Interaction between protease from Staphylococcus epidermidis and pork myofibrillar protein: Flavor and molecular simulation

This study investigated the influence of a protease from Staphylococcus (S.) epidermidis on the hydrolysis and flavor development in pork myofibrillar protein (MP). The surface hydrophobicity, fluorescence, Fourier transform infrared spectra, and atomic force microscopy analysis indicated that hydrolysis significantly changed surface hydrophobicity and secondary structure of MP (p < 0.05), and improved the stability of MP in water. The contents of free amino acid from MP, especially glutamic and alanine, significantly increased (p < 0.05), and the production of volatile compound such as aldehydes, alcohols and acid were promoted under the action of protease. MP treated with S. epidermidis protease is non-cytotoxic to the HEK-293 cells. Molecular docking analysis suggested that the interaction between the protease and actin was spontaneous and mainly involved hydrogen bonding forces. In summary, this study provides a theoretical basis for the future application of S. epidermidis protease in fermented meat products.