Functional properties of acetylated glutenin and gliadin at varying pH values

Applications of glutenin and gliadin in food products are limited as they cannot provide desirable functional properties. The objectives of this study were to improve the functional properties of glutenin and gliadin by acetylation using acetic anhydride and to study these properties at pH 3, 6 and 9. Under the experimental conditions, about 53.88% of glutenin and 28.46% of gliadin were acetylated. pH of the medium and acetylation of the proteins affected water solubility, water absorption, water holding capacity, emulsifying and foaming properties of the samples. The results of the sodium dodecyl sulfate polyacrylamide gel electrophoresis showed that high and low molecular weight glutenin subunits and ω-gliadins were affected by acetylation, while pH changes had no significant effect on the molecular weight of the proteins. Taken together, the results showed that acetylated glutenin and gliadin can be used as protein sources with good functional properties, particularly at alkaline pH.