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Fig. 3 | Microbial Cell Factories

Fig. 3

From: Characterization and high-efficiency secreted expression in Bacillus subtilis of a thermo-alkaline β-mannanase from an alkaliphilic Bacillus clausii strain S10

Fig. 3

pH and temperature profiles of the purified recombinant BcManA. a Optimal pH: the buffer used was 50 mM Na2HPO4–Citric acid buffer (pH 5.5–7.5, black down-pointing triangle), 50 mM Tris–HCl buffer (pH 7.5–8.5, black up-pointing triangle), 50 mM glycine–NaOH buffer (pH 8.5–10.5, black circle) and 25 mM Na2CO3–NaOH buffer (pH 10.5–11.5, black square); b pH stability: the buffer with different pH was 50 mM Na2HPO4–Citric acid buffer (pH 4.5–7.5, black down-pointing triangle), 50 mM Tris–HCl buffer (pH 7.5–8.5, black up-pointing triangle), 50 mM glycine–NaOH buffer (pH 8.5–10.5, black circle) and Na2HPO4–NaOH buffer (pH 11.0–12.0, black right-righting pointer); c optimal temperature; d thermal stability: the enzyme was incubated at 50 °C (black square), 60 °C (black up-pointing triangle), 70 °C (white square) and 80 °C (white circle) in 50 mM glycine–NaOH buffer (pH 9.0). All of the activities were measured under standard enzyme assay conditions with locust bean gum as the substrate. Values are expressed as the means of three experiments. Error bars represent standard deviations

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