Figure 3From: Novel xylanases from Simplicillium obclavatum MTCC 9604: comparative analysis of production, purification and characterization of enzyme from submerged and solid state fermentation Partial purification profile of xylanase of S. obclavatum. The bound proteins were eluted from Superose 12 10/300 GL column with 50 mM potassium phosphate buffer pH 7.0 and the fractions were collected at 1 ml volume each. The fractions were assayed for xylanase activity and subjected to determine the absorbance at 280 nm wavelength.Back to article page