Effect of the Biopolymer Mixing Ratio on the Formation of Electrostatically Coupled Whey Protein−κ- and ι-Carrageenan Networks in the Presence and Absence of Oil Droplets
Ricky Sze Ho Lam, Michael T. Nickerson
Abstract
Ricky Sze Ho Lam, Michael T. Nickerson
Abstract
The rheological properties of 1.0% (w/w) whey protein isolate (WPI)-κ-/ι-carrageenan (CG) mixtures were investigated during a slow acidification process by glucono-δ-lactone from pH 7.00 to ∼4.20 as a function of biopolymer mixing ratio and in the presence and absence of oil droplets. In all cases, electrostatic coupled biopolymer and emulsion gel networks were formed at pH values corresponding to where attractive interactions between WPI and CG began. Formed WPI-CG complexes were found to be surface active, capable of lowering interfacial tension and forming viscoelastic interfacial films within emulsion-based systems. Both biopolymer and emulsion-based gels increased in strength and elasticity as the CG content increased, regardless of the type of CG present. However, WPI-ι-CG coupled networks were stronger than WPI-κ-CG networks, presumably due to the higher number of sulfate groups attracting the WPI molecules.
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The rheological properties of 1.0% (w/w) whey protein isolate (WPI)-κ-/ι-carrageenan (CG) mixtures were investigated during a slow acidification process by glucono-δ-lactone from pH 7.00 to ∼4.20 as a function of biopolymer mixing ratio and in the presence and absence of oil droplets. In all cases, electrostatic coupled biopolymer and emulsion gel networks were formed at pH values corresponding to where attractive interactions between WPI and CG began. Formed WPI-CG complexes were found to be surface active, capable of lowering interfacial tension and forming viscoelastic interfacial films within emulsion-based systems. Both biopolymer and emulsion-based gels increased in strength and elasticity as the CG content increased, regardless of the type of CG present. However, WPI-ι-CG coupled networks were stronger than WPI-κ-CG networks, presumably due to the higher number of sulfate groups attracting the WPI molecules.
Key concepts: Biopolymer, Whey protein isolate, Emulsion, Chemistry, Chemical engineering, Rheology, Whey protein, Surface tension