Figure 1: Purification profile of A.fumigatus L-aao. (a) Ion-exchange chromatography of crude enzyme on a DEAE-Sephadex A-50 column. The column (30 x 1.8 cm) was pre-equilibrated with 10mM sodium-phosphate buffer (pH 7.2). Elution was done with a linear concentration gradient of NaCl (0-1 M) at a flow rate of 0.5 mL/min. Fraction F1 (indicated by an arrow) containing L-aao activities were pooled and lyophilized. (b) Gel filtration chromatography on a Sephadex G-75 column. Fraction F1 was loaded on a Sephadex G-75 column (65x1.5 cm) pre-equilibrated with 10 mM sodium phosphate buffer (pH 7.2) and eluted with the same buffer at a flow rate of 0.7 mL/min. Fractions with L-aao activity were pooled and lyophilized (Fraction F2, indicated by an arrow).