Parameters such as interfacial tension, dynamics, and rheology are intricately linked to the emulsifying and foaming properties of proteins. In this study, the effects of different Tween types and concentrations on the structure and interfacial characteristics of ovalbumin (OVA) were examined, and their relationships with emulsifying and foaming properties were explored. The results showed that the addition of Tween caused the structure of OVA to become looser and more disordered (β-sheets gradually transformed into β-turns) and exposed more hydrophobic groups. In addition, with the increase in Tween concentration, OVA-Tween systems exhibited lower interfacial tension and could adsorb more rapidly at both the air-water and oil-water interfaces. Additionally, the interfacial elastic modulus of these systems also increased. Compared with natural OVA (EAI = 4.023 m