Interactions between different proteins and their technological importance for food systems.

Wheat proteins are the most consumed food proteins worldwide. Based on sequential extraction in various solvents, they are classified into albumins, globulins, gliadins and glutenins. The latter two fractions greatly determine the structure of wheat-based foods. They develop into gluten upon mixing with water, and form strong protein networks during baking, boiling or extrusion steps. It remains to be investigated how gliadin and glutenin react with each other. In non-cereal foods, albumins and globulins significantly contribute to physical properties of food. For instance, egg white albumins denature and form strong gels during heating. In e.g. cakes, egg noodles, and bread supplemented with milk or soy flour, mixtures of gluten proteins and considerable levels of albumins and globulins are subjected to high temperatures. However, it is not clear whether or to what extent gluten proteins react with albumins and globulins. The overall objective of the work is to study heat-induced reactions between albumins, globulins, gliadins and glutenins, of relevance for food systems.

Keywords:Water dynamics, Degradation, Cross-linking, Aggregation, Denaturation, Globulins, Albumins, Gluten proteins

Disciplines:Food sciences and (bio)technology