during baking is of limited importance for fermented pastry dough lift.•(Disulfide bond) interconnections between separate dough layers prevent pastry collapse during baking.

Gluten proteins functionality during pastry production was examined by including redox agents in the ingredient bill. Addition of reducing and oxidizing agents respectively increased and decreased dough height during fermentation. The presence of large gas bubbles in the samples with oxidizing agents may have caused a 'stacking'-effect and a more effective dough lift. During baking, the level of extractable proteins decreased to comparable values for all samples, except when potassium iodate (KIO3) was used in the recipe. As a result of its use, a lower level of gliadin was incorporated into the gluten polymer and dough layers tended to 'slide' apart during baking, thereby causing collapse. Most likely, KIO3 caused glutenin oxidation within each individual dough layer to such extent during the dough stage that insufficient thiol groups were available for forming dough layer interconnections during baking, after margarine melting. Furthermore, addition of redox agents impacted the product's crumb structure.