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Abstract
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Article Information:
Purification and characterization of catechol 1, 2-dioxygenase from Rhodococcus sp. NCIM 2891
Naiem H. Nadaf and Jai S. Ghosh
Corresponding Author: Jai S. Ghosh
Submitted: 2011 May, 11
Accepted: 2011 June, 15
Published: 2011 August, 10 |
Abstract:
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The main aim of this study was to purify Catechol 1, 2 dioxygenase from phenol utilizing
Rhodococcus sp. NCIM 2891 which is basically an organism used wide for desulfurization purposes like
desulfurization of diesel. The organism was cultivated in minimal medium supplemented with 500 mg/L phenol,
as a sole carbon source. The temperature of incubation was 30ºC at pH 7.0±0.2. The growth and phenol
degradation studies show that organism was able to degrade the phenol completely within 120 h. The stationary
phase of growth of the organism, however, started after 72 h. This implies that the degradation activities starts
from late log phase and carries on till late stationary phase of growth. The enzyme responsible for phenol
degradation was catechol 1, 2 dioxygenase. The optimal activity of catechol 1, 2 dioxygenase was observed
at 500 mg/L phenol concentration. The enzyme was purified 2.34 fold by ion exchange chromatography. The
Km was found to be 5 μmole with Vmax of 62.5 U/mg of protein. The optimal pH and temperature of the enzyme
was 7.5 and 30ºC respectively. The enzyme activity was completely inhibited by Cu++, Hg++ and Fe+++ metal
ions. The SDS-PAGE analysis reveals that the enzyme has a molecular weight of 30 k Dalton.
Key words: Catechol, dioxygenase, Rhodococcus, muconate, phenol, ,
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Cite this Reference:
Naiem H. Nadaf and Jai S. Ghosh, . Purification and characterization of catechol 1, 2-dioxygenase from Rhodococcus sp. NCIM 2891. Research Journal of Environmental and Earth Sciences, (5): 608-613.
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ISSN (Online): 2041-0492
ISSN (Print): 2041-0484 |
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