A Comparison of the Functional and Interfacial Properties of β-Casein and Dephosphorylated β-Casein

New views on foams from protein solutions

“…Apparently the relationships defined are not necessarily cause-effect relations. As a result, there are also many reported examples where these relations are not found [66] [67,68 • ]. Ipsen et al studied the interfacial and foam properties of hydrolysates of β-lactoglobulin [67].…”

The Effects of Caseinate Submicelles and Lecithin on the Thin Film Drainage and Behavior of Commercial Caseinate

“…The decrease in film thickness of caseinate and reconstituted caseinate above 35°C may be as a result of further lipid protein interactions arising from increased lipid hydration and phase transition as discussed earlier. The film thickness of extracted caseinate is much higher than that previously observed for ␤-casein (12). This may be due to the association of ␣-casein with ␤-casein creating a larger charge repulsion between thin film surfaces than ␤-casein alone.…”

“…This may be due to the association of ␣-casein with ␤-casein creating a larger charge repulsion between thin film surfaces than ␤-casein alone. Decreasing the charge of ␤-casein by dephosphorylation resulted in a decrease in film thickness (12). Localized thinning of extracted caseinate above 35°C, coupled with the presence of very slow surface lateral diffusion (D ϭ 10 Ϫ9 cm 2 /s), suggests that there may still be a small amount of lipid, with a relatively high phase transition temperature, remaining in the extracted sample.…”

Protein-lipid interactions at interfaces

“…By increasing the overall charge on a dispersed phase droplet through the charge of the adsorbed protein the dispersion can be stabilised by the electrostatic repulsion of the droplets hindering their close approach. Reduction of the charge can have drastic effects on dispersion stability (Husband et al, 1997). Similarly, the presence of large hydrophilic loops or tails can provide a steric hindrance to particle encounter.…”