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Electrostatic interaction between proteins and negatively charged polysaccharides leads to formation of stable colloidal system or causes complex coacervation. Therefore, in this study phase behavior of the mixtures of 0.4% milk proteins (sodium caseinate or whey protein isolate) with soluble fraction of tragacanth (up to 1%) or soluble fraction of Persian gum (up to 2%) as a function of pH (2–7) was investigated, in order to obtain appropriate protein:polysaccharide ratio to formation of soluble complexes in a wide range of pH. According to the results, the mixtures of sodium caseinate–soluble fraction of Persian gum, sodium caseinate–soluble fraction of tragacanth, whey protein isolate–soluble fraction of Persian gum and whey protein isolate–soluble fraction of tragacanth were soluble complexes at the whole pH range at the ratio of 0.4:0.6, 0.4:0.6, 0.4:2 and 0.4:1, respectively. Moreover, it was found that enhancement of total biopolymer concentration (at a same ratio) had no effect on the phase behavior of complexes. In addition, evaluation of the phase behavior of the mixture of milk proteins–alcohol-insoluble fraction of soluble part of native gums illustrated that both alcohol-insoluble and soluble fractions probably have impact on stability of complexes at mentioned ratios.

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Complex coacervation is generated through electrostatic interaction between oppositely charged biopolymers (proteins and polysaccharides). Complexation via electrostatic interactions can lead to formation of soluble or insoluble complexes. In the current research, the production and characteristics of the complexes formed from whey protein concentrate (WPC) and gum tragacanth (GT) were evaluated. In order to find the optimum pH for complexation, absorbance of protein-polysaccharide mixtures were measured at a wide range of pH (2–8), Furthermore, particle size, zeta potential, microstructure and rheological properties of the complexes were investigated. Based on the results, the best condition to form complex between WPC and GT was found to be at pH=4.5. With Increasing the amount of GT up to 0.75% w/w in a constant protein concentration (0.5% w/w), the lowest and highest particle size for WPC- GT complex was found at protein: polysaccharide ratio of 1: 1 (3018 nm) and 10:1 (4070 nm), respectively. Zeta potential changed from +3.11 mV (0% gum tragacanth) to -6.82 mV due to addition of GT (0.75% w/w). Microscopic images showed the presence of separate spherical particles, except at the concentration of 0.05% w/w. The appropriate rheological model to predict flow behavior of complexes was depended on protein-polysaccharide ratio and the dominate flow behavior index was found to be shear thinning. Increasing of TG concentration lead to lower flow behavior index as well as higher apparent viscosity, consistency coefficient and the yield stress