Enzymatic transformation of nitro-aromatic compounds by a flavin-free NADH azoreductase from Lysinibacillus sphaericus

Azo dyes and nitro-aromatic compounds are the largest group of pollutants released in the environment as industrial wastes. They create serious health and environmental problems. Azoreductases catalyze the reduction of azo dyes and nitro compounds to their respective amines. AN azoreductase was puri...

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Bibliographic Details
Published in:Biotechnology letters 2014, Vol.36 (1), p.127-131
Main Authors: Misal, Santosh A, Lingojwar, Devendra P, Lokhande, Mahendra N, Lokhande, Pradeep D, Gawai, Kachru R
Format: Article
Language:English
Subjects:
Amines
Applied Microbiology
Aromatic compounds
Azo Compounds - analysis
Azo Compounds - metabolism
Azo dyes
Bacillaceae - enzymology
Biochemistry
Biomedical and Life Sciences
Bioremediation
Biotechnology
Biotransformation
Dyes
environmental health
Enzymes
Hydrogen-Ion Concentration
Industrial wastes
Life Sciences
Lysinibacillus
Microbiology
molecular weight
NAD
NAD (coenzyme)
NADH
NADH, NADPH Oxidoreductases - chemistry
NADH, NADPH Oxidoreductases - isolation & purification
NADH, NADPH Oxidoreductases - metabolism
NADP
NADP (coenzyme)
Nitro compounds
Nitro Compounds - analysis
Nitro Compounds - metabolism
nuclear magnetic resonance spectroscopy
Optimization
Original Research Paper
pollutants
Reduction
size exclusion chromatography
Studies
Temperature
Transformations
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Summary:Azo dyes and nitro-aromatic compounds are the largest group of pollutants released in the environment as industrial wastes. They create serious health and environmental problems. Azoreductases catalyze the reduction of azo dyes and nitro compounds to their respective amines. AN azoreductase was purified up to 12-fold from Lysinibacillus sphaericus using ion-exchange and size exclusion chromatography. It was optimally active at pH 7.4 and 75 °C. It was stable at 70 °C for 30 min. The purified enzyme utilized NADH rather than NADPH as an electron donor to reduce substrates. The molecular weight of the purified enzyme was ~29 kDa. The enzyme also acted as nitroreductase and could selectively reduce the nitro group of 2-nitrophenol, 4-nitrobenzoic acid, 2-nitro-benzaldehyde and 3-nitrophenol. Reduction products of these compounds were identified by IR and NMR.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-013-1338-8