Azoreductases are the enzymes which catalyze the reductive cleavage of azo bonds to produce colorless aromatic amine products. Azoreductases are observed in many organisms, including the rat liver enzyme, rabbit liver aldehyde oxidase and intestinal microbiota. Several studies have been investigated bacterial Cytoplasmic azoreductases, and suggested that they can be applied for the purpose of environmental biotechnology. In the present study, the enzyme Azoreductase was assayed for extracellular activity. As there was no significant activity observed, intracellular release of the enzyme was performed. After each step of purification the activity was assayed and it was found that the specific activity of the enzyme increased after each step of purification. Azoreductase activity in the crude cell extract was found to be 0.0015 U/mg. After ammonium sulfate precipitation, the activity increased to 91.66 U/mg. The optimum pH found for the activity of azoreductase enzyme was pH 7 with an activity of 0.0010 U/mg. The optimum temperature was found to be 40°C with an activity of 0.00098 U/mg.
