Chemical characterization and functionality assessment of oat protein fractions

Protein fractions (albumins, globulins, prolamins, and glutelins) were prepared from oat seeds (variety Sentinel). Column chromatography on Sephacryl S-200 revealed that the four solubility fractions had unique polypeptide compositions and there was little cross contamination among the fractions. Isoelectric focusing on polyacrylamide gels resolved the fractions into a large number of bands covering a wide pH range. Differential scanning calorimetric studies showed that albumins and globulins had an endothermic peak at 87 and 110 °C, respectively, while prolamins and glutelins had no thermal response. Some functional properties of the solubility fractions were determined to assess the potential use of oat proteins as a food ingredient. Some fractions had high emulsifying, fat-binding, and water hydration capacities, and the albumins also had excellent foaming properties.link_to_subscribed_fulltex