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. 2013 Sep 9;8(9):e73729. doi: 10.1371/journal.pone.0073729

Figure 4. Effects of pH and temperature on the activity and stability of xylanolytic enzymes from L. chartarum SJTU59.

Figure 4

(A) pH effect on xylanolytic enzyme activity determined in the McIlvaine buffer (pH 3.0 to pH 7.0), Tris-HCl (pH 7.0 to pH 9.0), and Glycine-NaOH solution (pH 9.0 to pH 11.0) at 50°C. (B) pH stability of xylanolytic enzyme determined at 50°C after 12 h of pre-incubation in the McIlvaine buffer (pH 3.0 to pH 7.0), Tris-HCl (pH 7.0 to pH 9.0) or Glycine-NaOH solution (pH 9.0 to pH 11.0) at 4°C. (C) Temperature effect on xylanolytic enzyme activity determined in sodium acetate buffer (0.1 M, pH 5.0, 10°C to 100°C). (D) Thermostability of xylanolytic enzymes determined at 50°C after pre-incubation in sodium acetate buffer (pH 5.0) at 40, 50, or 60°C without substrate.