Figure 8

Enzymatic characteristics of rTsPPase (ATP as substrate). A Enzymatic activity at temperature 25–70 °C, the best temperature was 50 °C. B Optimum pH at 50 °C, and the optimum pH was 6.0. C, D Enzymatic activity at various Mg²⁺ concentrations (1–25 mM) at 50 °C and pH 6.0. The best activity was observed at 8 mM Mg²⁺. E Different divalent cation effects on the enzyme activity were compared, the result showed that the ability of Mg²⁺ was the strongest. F Michaelis–Menten curve and Lineweaver–Burk Plot at pH 6.0, 50 °C and 8 mM Mg²⁺. The K_m value was deduced to 108 μM due to the X axis intercept which represent − 1/K_m.