Characterization of thermostable FMN-dependent NADH azoreductase from the moderate thermophile Geobacillus stearothermophilus
Autor: | Ken'ichiro Matsumoto, Daiki Ogata, Fumi Shozui, Toshihiko Ooi, Seiichi Taguchi, John Masani Nduko, Yuichi Mukai |
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Rok vydání: | 2009 |
Předmět: |
Flavin Mononucleotide
Coenzymes Flavoprotein Flavin group Applied Microbiology and Biotechnology Substrate Specificity Geobacillus stearothermophilus chemistry.chemical_compound Enzyme Stability Escherichia coli NADH NADPH Oxidoreductases Cloning Molecular Thermostability biology Circular Dichroism Thermophile General Medicine Nitroreductases NAD Congo red Biochemistry chemistry Acid red 88 Methyl red biology.protein Azo Compounds Biotechnology |
Zdroj: | Applied Microbiology and Biotechnology. 86:1431-1438 |
ISSN: | 1432-0614 0175-7598 |
Popis: | The gene encoding an FMN-dependent NADH azoreductase, AzrG, from thermophilic Geobacillus stearothermophilus was cloned and functionally expressed in recombinant Escherichia coli. Purified recombinant AzrG is a homodimer of 23 kDa and bore FMN as a flavin cofactor. The optimal temperature of AzrG was 85 degrees C for the degradation of Methyl Red (MR). AzrG remained active for 1 h at 65 degrees C and for 1 month at 30 degrees C, demonstrating both superior thermostability and long-term stability of the enzyme. AzrG efficiently decolorized MR, Ethyl Red at 30 degrees C. Furthermore, the enzyme exhibited a wide-range of degrading activity towards several tenacious azo dyes, such as Acid Red 88, Orange I, and Congo Red. These results suggested the sustainable utilization of G. stearothermophilus as an azo-degrading strain for AzrG carrying whole-cell wastewater treatments for azo pollutants under high temperature conditions. |
Databáze: | OpenAIRE |
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