Protein/Emulsifier Interactions

  • Martin Bos
  • Tommy Nylander
  • Thomas Arnebrant
  • David C. Clark


Many food emulsions are more complex than the traditional definition of an emulsion: a colloidal dispersion of liquid droplets in another liquid phase. This is mainly because the dispersed phase is often partially solidified or the continuous phase may contain crystalline material, as in ice cream. However, one characteristic that all emulsions have in common is that they are (thermodynamically) unstable. The four main mechanisms that can be identified in the process of breaking down an emulsion are creaming, flocculation, coalescence, and Ostwald ripening. There are two ways in which the process of breakdown of an emulsion can be influenced. First, use of mechanical devices to control the size of the dispersion droplets and second, the addition of stabilizing chemical additives like low molecular weight emulsifiers and polymers to keep it dispersed. The main purpose of the latter is to prevent the emulsion droplets from fusing together (coalescence), often achieved by repulsive droplet/droplet interactions. These interparticle interactions are determined mainly by the droplet surface, which is coated with emulsifiers, often biologically surface-active components like proteins, mono- and diglycerides, fatty acids, or phospholipids. The forces most commonly observed are electrostatic double layer, van der Waals, hydration, hydrophobic, and steric forces. They are responsible for many emulsion properties including their stability.


Colloid Interface Adsorbed Protein Phosphatidic Acid Competitive Adsorption Emulsion Droplet 


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Copyright information

© Springer Science+Business Media Dordrecht 1997

Authors and Affiliations

  • Martin Bos
  • Tommy Nylander
  • Thomas Arnebrant
  • David C. Clark

There are no affiliations available

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