Abstract:[Objective]This study aims to investigate the effects of ginger protease on beef tenderness.[Method]Ginger protease was extracted from mature ginger via ammonium sulfate precipitation. The fundamental properties of the ginger protease, including enzyme activity, protein mass fraction, optimal temperature and pH, and relative molecular mass, were evaluated. Furthermore, the effects of ginger protease on the physicochemical properties, sensory quality, microstructure, and protein degradation characteristics of beef were examined.[Result]Ginger protease was mainly composed of two proteins with relative molecular masses of 15 293 and 34 191, with a total protein mass fraction of (574.60±0.25) mg/g, an enzyme activity of (31 787±307) U/g, an optimum temperature of 60 ℃, and an optimum pH of 6. Compared with the control group, 30 to 90 U/mL ginger protease significantly reduced the shear force, hardness, chewiness, and gumminess, while enhancing the lightness value without altering the water-holding capacity of beef. When enzyme activity is the same, there is no significant difference in the tenderness of beef treated with ginger protease and papain. The sensory evaluation results indicated that the ginger protease improved the sensory quality of beef. Microstructural analysis revealed that ginger protease disrupted the integrity of muscle structure. Protein degradation analysis indicated that ginger protease primarily improved beef tenderness by modifying collagens in beef, whereas papain improved beef tenderness through its effects on myofibrillar proteins, myogens, and collagens.[Conclusion] Ginger protease can be applied as an effective enzyme for meat tenderisation.
