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 degrees C. The secondary structure of WISPs was determined to be as follows: beta-sheet: 49.33 %, random coil: 13.87 %, alpha-helix: 16.35 %, beta-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 degrees 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.