Figure 1
(a) Modeled structure of Xyn-2. The (β/α)8 barrel is a characteristic feature of family 10 xylanases (b) SDS-PAGE and native PAGE of purified Xyn-2. Lane 1—molecular weight marker, lane 2—purified Xyn-2, lane 3—cell lysate of E. coli BL21(DE3) expressing Xyn-2, lane 4—native PAGE and activity staining of Xyn-2 with Congo-red (from supplementary Fig. S3). The arrow indicates the yellowish band of xylan hydrolysis (c) Effect of pH on the activity of Xyn-2 measured by running reactions in various pH buffers at 35 °C. The highest enzyme activity, obtained at pH 5, was taken as 100%, and the enzyme activities obtained at other pH conditions were expressed as a percentage of the highest activity (d) Influence of temperature on the activity of Xyn-2 measured at pH 5 in citrate buffer. The highest enzyme activity, obtained at 20 °C, was taken as 100%, and the enzyme activities obtained at other temperatures were expressed as a percentage of the highest activity. The significant difference between the peak value and other values of enzyme activity is indicated by the stars (p ≤ 0.001). Letters reflect values that are not significantly different from each other.
