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Dehalogenation of 4 — Chlorobenzoic Acid by Pseudomonas isolates

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Abstract

Twenty three bacterial isolates either pure or consortium were initially screened on the basis of their ability to degrade as well as dechlorinate 4 — chlorobenzoic acid (4-CBA). Based on comparative growth response, three pure isolates Pseudomonas putida GVS-4, Pseudomonas aeruginosa GVS-18 and Pseudomonas aeruginosa GWS-19 and a consortium SW-2 was finally selected for further studies. The enzyme studies performed with cell free extracts revealed that dehalogenase activity was substrate specific with maximum activity at 300 μgml−1 substrate concentration. Catechol 1,2 dioxygenase activity was found to be present in cell free extracts suggesting that 4 — chlorobenzoic acid (4-CBA) is catabolized by ortho-ring cleavage pathway. The dehalogenase enzyme profile showed single enzyme band in case of GVS-4 (Rm 0.76), GVS-18 (Rm 0.84), GWS −19 (Rm 0.85) and two bands in SW-2 (Rm 0.71 & 0.10).

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  1. Department of Microbiology, Punjab Agricultural University, Ludhiana, 141 004, India

    G. Banta & R. S. Kahlon

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  1. G. Banta
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  2. R. S. Kahlon
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Correspondence to G. Banta.

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Banta, G., Kahlon, R.S. Dehalogenation of 4 — Chlorobenzoic Acid by Pseudomonas isolates. Indian J Microbiol 47, 139–143 (2007). https://doi.org/10.1007/s12088-007-0027-5

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  • DOI: https://doi.org/10.1007/s12088-007-0027-5

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