Degradation of 4-aminophenol by hydrogen peroxide oxidation using enzyme from Serratia marcescens as catalyst
This paper reports on the degradation of 4-aminophenol using hydrogen peroxide as oxidizer and the enzyme from Serratia marcescens AB 90027 as catalyst. The effecting factors during degradation and the degrading mechanism were studied. Also, the location of the enzyme in the cell, which could catalyze the degradation of 4-aminophenol, was analyzed. The results showed that to degrade 50 mL of 4-aminophenol whose concentration was 500 mg/L, the optimal conditions were: volume of H2O2 = 3 mL, temperature = 40–60°C and pH = 9–10. In the degradation process, 4-aminophenol was first converted to benzoquinone and NH3, then organic acids including maleic acid, fumaleic acid, and oxalic acid were formed, and then finally CO2 and H2O were generated as final products. The enzyme that could catalyze the degradation of 4-aminophenol was mainly extracellular enzyme.