Abstract

The foaming and emulsifying characteristics of proteins are important attributes during the production stage, storage, transport, and consumer perception of quality (appearance) of food dispersions (emulsions and foams). In this contribution, we are concerned with the analysis of interfacial, foaming, and emulsifying characteristics of a typical milk protein (sodium caseinate) as a function of protein concentration in aqueous solution ( C, % w/w). We have observed that there exists close relationships between foaming (power of foaming, foam capacity, foam density, and foam conductivity) and the rate of diffusion (slope of π vs. t 1/2) of caseinate to the air–water interface. The foam stability (quantified by the relaxation time ( t) due to drainage and disproportionation/collapse) correlates linearly with the equilibrium surface pressure ( π e) of aqueous solutions of caseinate. At surface pressures lower than that of monolayer saturation (at C<1×10 −3%, w/w) the foaming is zero. The emulsifying capacity (quantified by the droplet size and the specific surface area) was correlated with the protein concentration in solution (surface pressure at equilibrium). Coalescence was observed only at the lower caseinate concentration in solution ( C<0.1%, w/w). As a coherent protein layer (multilayer) saturates the interface, at higher protein concentrations, the emulsion instability is due to flocculation and/or creaming. The coalescence and creaming rates correlate well with the protein concentration in solution (thus with the surface pressure and/or surface dilatational modulus).

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