Figure 2

DEAE anion exchange chromatography and SDS-PAGE analysis of the recombinant β-glucosidase. A. Anion exchange chromatography was used to measure protein by its absorbance at 280 nm with increasing fractions as indicated on the x-axis. Two successive NaCl concentrations were used first to first elute non-specific protein and then to elute the recombinant β-glucosidase. Peak A demonstrates other impurity proteins eluted with 200 mM NaCl and peak B is recombinant β-glucosidase eluted with 400 mM NaCl. B. Following secretion, supernatant was collected and SDS-PAGE was performed before and after purification. Lane M shows a protein size marker, lane 1 shows total protein in culture supernatant before purification, and lane 2 shows recombinant β-glucosidase following purification. The arrow at approximately 120 kDa shows the β-glucosidase dimer.