eISSN 1738-8872
pISSN 1017-7825

Fig. 3.

Download original image
Fig. 3. Purification and characterization of the xylanase obtained from S. viridodiastaticus MS9. (A) Estimation of molecular weight and xylanase activity of the purified protein. The xylanase-active fraction, obtained from Resource-Q column chromatography through several stages of purification, was analyzed using 0.1% sodium dodecyl sulfate– 15% polyacrylamide gel electrophoresis (lane 1). The xylanase activity of the isolated protein (molecular weight ≈ 21 kDa) was confirmed by a zymogram, as indicated by an arrow (lane 2). M, molecular-weight standard. (B) Substrate specificity was measured using the DNS method on different substrates (0.5%, w/v), such as birchwood xylan, beechwood xylan, oat spelt xylan, carboxymethyl (CM)-cellulose, and avicel. The enzyme reaction was performed in 20 mM Tris-Cl (pH 7.0) buffer at 60°C for 10 min. The enzyme activity of oat-spelt xylan was considered to be 100%. (C) TLC of the xylan hydrolysate obtained using purified xylanase. The enzyme reaction was carried out at 60°C for 12 h in 20 mM Tris-Cl (pH 7.0) containing 0.2% (w/v) beechwood xylan and then separated on a Silica Gel 60 TLC plate. X1: xylose; X2: xylobiose; X4: xylotetraose. The spot corresponding to X2 is indicated by arrows.
J. Microbiol. Biotechnol. 2024;34:176~184
© J. Microbiol. Biotechnol.