Emulsifying Properties of Pea Globulins as Related to Their Adsorption Behaviors

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Abstract
Emulsifying properties of purified pea globulins and of vicilin‐legumin mixtures were evaluated through their emulsifying capacity, emulsifying activity index and stability of the resulting emulsions. The results were discussed by reference to the interface adsorption behaviors of these proteins. The influence of the vicilin/legumin ratio on the efficiency of pea isolates as emulsifying agents was also studied. Vi‐cilin which has been shown to be more surface active at air/water and dodecane/water interfaces, led also, in both cases, alone or mixed, to better emulsifying properties than legumin. The globulin composition of the isolates did not completely explain their emulsifying behaviors.