Isolation of ice structuring proteins from winter wheat in frigid region (Dongnongdongmai1) and the effect on freeze–thaw stability of dough

In this study, ice structuring proteins (WISPs) extracted from winter wheat in a frigid region were prepared and added to frozen-thawed dough. The WISPs were characterized, revealing that they contained a higher proportion of hydrophilic amino acids and had a molecular weight of approximately 15 kDa. The highest thermal hysteresis activity (THA) observed was 0.62 °C. The secondary structure of WISPs was determined to be as follows: β-sheet: 49.33 %, random coil: 13.87 %, α-helix: 16.35 %, β-turn: 20.45 %. The study investigated the effects of different additions of WISPs on the water mobility, glass transition temperature, microstructure, rheological properties, and texture analysis of frozen-thawed dough. The results demonstrated that the inclusion of WISPs reduced the fluidity of water and water migration in the dough during the frozen-thawed cycle. This protective effect preserved the internal structure and gluten network of the dough, leading to increased viscosity, elasticity, and improved texture properties of the frozen-thawed dough. Furthermore, the addition of WISPs at concentrations ranging from 0 % to 0.7 % resulted in a 1.8 °C increase in the glass transition temperature (Tg). Overall, these findings suggest that WISPs can serve as a beneficial additive for enhancing the freeze–thaw stability of dough.