eISSN 1738-8872
pISSN 1017-7825

Fig. 4.

Download original image
Fig. 4. Biochemical characteristics of the purified xylanase from S. viridodiastaticus MS9. The following enzymatic reaction was performed at 60°C for 10 min in 20 mM Tris-Cl (pH 7.0) buffer using beechwood xylan as a substrate unless otherwise specified. (A) Effect of pH. The xylanase assay was performed under different pH conditions. Values obtained with 20 mM Tris-Cl (pH 7.0) were considered 100%. ●, 20 mM MOPS buffer; ■, 20 mM Tris-Cl buffer. (B) Effects of temperature. The xylanase assay was carried out at different temperatures ranging from 40°C to 70°C. The values obtained at 60°C were taken to be 100%. (C) Temperature stability. The enzyme was heat-treated at the indicated temperatures for 10, 20, 30, 60, and 120 min, and residual enzyme activity was measured. The activity value without preincubation was set to 100%. ●, 60°C; ■, 65°C; ♦, 70°C. (D) The effects of metal ions and chelating reagents. Each compound was added to the reaction mixture at a final concentration of 5 mM. The enzyme activity in the absence of chemicals was 100%. (E) Determination of kinetic parameters. Lineweaver-Burke plots were used to determine the kinetic parameters of the purified xylanase acting on beechwood xylan. Data are shown as mean values of at least three replicate experiments.
J. Microbiol. Biotechnol. 2024;34:176~184
© J. Microbiol. Biotechnol.