Phase model interpretation of the structural properties of two molecular soy protein fractions

Abstract

The structural properties of mixtures of two molecular soy fractions, 11S (glycinin) and 2S, were investigated in the presence of glucono-δ-lactone (GDL) during an isothermal run at 25°C for 1500 min. Analytical methodology included small-deformation dynamic oscillation, visual observations, scanning electron microscopy, and blending-law modeling. The aim of the work was to identify the state of phase separation and the pattern of solvent distribution between the two constituent polymers. It was found that the high molecular weight distribution of 11S supported rapid kinetics of structure formation, with this continuous matrix being concentrated and, hence, further reinforced in the presence of small additions of 2S. Blending-law modeling suggested that 2S was able to retain disproportionate volumes of solvent within its phase. A consequence of such property was that high additions of 2S leading to equal concentrations of the two molecular fractions in the blend resulted in a catastrophic drop in the values of the overall network strength. This behavior is rather unexpected for the structural properties of a phase-separated system, and it has been rationalized on the basis of the high water-holding capacity of the small molecular weight fraction. 2S entraps in its phase the polymeric segments of glycinin, which are then unable to become structural knots of a cohesive three-dimensional morphology observed in single 11S preparations. © 2008 American Chemical Society.