The effect of pH on textural properties of native and acetylated glten, gliadin and glutenin by cluster analysis

Wheat gluten is one of the most important plant proteins of fairly low price consisting of glutenins and  gliadins. The hydrophobic nature and low water solubility of gluten has limited its applications in many food and non-food products. In order to improve the applications of gluten, it was first fractionated into its main components; gliadins and gluteneins and then they were acetylated using acetic anhydride. In the next stage, the rhelogical properties of these proteins at different pH values (3, 6 and 9) were compared with their corresponding controls. The pH had a great impact on the degree of acetylation. Glutenin had the highest, while gliadin had the lowest degree of acetylation at different pH values. Moreover, all these proteins were de-aceytelated at pH 3. Hardness, gumminess, chewiness and elasticity of the acetylated gluten and glutenin decreased significantly at pH 3.