Proteins, one of the vital nutritional compounds sensitive to the environment, can be modified by interaction with polyphenols. Ultrasonication has been applied for enhancing the functional properties of proteins. In this study, the interactions of gliadin (G) and rutin (R) in the absence and presence of ultrasonication (0, 150, 300, 450, and 600 W) for 20 min were investigated, with a focus on the properties of emulsions prepared by G-R complexes. Ultrasonication improved the interaction, which increased the content of β-type secondary structure. Ultrasonication at 450 W increased the particle size of the conjugates. For Pickering emulsions, treating the covering of R on G with ultrasonication improves the stability of the G-based emulsion significantly, owing to the strong films formed on the oil-water interfaces. The G-R complexes treated at 450 W ultrasonication formed emulsions that showed higher potential and storage modulus (G') and denser microstructures than those of the untreated emulsions. Nevertheless, ultrasound treatment at 600 W weakened the emulsion properties that were stabilized by the conjugates. Ultrasound combined R was shown to be a potential processing technology for changing the protein structure and producing stable emulsions. PRACTICAL APPLICATION: The interactions between proteins and polyphenols are able to preserve the stability of the functional compounds, allow targeted and controlled release, and improve the texture of these complexes employed in the food industry. Improvements in the functional characteristics of the protein-polyphenol complexes so that they possess high emulsifying stability during food processing is a crucial factor for employing them in the food industry. Therefore, the aim of this research is using a soluble complex of gliadin-rutin for the development of its functional characteristics.
Keywords: emulsions; gliadin; rheological properties; rutin; ultrasonication.
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