Abstract
The effect of processing, and heat in particular, on the wheat gluten proteins can be difficult to explain due to its complex, and often unusual, rheological and biochemical properties. Heat denaturation of wheat gluten proteins and the accompanying rheological changes, together with a number of interactions, such as hydrogen bonding, SS bonding and hydrophobic interactions have an effect on the native structure of the protein. During the heat treatment of gluten, denaturation, aggregation and cross-linking all combine to give rise to a series of changes that affect rheological and biochemical properties alike. Different components of gluten might exhibit different responses to heat treatment, based on their parent wheat variety, their size, their composition, or the environment the heat treatment took place. Today's food scientists are yet to fully understand all the interactions and mechanisms involved in the effect of heat on gluten but this field of research has grown enormously over the last few decades and continuously expands offering us a better insight and understanding.