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- Title
Rhodococcus lactonase with organophosphate hydrolase (OPH) activity and His-tagged OPH with lactonase activity: evolutionary proximity of the enzymes and new possibilities in their application.
- Authors
Sirotkina, Mariia; Efremenko, Elena
- Abstract
Decontamination of soils with complex pollution using natural strains of microorganisms is a matter of great importance. Here we report that oil-oxidizing bacteria Rhodococcus erythropolis AC-1514D and Rhodococcus ruber AC-1513D can degrade various organophosphorous pesticides (OP). Cell-mediated degradation of five different OP is apparently associated with the presence of N-acylhomoserine lactonase, which is pronouncedly similar (46-50 %) to the well-known enzyme organophosphate hydrolase (OPH), a hydrolysis catalyst for a wide variety of organophosphorous compounds. Additionally, we demonstrated the high lactonase activity of hexahistidine-tagged organophosphate hydrolase (His-OPH) with respect to various N-acylhomoserine lactones, and we determined the catalytic constants of His-OPH towards these compounds. These experimental data and theoretical analysis confirmed the hypothesis about the evolutionary proximity of OPH and lactonases. Using Rhodococcus cells, we carried out effective simultaneous biodegradation of pesticide paraoxon (88 mg/kg) and oil hydrocarbon hexadecane (6.3 g/kg) in the soil. Furthermore, the discovered high lactonase activity of His-OPH offers new possibilities for developing an efficient strategy of combating resistant populations of Gram-negative bacterial cells.
- Subjects
RHODOCOCCUS; HYDROLASES; LACTONASE; METALLOENZYMES; ORGANOPHOSPHORUS pesticides; ORGANOPHOSPHORUS compounds
- Publication
Applied Microbiology & Biotechnology, 2014, Vol 98, Issue 6, p2647
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-013-5233-y