Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/5626
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dc.contributor.authorSaxena, Preti-
dc.contributor.authorThakur, Indu Shekhar-
dc.date.accessioned2009-07-30T06:02:13Z-
dc.date.available2009-07-30T06:02:13Z-
dc.date.issued2005-01-
dc.identifier.issn0975-0967 (Online); 0972-5849 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/5626-
dc.description134-138en_US
dc.description.abstractThe degradation of 4-chlorobenzoic acid (4-CBA) by Pseudomonas fluorescens IST8 was determined. The degradation of 4-CBA proceeded through an oxidative route to yield ortho ring cleavage enzyme, catechol 1, 2-dioxygenase. The cell free extract fractionated by DEAE-cellulose ion-exchange and gel filtration chromatography showed two different fractions of catechol 1,2-dioxygenase with an expected molecular weight of 62 and 48 kDa, respectively. The catechol 1, 2-dioxygenase in the fractions I and II was purified to about 22.3 and 36.5 fold by using purification steps. The pH and temperature optima for enzyme activity were 6.5 and 25°C, respectively. The purified protein on SDS-polyacrylamide gel electrophoresis showed molecular weights of 28 and 24 kDa, indicating dimeric nature of the enzyme.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.relation.ispartofseriesInt. Cl.7 A 01 N 29/00, 63/00; C 07 C 63/10en_US
dc.sourceIJBT Vol.4(1) [January 2005]en_US
dc.subjectcatechol-1,2-dioxygenaseen_US
dc.subject4-chlorobenzoic aciden_US
dc.subjectchlorocatecholen_US
dc.subjectDEAE-celluloseen_US
dc.subjectgel filtrationen_US
dc.subjectSDS-polyacrylamide gel electrophoresisen_US
dc.titlePurification and characterization of catechol 1,2-dioxygenase of Pseudomonas fluorescens for degradation of 4-chlorobenzoic aciden_US
dc.typeArticleen_US
Appears in Collections:IJBT Vol.04(1) [January 2005]

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