Purification and Characterization of an ATPase GsiA from Salmonella enterica

Figure 2

Characterization the ATPase of GsiA protein. (a) Effect of temperature on GsiA activity determined in Tris/HCl buffer (pH 8) at 4–60°C. (b) Thermostability assay. The purified GsiA protein was incubated in Tris/HCl buffer (pH 8) at 20, 30, and 40°C. Aliquots were collected at specific time points for residual activity assay at 30°C in Tris/HCl buffer (pH 8). (c) Effect of pH on GsiA protein activity. The enzyme activity was measured at 30°C in different buffers with pH varied from 6 to 10. (d) pH stability assay. The GsiA was incubated at pH 7, 8, or 9; aliquots were collected at different time points for residual activity assay. The error bars represent the mean ± standard deviation ().

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