Department of Food and Bioproduct Sciences, University of Saskatchewan , 51 Campus Drive, Saskatoon, Saskatchewan, Canada S7N 5A8.
J Agric Food Chem. 2014 Aug 27;62(34):8730-9. doi: 10.1021/jf5023669. Epub 2014 Aug 13.
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.
1.0%（w/w）乳清蛋白分离物（WPI）-κ-/ι-卡拉胶（CG）混合物的流变性在通过戊二酸-δ-内酯从 pH 7.00 缓慢酸化至约 4.20 的过程中进行了研究，这是作为两种生物聚合物混合比例的函数，并在存在和不存在油滴的情况下进行了研究。在所有情况下，均在 WPI 和 CG 之间的吸引力相互作用开始的 pH 值处形成静电偶联的生物聚合物和乳液凝胶网络。发现形成的 WPI-CG 复合物具有表面活性，能够降低界面张力并在基于乳液的系统中形成粘弹性界面膜。无论存在哪种类型的 CG，随着 CG 含量的增加，生物聚合物和基于乳液的凝胶的强度和弹性都增加了。然而，WPI-ι-CG 偶联网络比 WPI-κ-CG 网络更强，这可能是由于更高数量的硫酸基团吸引 WPI 分子。
