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Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase | OMICS International | Abstract
ISSN: 2155-6199

Journal of Bioremediation & Biodegradation
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Research Article

Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADHAzoreductase

Santosh A. Misal1,3*, Vivek T. Humne2, Pradeep D. Lokhande2 and Kachru R. Gawai3*
1Department of Chemistry, Indiana University Bloomington, Indiana, 47405, USA
2Center for Advance Studies, Department of Chemistry, University of Pune, Pune-411 007, India
3Biochemistry Division, Department of Chemistry, University of Pune, Pune-411 007, India
Corresponding Authors : Santosh A. Misal
Department of Chemistry
Indiana University Bloomington
Indiana, 47405, USA
Tel: +1 574 516 8259
E-mail: [email protected]
  Kachru R. Gawai
Biochemistry Division
Department of Chemistry
University of Pune, Pune-411 007, India
Tel: +91-020-25691395
Fax: +91-020-25691728
E-mail: [email protected]
Received October 05, 2014; Accepted January 28, 2015; Published January 30, 2015
Citation: Misal SA, Humne VT, Lokhande PD, Gawai KR (2015) Biotransformation of Nitro Aromatic Compounds by Flavin-Free NADH-Azoreductase. J Bioremed Biodeg 6:272. doi:10.4172/2155-6199.1000272
Copyright: © 2015 Misal SA, et al. This is an open-a ccess article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Nitro aromatic compounds are the potential toxic organic pollutant released into the environment and are often resistant to degradation under normal environmental conditions. The biotransformation and/or detoxification of these compounds can be possible by microbial azoreductase enzyme. Azoreductase enzyme has an ability to reduce the toxic nitro group to corresponding amino group. In present report, the flavin-free NADH azoreductase was isolated and purified from alkaliphilic bacteria Bacillus badius. The enzyme was purified by a combination of ammonium sulphate precipitation and size exclusion chromatography. The purified azoreductase has efficiently demonstrated both azoreductase and nitroreductase activities. The biochemical properties of the azoreductase including cofactor requirement, substrate specificity and enzyme inhibition have been studied. The biotransformation of some selected nitro aromatic compounds like 3-nitro benzoic acid, 4-nitro toluene, 3-nitro toluene and 1-chloro-2-nitro benzene by purified azoreductase was carried out at 37°C. The reduction products of these nitro aromatic compounds were analyzed by IR and NMR spectroscopy.

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