Interactions between whey protein isolate and gum Arabic

In this study we have attempted to understand the nature of " charge interactions" between two negatively charged biopolymers (whey protein isolate, WPI and gum Arabic, GA) and, consequently, why their mixture exhibits better interfacial activity. Surface tension (γ₀) measurements indicated that at ca. 1wt.% of the biopolymer mixture (3:1wt. ratio) the air/water surface is saturated. At 5wt.% the γ₀ of the mixture is lower than the calculated co-operative value. The ζ-potential measurements revealed that the isoelectric point of the WPI:GA 3:1. wt. ratio mixture is 3.8. The ζ-potential values up to pH 6 are below those calculated. Similarly, the electrical conductivities of the mixture are lower than those calculated. All these measurements indicate: (1) partial charge neutralization in spite of the fact that both biopolymers are negative or (2) partial charge-charge interactions between the two biopolymers. The thermal heating behavior of the frozen water in the aqueous mixture studied by DSC (heating cycle of the frozen sample) clearly indicates that the two biopolymers are interacting. We calculated the enthalpy, the free energy and the chemical potential of the interactions. We found that the interactions of the biopolymers are rather weak. They are likely derived from some local positively charged domains (pH 7) on the protein that neutralize some of the negatively charged GA. These interactions form weak charge adducts. These charge adducts are sufficient to improve its adsorption into the oil-water interface and enhance the emulsion stability.