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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| Veröffentlicht in: | Biotechnology letters 2014, Vol.36 (1), p.127-131 |
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| creator | Misal, Santosh A Lingojwar, Devendra P Lokhande, Mahendra N Lokhande, Pradeep D Gawai, Kachru R |
| description | 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. |
| doi_str_mv | 10.1007/s10529-013-1338-8 |
| format | Article |
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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.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-013-1338-8</identifier><identifier>PMID: 24068503</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>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</subject><ispartof>Biotechnology letters, 2014, Vol.36 (1), p.127-131</ispartof><rights>Springer Science+Business Media Dordrecht 2013</rights><rights>Springer Science+Business Media Dordrecht 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-18844042ed00282d96b2368b177ce7518b000ec2c124da2f6fa1afaed1968fab3</citedby><cites>FETCH-LOGICAL-c499t-18844042ed00282d96b2368b177ce7518b000ec2c124da2f6fa1afaed1968fab3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-013-1338-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-013-1338-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,4024,27923,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24068503$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Misal, Santosh A</creatorcontrib><creatorcontrib>Lingojwar, Devendra P</creatorcontrib><creatorcontrib>Lokhande, Mahendra N</creatorcontrib><creatorcontrib>Lokhande, Pradeep D</creatorcontrib><creatorcontrib>Gawai, Kachru R</creatorcontrib><title>Enzymatic transformation of nitro-aromatic compounds by a flavin-free NADH azoreductase from Lysinibacillus sphaericus</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>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.</description><subject>Amines</subject><subject>Applied Microbiology</subject><subject>Aromatic compounds</subject><subject>Azo Compounds - analysis</subject><subject>Azo Compounds - metabolism</subject><subject>Azo dyes</subject><subject>Bacillaceae - enzymology</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Bioremediation</subject><subject>Biotechnology</subject><subject>Biotransformation</subject><subject>Dyes</subject><subject>environmental health</subject><subject>Enzymes</subject><subject>Hydrogen-Ion Concentration</subject><subject>Industrial wastes</subject><subject>Life Sciences</subject><subject>Lysinibacillus</subject><subject>Microbiology</subject><subject>molecular weight</subject><subject>NAD</subject><subject>NAD (coenzyme)</subject><subject>NADH</subject><subject>NADH, NADPH Oxidoreductases - chemistry</subject><subject>NADH, NADPH Oxidoreductases - isolation & purification</subject><subject>NADH, NADPH Oxidoreductases - metabolism</subject><subject>NADP</subject><subject>NADP (coenzyme)</subject><subject>Nitro compounds</subject><subject>Nitro Compounds - analysis</subject><subject>Nitro Compounds - metabolism</subject><subject>nuclear magnetic resonance spectroscopy</subject><subject>Optimization</subject><subject>Original Research Paper</subject><subject>pollutants</subject><subject>Reduction</subject><subject>size exclusion 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R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic transformation of nitro-aromatic compounds by a flavin-free NADH azoreductase from Lysinibacillus sphaericus</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2014</date><risdate>2014</risdate><volume>36</volume><issue>1</issue><spage>127</spage><epage>131</epage><pages>127-131</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>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.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>24068503</pmid><doi>10.1007/s10529-013-1338-8</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biotechnology letters, 2014, Vol.36 (1), p.127-131 |
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| 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 |
| title | Enzymatic transformation of nitro-aromatic compounds by a flavin-free NADH azoreductase from Lysinibacillus sphaericus |
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