Archives of Microbiology

, Volume 161, Issue 5, pp 425–433

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


  • Milind C. Mahajan
    • Department of BiochemistryIndian Institute of Science
  • Prashant S. Phale
    • Department of BiochemistryIndian Institute of Science
  • Chelakara S. Vaidyanathan
    • Department of BiochemistryIndian Institute of Science
Original Papers

DOI: 10.1007/BF00288954

Cite this article as:
Mahajan, M.C., Phale, P.S. & Vaidyanathan, C.S. Arch. Microbiol. (1994) 161: 425. doi:10.1007/BF00288954


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 GC-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-CH2OH 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.

Key words

PseudomonasMethylnaphthalenesMetabolismHydroxylationOxygenasesAromatic ring cleavage

Copyright information

© Springer-Verlag 1994