The foamin
g characteristics of low-molecular-wei
ght emulsifiers (LMWEs) and proteins are important attributesdurin
g the production, stora
ge, transport, and consumer perception of quality (appearance) of food dispersions(emulsions and foams). In this article, we consider the analysis of interfacial (adsorption isotherm and rate ofadsorption) and foamin
g (foamin
g power and foam stability) properties of a typical milk protein(
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ges/
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globulin) and di
glycerol esters (di
glycerol monostearate and di
glycerol monolaurate) as LMWEs, asa function of the foamin
g a
gent concentration in aqueous solution. We observed that the adsorption andfoamin
g power (foam capacity,
gas and liquid retention in the foam, and foam density) increase with thefoamin
g a
gent concentration in the aqueous phase. The adsorption kinetics at short adsorption times is diffusion-controlled. However, the mechanism that controls the lon
g-term adsorption is the penetration of the foamin
ga
gent at the interface. At surface pressures lower than that of monolayer saturation, the foamin
g is zero. Aclose relationship was observed between foamin
g and the rate of diffusion of the foamin
g a
gent to the air-water interface. The foam stability, quantified by the relaxation times due to draina
ge (
td) and disproportionation/coalescence (
tdc), correlates with the equilibrium surface pressure (
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e) of the film adsorbed from aqueoussolutions of the foamin
g a
gent.