Tomiko Asakura and co-workers, University of Tokyo, Japan, have used surface plasmon resonance to evaluate the continuity of taste by monitoring the interaction of food proteins with a lipid bilayer that mimics the tongue’s epithelial lingual cells.

Samples were classified as those that gradually bind to and interact strongly with the lipid bilayer, and those that interacted weakly, with fast binding and release and no additive effects. Sweet proteins and gymnemic acids that prolong sweet perception were categorized as strongly interacting with the liposome, as were milk proteins. Egg proteins, carbohydrates, and aspartame, were shown to interact weakly.

The authors suggest that strong interaction with the lipid bilayer generates longer continuity as, for example, gymnemic acid is retained on the epithelial cells of the tongue. It can then be dissolved by saliva, enter the pores of the taste buds and inhibit the binding of sweeteners to sweet taste receptor T1R over a prolonged period.

Image: (c) Purestock

• Surface Plasmon Resonance Analysis on Interactions of Food Components with a Taste Epithelial Cell Model
  M. Miyano, H. Yamashita, T. Sakurai, K. Nakajima, K. Ito, T. Misaka, Y. Ishimaru, K. Abe, T. Asakura,
  J. Agric. Food Chem. 2010.
  DOI: 10.1021/jf102573w