Xylanase SMXL1 from Stenocarpella maydis: Purification and Biochemical Characterization

This study aimed to develop a method for the purification of a xylanase called SMXL1 produced by Stenocarpella maydis and its biochemical characterization. The enzyme was purified using a Rotofor preparative chamber and one chromatographic step in an ion exchange column coupled to equipment FPLC. Posteriorly the protein was characterized, and its effect on the birchwood xylan degradation was determine by HPLC. The purified enzyme showed a molecular weight of 55 kDa calculated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The purification process obtained a yield of 6.5 +/- 0.3 %. The activity was stable at a pH range of 4 to 10 and temperatures of 45 to 60 degrees C. The optimum values of temperature and pH were 55 degrees C and 4, respectively. The Michaelis constant (K-m) value was 2.61 mg/mL and the V-max was 3.02 mu mol/mL/min using birchwood xylan as substrate and the Michaelis-Menten equation. The enzyme is inhibited by the cations Mn2+ and by Fe3+ and degrades the birchwood xylan being the principal products the xylobiose and the xylose. This work is the first report of the purification and biochemical characterization of a xylanase called SMXL1 produced by S. maydis.