Dc. Clark et al., DIFFERENCES IN THE STRUCTURE AND DYNAMICS OF THE ADSORBED LAYERS IN PROTEIN-STABILIZED MODEL FOAMS AND EMULSIONS, Faraday discussions, (98), 1994, pp. 253-262
Protein-stabilized food dispersions often contain a range of surface a
ctive species. Many of these are of low molecular weight and include l
ipids or food emulsifiers. Depletion measurements, fluorescence and fl
uorescence recovery after photobleaching (FRAP) studies have shown tha
t competitive adsorption of these molecules at the interface causes br
eakdown of protein-protein interactions in the adsorbed layer. This re
sults in partial displacement of adsorbed protein and the initiation o
f lateral diffusion in the remaining adsorbed fraction However, there
are distinct differences between the structure of the adsorbed protein
layers found at air/water and oil/water interfaces. This causes diffe
rences in behaviour of the adsorbed layer in response to competitive a
dsorption of low-molecular-weight surfactant. This paper contrasts the
behaviour of adsorbed layers formed by the milk proteins, beta-lactog
lobulin and beta-casein, adsorbed at the interfaces of air-suspended t
hin liquid films and the thin aqueous him between two oil droplets, as
a function of increasing concentration of the non-ionic surfactant, T
ween 20.