Effects of Tweens on the Structure, interfacial Characteristics, and emulsifying and foaming properties of Ovalbumin

[Display omitted] •Tween made the structure of OVA unfolding and exposed more hydrophobic groups.•OVA and Tween competed adsorption on the interface upon high concentration Tween.•Emulsifying and foaming ability of OVA-Tween was improved but stability was impaired.•Order of emulsifying and foaming property was OVA-T20 > OVA-T40 > OVA-T80 > OVA-T60.•Correlation existed among structure, interface, and function properties of OVA-Tween. 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 m2/g, FA = 60.00 %), OVA-Tween showed significantly enhanced emulsifying and foaming abilities. However, higher Tween concentrations (0.1 %) led to competitive adsorption between OVA and Tween, inducing a reduction in the interfacial modulus and a slight decrease in the emulsifying and foaming stability. The emulsifying and foaming performance of the four composite systems were as follows: OVA-Tween 20 > OVA-Tween 40 > OVA-Tween 80 > OVA-Tween 60. Correlation analysis revealed a significant association between the structure and interfacial properties and the emulsifying and foaming performance of OVA-Tween (p