Revealing protein aggregation behaviour and dispersion properties induced by molecular interactions between sucrose...

The effects of sucrose esters (SE) with varying hydrophilic-lipophilic balance (HLB) values (SE 11, 13, 15) and different concentrations (0.01, 0.1, 1.0 mM) on the dispersion properties and structure of myofibrillar proteins (MPs) in the aqueous phase were investigated. The results demonstrated that the SE 11 and SE 13 reduced the particle size and enhanced the distribution uniformity of the MPs. All of the SE exhibited a slight reduction in the ζ-potential absolute values of the MPs. Meanwhile, the SE 11 significantly reduced the turbidity of the MPs, especially in the 0.1 mM group. Macroscopic and microscopic images showed that the optimum dispersion state was in the SE 11-0.1 group. Furthermore, the interactions between SE and MPs exerted a significant impact on the proteins structure. The SE 13 and SE 15 caused significant changes, which presented concentration correlation, in the tertiary and secondary spatial structures of the MPs. Nevertheless, slight structural changes were observed in MPs with different SE11 concentrations. The SE did not alter the molecular weight of the MPs, i.e. it did not induce irreversible aggregation, nor degradation of the proteins. These results were verified by the surface hydrophobicity, UV-Vis spectroscopy, intrinsic fluorescence, circular dichroism, and SDS-PAGE. Molecular docking simulation showed that hydrophobic interactions and hydrogen bonds were the main interaction force between SE 11 and MPs. Therefore, our findings provided meaningful insights into the dispersion state of the MPs aqueous containing SEs and contributed to the practical application of non-ionic surfactants in meat protein processing.