Abstract
AbstractAn ultrastructural comparison is given for dispersions of a protein isolate (FBPI) from faba beans (Vicia faba L.) and its highly acetylated derivative (AFBPI) as well as for various o/w emulsions stabilized by FBPI and AFBPI. Both protein isolates contain substantial amounts of surface‐active phospholipids (about 3%) which occur as vesicles (diameter 30 … 500 nm). Their membranes and rather cores contain protein. Interfacial protein layers of Triolein/Water‐emulsion droplets possess smooth external surfaces and rather coarse internal surfaces with peculiar paracrystalline structured areas. Tangible differences are found in the droplet‐size distribution and ultrastructure of sunflower‐oil/water emulsions due to both the homogenization process (high pressure homogenizer or ultrasonic disintegrator) and the acetylation of the isolate. The modification by acetylation increases the emulsifying activity of the isolate and prevents the strong aggregation of oil droplets observed in FBPI‐stabilized emulsions.
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