RESUMO
This study aimed to investigate the structural and functional changes in polyhydroxy alcohol-mediated curing on pork myofibrillar proteins (MP). The results obtained from total sulfhydryl groups, surface hydrophobicity, fluorescence and Raman spectroscopies, and solubility demonstrated that the polyhydroxy alcohols (especially xylitol) significantly modified the MP tertiary structure, making this structure more hydrophobic and tighter. However, no significant differences were detected in the secondary structure. Furthermore, the thermodynamic analysis revealed that polyhydroxy alcohols could develop an amphiphilic interfacial layer on the MP surface, significantly increasing the denaturation temperature and enthalpy of denaturation (P < 0.05). On the other hand, the molecular docking and dynamics simulations showed that polyhydroxy alcohols interact with actin mainly through hydrogen bonds and van der Waals forces. Therefore, this could help reduce the effect of high-content salt ions on MP denaturation and improve the cured meat quality.
