Characterization of an α-haloalkanoic acid-degrading Pseudomonas aeruginosa MX1 isolated from contaminated seawater

• Main Authors: Edbeib, Mohamed Faraj Abdulgader, Abdul Wahab, Roswanira, Huyop, Fahrul
• Format: Article
• Published: Taylor and Francis Inc. 2016
• Subjects: QD Chemistry
• Online Access: http://eprints.utm.my/id/eprint/72643/; https://www.scopus.com/inward/record.uri?eid=2-s2.0-84961927052&doi=10.1080%2f10889868.2015.1114464&partnerID=40&md5=afc9e659b29c426d6d69b8f686dea0b3

Halogenated compounds such as α-halocarboxylix acids (αHAs) are widely liberated into the ecosystem through the prevailing xenobiotic activities that involve the use of herbicides for weed management in the agricultural sector and mass production of various commercial halogenated chemical intermediates. Since such compounds exert stress on the environment owing to their recalcitrance and are not easily degraded, the study aimed to isolate, identify, and characterize dehalogenase-producing bacteria with the purpose of bioremediation. The MX1 bacterium was successfully isolated from seawater samples off the coast of Desaru, Malaysia, using an enrichment technique supplemented with 2,2-dichloropropionic acid (2,2-DCP). Interestingly, the MX1 strain grew best in a 20 mM 2,2-DCP minimal medium as the sole carbon source and illustrated a 44 ± 0.2 h cell-doubling time as well as a 38 mol Cl-/ml maximum rate of chloride ion release. However, 2,2-DCP-containing medium with concentrations that exceeded 30 mM inhibited the growth of the MX1, possibly attributable to the increased toxicity of the compound on the bacteria. Biochemical examinations and 16S rDNA sequence analysis revealed that the MX1 strain shares high identity to Pseudomonas aeruginosa, and the gene sequence was deposited into GenBank as Pseudomonas aeruginosa MX1 under accession number KP336490. The presence of the putative dehalogenase gene in the MX1 strain was established by polymerase chain reaction (PCR) analysis, which proved the presence of conserved amino acid residues belonging to the Group I dehalogenase. This is the first report detailing a P. aeruginosa strain capable of degrading the recalcitrant 2,2-DCP and its functional amino acid residues.