In the context of replacing animal proteins in food matrices, rice proteins (RP) become promised because they come from an abundant plant source, are hypoallergenic, and have high digestibility and nutritional value. However, commercial protein isolates obtained by spray drying have low solubility and poor functionality, especially in their isoelectric point. One way to modify these properties is through interaction with polysaccharides, such as gum arabic (GA).
View Article and Find Full Text PDFRice protein isolates (RPI) are promising plant-protein sources but present low solubility and poor surface activity in neutral conditions. Improving these characteristics is a crucial challenge to capitalize on them. This is the first work performing pH-shifting, ultrasound, and heat treatments on a commercial RPI.
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