Oxidation of cadaverine by putrescine oxidase from Rhodococcus erythropolis

BACKGROUND Putrescine oxidase (EC 1.4.3.10) is of interest for the microbial production unsubstituted platform nitrogen (N-)heterocycles, because it only requires inexpensive oxygen as co-substrate. from Rhodococcus erythropolis (Re-PuO) was shown previously to catalyze oxidation cadaverine; however, there little information in literature about robustness this enzyme biotechnological applications. The aim study investigate suitability Re-PuO bioproduction 1-piperideine cadaverine under different reaction conditions. RESULTS formation catalyzed by demonstrated using o-aminobenzaldehyde a reagent trap cyclic imine and shift equilibrium cyclization. A direct assay activity then implemented, monitoring consumption. Characterization mixture 1H NMR mass spectrometry confirmed presence piperideine dimers trimers, yet quantification products could not be achieved. optimum temperature pH conditions were determined 55 °C 8.5, respectively. At 7.5, retained its after 65 h incubation at 25 °C, but lost 75% 1 °C. showed no substrate inhibition concentrations high 100 mmol L–1 cadaverine. Complete biotransformation observed whole cells physiological CONCLUSIONS These results successfully demonstrate potential putrescine N-heterocycles © 2021 Authors. Journal Chemical Technology Biotechnology published John Wiley & Sons Ltd on behalf Society Industry (SCI).