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Due to their physicochemical characteristics, proteins can be used as emulsifiers. The demand for vegan foods associated with the nutritional benefits conferred by rice proteins justifies their production on a commercial scale. However, the technological potential of rice proteins has not been fully investigated. In order to allow the use of commercial rice proteins as a technological ingredient, the functional properties (solubility and interfacial property) at pH 3, 5 and 7 of commercial rice protein concentrate (CRP) were investigated. O/W emulsions stabilized by CRP under the following pretreatments were studied: thermal (85 ° C / 1h) (CRP-T) and ultrasound (450W / 10min) (CRP-U). Protein without pretreatment (CRP-C) was used as a control. The CRP showed low activity at the O/W interface regardless of the pH. This result could be related to low CRP solubility (<10%) for the three pH values considered. For emulsions stabilized by CRP-C, the largest droplet size (~35 µm) was associated with their low stability. Emulsions stabilized by CRP-T and CRP-U showed significantly smaller droplet size and higher kinetic stability when compared to emulsions stabilized by untreated CRP. This result can be attributed to the conformational changes in the three-dimensional structure of CRP caused by the treatments that resulted in increased solubility. CRP-T and CRP-U samples stabilized the emulsion interface resulting in the formation of individual droplets, while aggregates around the oil droplets were observed for CRP-C emulsions. CRP proteins are a promising class of emulsion stabilizing particles as they are edible materials based on renewable and natural resources. In addition, CRP can also be used in the development of conventional O/W emulsions, since it has been possible to modify its interfacial property through pretreatments.
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