Aggregate Size Modulates the Oil/Water Interfacial Behavior of a Myofibrillar Protein: Toward the Thicker Interface Film and Disulfide Bond.

Myofibrillar protein (MP) aggregate models have been established to elucidate the correlation between their aggregate sizes and interfacial properties. The interfacial layer thickness was measured by the polystyrene latex method and quartz crystal microbalance with dissipation measurement. Interfacial conformations were then characterized in situ (front-surface fluorescence spectroscopy) and ex situ (reactive sulfhydryl group and secondary structure measurement following MP displacement). The viscoelasticity of the interfacial film and its resistance to surfactant-induced competitive displacement were reflected by the dilatational rheology and dynamic interfacial tension with the bulk phase exchange. Finally, we compared the findings of competitive displacement before/after adding a sulfhydryl-blocking agent, N -ethylmaleimide, to highlight the role of S-S linkage on interfacial film formation and stability. We substantiated that the aggregate size of the MP governed their interfacial properties. Small-sized aggregates exhibited more ordered secondary structures on the oil-water interface, which was conducive to the adsorption ratio of the protein and the adsorption dynamics. Although larger aggregates lowered the diffusion rate during interfacial film formation, they allowed the thicker and more viscoelastic interfacial film to be constructed afterward through more disulfide bond formation, resulting in greater resistance to surfactant-induced competitive displacement.