Investigation of the behavior of wheat flour dough under different sheeting-resting cycles and temperatures: Large deformation rheology and gluten molecular interactions

The molecular mechanisms underlying the structural changes in wheat flour dough subjected to repeated sheeting-resting treatments at two temperatures were investigated. The results revealed that alternating calendering and resting processes significantly contributed to the formation of a well-developed and organized gluten network, thereby enhancing the dough's resistance to deformation. Multiple complex treatments in a low-temperature environment promoted the formation of small aggregated proteins and monomeric proteins. In contrast, treatments at a high-temperature environment facilitated the formation of large aggregated proteins, reaching a maximum of 23.58 mg/g. The contribution of ionic and hydrogen bonding was maximum in the dough after two and three alternating treatments in both low- and high-temperature environments, while the strength of hydrophobic interactions remained weak. Furthermore, a combination of noncovalent interactions and sulfhydryl disulfide bond transitions induced notable changes in the structure of the glutenin molecular chain.