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Figure 3 | BMC Biotechnology

Figure 3

From: Cultivation to improve in vivo solubility of overexpressed arginine deiminases in Escherichia coliand the enzyme characteristics

Figure 3

Enzymatic characteristics of the purified rADI protein. (A) SDS-PAGE analysis of the purified rADI proteins. The proteins were prepared by co-expression with pGro7 and under the conditions with the addition of 0.5% L-arginine and 0.5% D-glucose. Lanes: M, molecular-mass marker protein; 1, rADI purified using Ni-NTA affinity chromatography. (B) The pH stability of the rADI after 12 hrs incubation at 4°C. (C) The optimal pH, assayed in buffers ranging from 3.0 to 8.6 at 40°C (Citric Acid-sodium citrate buffer for pH 3.0-5.4, Sodium phosphate buffer for pH 6.0-8.6). (D) Thermostability at 30°C (diamond), 40°C (square) and 50°C (triangle). (E) The optimal temperature, measured at various points from 10°C to 100°C in 500 mM Sodium phosphate buffer (pH 6.0).

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