Enzymological aspects of bioconversion of m-dinitrobenzene.

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dc.contributor.authorDey, Sabitaen_US
dc.date.accessioned2002-07-25en_US
dc.date.accessioned2009-06-02T04:20:50Z
dc.date.available2002-07-25en_US
dc.date.available2009-06-02T04:20:50Z
dc.date.issued2002-07-25en_US
dc.description.abstractThree main enzymes, responsible for bioconversion of 1,3 dinitrobenzene (m-DNB) by Micrococcus colpogenes MCM B 410, were isolated from the sonicated cell mass, grown in presence of m-DNB in a synthetic medium, for 7 days. The soluble proteins were separated by differential precipitation and also separated by native PAGE. Each fraction obtained from both the protocols, was tested for nitro aryl reductase, aryl mono oxygenase and resorcinol 2,3 dioxygenase. The apparent molecular weight of the proteins were nitro aryl reductase (30 kDa), aryl mono oxygenase (110 kDa) and resorcinol 2,3 di oxygenase (65 kDa).en_US
dc.description.affiliationDivision of Microbial Sciences, Agharkar Research Institute, G.G. Agharkar Road, Pune 411 004, India. sabitadey@hotmail.comen_US
dc.identifier.citationDey S. Enzymological aspects of bioconversion of m-dinitrobenzene. Journal of Environmental Biology. 2002 Jul; 23(3): 289-94en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/113706
dc.language.isoengen_US
dc.source.urihttps://www.geocities.com/j_environ_biol/en_US
dc.subject.meshBiotransformationen_US
dc.subject.meshDinitrobenzenes --metabolismen_US
dc.subject.meshMicrococcus --enzymologyen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshPrecipitationen_US
dc.titleEnzymological aspects of bioconversion of m-dinitrobenzene.en_US
dc.typeJournal Articleen_US
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