Further purification was achieved
by subjecting the pooled enzyme fraction to a DEAE Sepharose CL-
6B column (Fig. 1b). In this step, fractions eluted by 350–600 mM
NaCl in 50 mM Tris–HCl buffer resulted in a 6.78-fold purity with
a yield of 3.26% and a specific activity of 363.92 M/mg protein as
compared to the crude extract.