The present study provided information about the interactions of rutin with soybean protein, and their impact of the foaming capacity and foaming stability of this plant-based protein. The foaming properties of the protein were appreciably increased after interacting with rutin, which was mainly ascribed to interacting of the proteins by the poly- phenols. As a result, the gas bubbles in the formed were protected by a thicker and more rigid interfacial layer, which inhibited bubble coa- lescence, disproportionation, or creaming. Thermodynamic analyses indicated that the binding interaction was spontaneous, with the main driving force being hydrophobic attraction. The interfacial tension (γ) was decreased when rutin/SPI complexes was formed, indicating that their foaming properties and emulsification ability was improved. The rutin/SPI complexes formed in this study may therefore be helpful in providing some basic information for forming the stable foams in many type of food products, such as beer heads. Nevertheless, the long-term stability of the foams requires further improvement before they can be used in many commercial applications.