Associative interactions between chitosan and soy protein fractions: Effects of pH, mixing ratio, heat treatment and ionic strength

The objective of this paper is to explore the complexation between the soy protein fractions (glycinin and β-conglycinin) and chitosan (CS) and to investigate the influence of pH, mixing ratio, heat treatment and ionic strength. Phase behavior and microstructure showed that soluble complex and coacervate were obtained in glycinin/CS and β-conglycinin/CS mixtures at specific pHs, following a nucleation and growth mechanism. Moreover, the coacervates showed higher thermal stability than protein alone. Specially, the glycinin/CS mixture displayed a gel-like network structure at pH 5.5 and 6.0, and this structure kept the mixture soluble at a long pH region. The turbidity versus ζ-potential pattern showed that, independent of protein, the self aggregation of soy protein fractions and the coacervation of glycinin/CS and β-conglycinin/CS mixtures were all obtained at charge neutralization pH, indicating that the ζ-potential is the most critical parameter to understand the stability of soy protein/chitosan mixture. This predictive parameter was less affected by mixing ratio and heating but was significantly affected by ionic strength because mixing ratio and heating only changed the equilibrium between repulsive and attractive forces in colloid system while sodium chloride destroyed the predictability of colloidal stability via shielding charged reactive sites on both biopolymers to disrupt electrostatic interactions.