ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Evidence for the involvement of multiple pathways in the biodegradation of 1- and 2-methylnaphthalene by pseudomonas putida CSV86

Mahajan, MC and Phale, PS and Vaidyanathan, CS (1994) Evidence for the involvement of multiple pathways in the biodegradation of 1- and 2-methylnaphthalene by pseudomonas putida CSV86. In: Archives of microbiology, 161 (5). pp. 425-433.

[img] PDF
Evidence.pdf - Published Version
Restricted to Registered users only

Download (769Kb) | Request a copy
Official URL: http://www.springerlink.com/content/u133844525554u...

Abstract

Pseudomonas putida CSV86, a soil bacterium, grows on 1- and 2-methylnaphthalene as the sole source of carbon and energy. In order to deduce the pathways for the biodegradation of 1- and 2-methylnaphthalene, metabolites were isolated from the spent medium and purified by thin layer chromatography. Emphasis has been placed on the structural characterisation of isolated intermediates by CC-MS, demonstration of enzyme activities in the cell free extracts and measurement of oxygen uptake by whole cells in the presence of various probable metabolic intermediates. The data obtained from such a study suggest the possibility of occurrence of multiple pathways in the degradation of 1- and 2-methylnaphthalene. We propose that, in one of the pathways, the aromatic ring adjacent to the one bearing the methyl moiety is oxidized leading to the formation of methylsalicylates and methylcatechols. In another pathway the methyl side chain is hydroxylated to -CH2-OH which is further converted to -CHO and -COOH resulting in the formation of naphthoic acid as the end product. In addition to this, 2-hydroxymethylnaphthalene formed by the hydroxylation of the methyl group of 2-methylnaphthalene undergoes aromatic ring hydroxylation. The resultant dihydrodiol is further oxidised by a series of enzyme catalysed reactions to form 4-hydroxymethyl catechol as the end product of the pathway.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Springer.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 31 May 2011 09:23
Last Modified: 31 May 2011 09:30
URI: http://eprints.iisc.ernet.in/id/eprint/36449

Actions (login required)

View Item View Item