Elevating the critical gelling concentration of soy protein by disulfide bond cleavage during preheating treatment.

There has been a growing demand for the development of high protein beverages in the food industry. However, during thermal processing, high-protein beverages undergo protein aggregation and gelation. In this study, thermostable soy protein was prepared by disulfide bond cleavage combined with preheating treatment. Thermostable soy protein had a higher denature extent than the control sample, which prevented the formation of larger aggregates upon reheating. Thermostable soy protein possessed lower viscosity (nearly 0 Pa·s) and an excellent fluidity index (around 0.8) after reheating at a concentration of 10 % (w / v), whereas the control sample had gelled. Moreover, rheology and dynamic light scattering collectively demonstrated that a minimum of 2.5 mM sodium metabisulfite (Na 2 S 2 O 5) was required to prepare thermostable protein solutions. The present study shows an innovative method to produce thermostable soy protein. Flowchart for Modified Protein Preparation. Diagram of Chemical Mechanism of Reductant Modification. [Display omitted] • Reducing and heat combined treatment was effective in preparing stabilized soy protein. • Combined treatment endowed proteins with larger particle size and denaturation degree than natural proteins. • Modified proteins (10 wt%) exhibited good fluidity and resisted gelling during heating. [ABSTRACT FROM AUTHOR]