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. 2016 Jun;17(6):455–464. doi: 10.1631/jzus.B1500317

Fig. 2.

Fig. 2

Characterization of the purified A. terreus β-glucosidase

(a) Effect of temperature on A. terreus β-glucosidase activities. The activity was measured in McIlvaine buffer (100 mmol/L, pH 5.0) using pNPG as the substrate. (b) Effect of pH on A. terreus β-glucosidase activities. The enzyme activities at various pH values were measured at 50 °C for 10 min using pNPG as the substrate. (c) Thermostability of A. terreus β-glucosidase. The residual activity was measured using pNPG as the substrate after pre-incubation without substrate at 50, 60, and 70 °C for different periods of time. (d) pH stability of A. terreus β-glucosidase. The residual activities were measured at optimal conditions against pNPG after incubation at various pH values, 25 °C for 1 h. The error bars represent the standard deviation (SD), with n=3