A Novel Cold-Adapted Nitronate Monooxygenase from sp. ANT206: Identification, Characterization and Degradation of 2-Nitropropane at Low Temperature.

Aliphatic nitro compounds cause environmental pollution by being discharged into water with industrial waste. Biodegradation needs to be further explored as a green and pollution-free method of environmental remediation. In this study, we successfully cloned a novel nitronate monooxygenase gene () from the genomic DNA library of sp. ANT206 and investigated its ability to degrade 2-nitropropane (2-NP). Homology modeling demonstrated that PsNMO had a typical I nitronate monooxygenase catalytic site and cold-adapted structural features, such as few hydrogen bonds. The specific activity of purified recombinant PsNMO (rPsNMO) was 97.34 U/mg, rPsNMO exhibited thermal instability and reached maximum catalytic activity at 30 °C. Moreover, rPsNMO was most active in 1.5 M NaCl and remained at 104% of its full activity in 4.0 M NaCl, demonstrating its significant salt tolerance. Based on this finding, a novel bacterial cold-adapted enzyme was obtained in this work. Furthermore, rPsNMO protected BL21 (DE3)/pET28a(+) from the toxic effects of 2-NP at 30 °C because the 2-NP degradation rate reached 96.1% at 3 h and the final product was acetone. These results provide a reliable theoretical basis for the low-temperature degradation of 2-NP by NMO.