Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/5626
Title: Purification and characterization of catechol 1,2-dioxygenase of <i style="">Pseudomonas fluorescens </i>for degradation of 4-chlorobenzoic acid
Authors: Saxena, Preti
Thakur, Indu Shekhar
Keywords: catechol-1,2-dioxygenase
4-chlorobenzoic acid
chlorocatechol
DEAE-cellulose
gel filtration
SDS-polyacrylamide gel electrophoresis
Issue Date: Jan-2005
Publisher: CSIR
Series/Report no.: Int. Cl.<sup>7</sup> A 01 N 29/00, 63/00; C 07 C 63/10
Abstract: The degradation of<i style=""> </i>4-chlorobenzoic acid (4-CBA) by<i style=""> Pseudomonas fluorescens </i>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 <i style="">p</i>H 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.
Description: 134-138
URI: http://hdl.handle.net/123456789/5626
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections:IJBT Vol.04(1) [January 2005]

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