Fig. 9
Kinetic properties of the purified L-GLS activity under various conditions. (A) This graph illustrates the effect of pH on enzyme activity. Enzyme activity increases steadily from pH 5 to 8, indicating a broad pH range for optimal activity. Despite suboptimal pH values, enzymatic activity can remain at pH 8.0. (B) The graph shows the pH stability profile of L-GLS. A pH stability of 8.0 (95% activity) is observed for the enzyme, gradually decreasing to a pH of 9.5. This suggests that the enzyme functions optimally in slightly alkaline conditions, with its active site and catalytic mechanisms best suited for this pH range. (C) This graph depicts the thermal stability of L-GLS. Maximum stability (98%) is observed at 50 °C, with stability gradually decreasing below this temperature. The enzyme exhibits optimal stability at moderately high temperatures, facilitating efficient substrate binding and catalytic reactions. (D) The graph illustrates the influence of metal cations and inhibitors on enzyme activity. These findings provide insights into L-GLS’s functional properties.
