Model salad dressing emulsion stability as affected by the type of the lupin seed protein isolate

Model salad dressing emulsions of an oil volume fraction of 0.50 were prepared using two types of lupin seed protein isolate (LSPI) differing in the method applied for their isolation and their protein composition. The dressing stability against creaming and droplet coalescence were studied and correlated with data on oil droplet size, rheological characteristics and the amount of protein adsorption at the droplet surfaces. Model salad dressing emulsions containing the isolate, mainly composed of lupin globulins, exhibited higher stability and more pronounced rheological characteristics compared to those prepared with the isolate enriched in albumins or with the mixture of the two isolates. The lupin albumins appeared to displace the globulins from the droplet surfaces, following competitive adsorption from mixtures of the two types of the lupin isolates. The results are discussed in terms of droplet interaction and rearrangement as they are influenced by the presence of the adsorbed protein molecules and aggregates which appear to determine long-term stability of the emulsion systems. (c) 2006 Society of Chemical Industry.