Precise control of aggregation morphology: Effective strategy to tune the properties of ovotransferrin particles.

Different aggregation morphologies of ovotransferrin (OVT) aggregates were successfully obtained through precise control, and the effects on structural, physical, liquid-liquid and gas-liquid interfacial characteristics as well as mechanisms were explored for the first time. It was observed that the surface hydrophobicity of OVT fibrils was higher than OVT spheres due to the acid-heat treatment. The exploration of liquid-liquid interface behaviors indicated that OVT fibrils possessed higher adsorption capacity at the interface, revealing the higher surface activity at the oil-water interface. During adsorption process, fibrils exhibited higher diffusion rate, while spheres were easier to penetrate and rearrange at the interface. The interfacial film composed of fibrils possessed more elastic solid-like behaviors owing to the higher surface activity of individual fibrous aggregates and rapid fibril-fibril interactions. The analysis of gas-liquid interface characteristics presented that OVT spheres possessed lower interfacial tension and higher interfacial viscoelasticity, and showed significantly higher FC and FS values in comparation to fibrils. These findings will facilitate the reader's understanding of the relationship between protein aggregate structure and properties, and lay a foundation for broadening the application of OVT and even other proteins.