The interfacial behaviour of three food proteins studied by the drop volume technique

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Abstract
The adsorption behaviour of three food proteins, a soy protein isolate, a sodium casein‐ate and a whey protein concentrate, at the air‐water interface has been studied by the drop volume method. The kinetics of surface tension decay were evaluated in terms of different rate‐determining steps at different ionic strengths and concentrations. This analysis indicates the following characteristics concerning the surface behaviour of the protein systems studied. The soy proteins diffuse slowly to the interface compared to the other proteins, probably due to the large particle size of the association complex of soy proteins. For the soy proteins, diffusion is slower in distilled water than in 0.2M‐NaCl solution and spreading of molecules at the interface is most easily performed in 0.2M‐NaCl solution. The whey proteins diffuse quickly to the interface, which is in accordance with their aqueous association; mainly small molecular complexes. Diffusion is slower and spreading easier in distilled water than in 0.2M‐NaCl solution. Although the caseinate has a complex quaternary structure, like the soy proteins, it has a very different surface behaviour. The diffusion step is rapid at concentrations above 10−3 wt % and contributes to a large extent to the interfacial tension decay, especially when the caseinate is dispersed in 0.2M‐NaCl solution. At a concentration of 10−3 wt % and below, the rate of the diffusion step is slowed down drastically, with an accompanying drop in the surface activity of the protein. This type of surface behaviour can be explained if the migration of the caseinates to the interface takes place via the casein monomers in the bulk phase.