Figure 7

Enzymatic characteristics of rTsPPase (PPi as substrate). A Enzymatic activity at temperature 25–70 °C, the optimal temperature was 50 °C. B Optimum pH at 50 °C, and the optimum pH was 7.5. C Enzymatic activity at various Mg²⁺ concentrations (1–25 mM) at 50 °C and pH 7.5. The highest activity was observed at 5 mM Mg²⁺. D Different divalent cation effects on the enzyme activity were compared, the result showed that the ability of Mg²⁺ was the strongest. E The enzymatic activity of rTsPPase was obviously inhibited by the inhibitors NaF and IDP with a dose-dependent mode. F Michaelis–Menten curve and Lineweaver–Burk Plot at pH 7.5, 50 °C and 5 mM Mg²⁺. The K_m value was deduced to 170 μM due to the X axis intercept which represent − 1/K_m.