Evolution of the morphological, structural, and molecular properties of gluten protein in dough with different hydration levels during mixing

To understand the formation process of dough with different hydration levels upon mixing and the response of dough rheology, the dynamic evolution of gluten protein was tracked and quantified at morphological, structural, and molecular levels. Both macroscopical and microscopic distribution images showed that partial and full hydration induced quick formation of a more compact gluten network compared with limited hydration. Gluten network in highly hydrated samples was more susceptible to the formation and collapse induced by mechanical force. SE-HPLC results indicated significant depolymerization of glutenin macropolymer (GMP) in fully and partially hydrated samples. Sufficient mixing was accompanied by the increase of ionic and hydrogen bonds, while excessive mixing increased exposure of free -SH. Higher hydration level induced more ordered secondary structure. Correlation and principal component analysis revealed the patterns and dynamics of gluten evolution during dough formation with different hydration levels, and their contribution to the changes in dough modulus.