Efficient, fast and robust degradation of chlortetracycline in wastewater catalyzed by recombinant Arthromyces ramosus peroxidase

Chlortetracycline (CTC), a widely used antibiotic, is recalcitrant and ubiquitous in the environment. Enzymatic degradation of CTC is an economical and efficient bioremediation method. In this work, recombinant Arthromyces ramosus peroxidase (rARP) at a concentration of 3.13 × 10−9 M was used to catalyze rapid degradation of CTC in water. The second-order rate constants of rARP showed up to 62-fold catalytic efficiency of horseradish peroxidase (HRP) toward CTC. The degradation half-life of CTC at the concentrations of 2 and 40 mg L−1 in wastewater under the rARP catalysis was, respectively, 5.3 and 5.7 min at 25 °C, and 2.7 and 3.1 min at 40 °C, which were up to 15-fold and 111-fold faster than HRP and laccase, respectively, but use of 3 % the amount of rARP as HRP. rARP catalyzed degradation of CTC at 2–40 mg L−1 in wastewater completed in 20–24 min, and its catalytic efficiency varied within only 2-fold at 25–40 °C. rARP showed only 2–3-fold discrepancy of catalytic efficiency among pH 5.0, 7.5 and 9.0. CTC under rARP catalysis underwent demethylation and oxidation to form nontoxic N-dedimethyl-9-hydroxy-CTC. The high catalytic efficiency of rARP agreed with a short distance between rARP's δN-His56 and CTC's dimethylamine N as indicated by docking simulation. rARP is a useful enzyme for CTC bioremediation. [Display omitted] •Recombinant A. ramosus peroxidase (rARP) has 62-fold catalytic efficiency of HRP.•Degradation half-life of rARP-catalyzed chlortetracycline (CTC) is 2.7–5.7 min.•rARP catalyzes complete degradation of CTC in 20–44 min.•The rARP catalytic efficiency varies little at pH 5.0–9.0 and 25–40 °C.•rARP-CTC docking simulation suggests a pH–structure–activity relationship of rARP.