This study aimed to assess the effect of an external protease secreted by Staphylococcus (S.) xylosus on the hydrolysis and flavor properties of meat protein. The results indicated that the protease significantly increased the solubility of myofibrillar proteins (MPs) and sarcoplasmic proteins (SPs) in water (P < 0.05), and altered their surface hydrophobicity and secondary structure. The results of micromorphological and free amino acids analyses suggested that the protease degraded the large and insoluble meat protein aggregates into small molecular proteins with uniform distribution and amino acids, especially glycine, glutamic acid, leucine, and cysteine. Moreover, the protease-catalyzed hydrolysis promoted the formation of some volatile compounds in the MPs and SPs. Additionally, molecular docking analysis suggested that hydrogen bond and hydrophobic interaction promoted the formation of a S. xylosus protease/meat protein complex. These results provided a basis for the future application of S. xylosus protease in meat products.
Keywords: Conformation; Flavor; Meat protein; Molecular docking; Staphylococcus xylosus protease.
© 2024 The Authors.