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Fig. 3 | Bioresources and Bioprocessing

Fig. 3

From: Characterization of a novel metallocarboxypeptidase from Streptomyces cinnamoneus TH-2

Fig. 3

Optimum pH, pH stability, optimum temperature, and thermostability of TH2-CP. a Optimum pH of TH2-CP against Z-Gly-Leu at 40 °C. The activities are presented as relative activity at the pH 8.0 (Tris–HCl buffer). Acetate buffer (filled circle), potassium phosphate buffer (empty circle), Tris–HCl buffer (filled triangle). b pH stability of TH2-CP against Z-Gly-Leu at 40 °C. The activities are presented as relative activity at pH 7.0 (potassium phosphate buffer). c Optimum temperature of TH2-CP against Z-Gly-Leu and potassium phosphate buffer (pH 7.0). The activities are presented as relative activity at 51 °C. d Thermostability of TH2-CP against Z-Gly-Leu and potassium phosphate buffer (pH 7.0). The activities are presented as relative activity at 5 °C. All the data are expressed as the mean ± SD of three independent experiments

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