Divergent temperature regulation of dough sheet extensibility driven by moisture threshold during mixing

Dough sheet extensibility is synergistically regulated by water addition and mixing temperature, yet their interaction mechanisms remain unclear. Employing water content (34%, 37%, 40%) and mixing temperature 4-45 °C, this study investigated dough sheet extensibility, water state and distribution homogeneity, glutenin-gliadin interactions, and gluten network structure. At 34% water content, extensibility first increased then decreased with mixing temperature, peaking at 25 °C. Conversely, at 40% condition, extensibility decreased monotonically by 29.66% from 4 °C to 45 °C. Mechanistically, mixing temperatures at 25 °C with 34% water condition optimized gluten network densification by increasing weakly bound water (increased 2.99% than 45 °C) and hydration homogeneity (reduced 30.94% CV than 45 °C). At 40%, low temperature (4 °C) suppressed free water surge (67.65% reduction) and protein depolymerization (25.08% LPP decrease), driving glutenin-gliadin crosslinking (23.81%/15.43% reduction in α/γ subunit extractability; 46.64% HMW-GS increase than 45 °C) to form hyper-branched networks. These insights establish quantitative processing windows: high-extensibility zone (40% water content + ≤15 °C), high-strength zone (34% water content + ≥35 °C), and balanced zone (37% moisture +4-35 °C).