{"title":"Characterization of Novel Atrazine-Degrading Klebsiella sp. isolated from Thai Agricultural Soil","authors":"Sawangjit Sopid","volume":68,"journal":"International Journal of Agricultural and Biosystems Engineering","pagesStart":618,"pagesEnd":621,"ISSN":"1307-6892","URL":"https:\/\/publications.waset.org\/pdf\/9601","abstract":"
Atrazine, a herbicide widely used in sugarcane and corn production, is a frequently detected groundwater contaminant. An atrazine-degrading bacterium, strain KB02, was obtained from long-term atrazine-treated sugarcane field soils in Kanchanaburi province of Thailand. Strain KB02 had a rod-to-coccus morphological cycle during growth. Sequence analysis of the PCR product indicated that the 16S rRNA gene in strain KB02 was ranging from 97-98% identical to the same region in Klebsiella sp. Based on biochemical, physiological analysis and 16S rDNA sequence analysis of one representative isolate, strain KB02, the isolates belong to the genus Klebsiella in the family Enterobacteriaceae. Interestingly that the various primers for atzA, B and C failed to amplify genomic DNA of strain KB02. Whereas the expected PCR product of atzA, B and C were obtained from the reference strain, Arthrobacter sp. strain KU001.<\/p>\r\n","references":"[1] U.S. Environmental Protection Agency, Rules and regulations.Fed.\r\nRegist, 56:3552, 1991.\r\n[2] A.M. Cook, \"Biodegradation of s-triazine xenobiotics,\" FEMS\r\nMicrobiol.Rev,vol. 46, pp.93-116, 1987.\r\n[3] E.L. Erickson, and K.H. Lee, \"Degradation of atrazine and relatedstriazines,\"\r\nCrit. Rev. Environ. Contam, vol. 19, pp.1-13, 1989.\r\n[4] R.W. Eaton, and J.S. Karns, \"Cloning and comparison of the DNA\r\nencoding ammelide aminohydrolase and cyanuric acid amidohydrolase\r\nfrom three s-triazine-degrading bacterial strain,\" J. Bacteriol, vol. 173,\r\npp.1363-1366, 1991.\r\n[5] C.Yanze-Kontchou, and N. Gschwind, \"Mineralization of the herbicide\r\natrazine as a carbon source by a Pseudomonas strain,\" Appl.Environ.\r\nMicrobiol, vol. 60, pp. 4297-4302, 1994.\r\n[6] C. Bouquard, J. Ouazzani, J.C. Prome, Y. Michel-Briand, and P.\r\nPlesiat,\"Dechlorination of atrazine by a Rhizobium sp. Isolate,\" Appl\r\nEnviron Microbiol, vol. 63, pp. 862-866, 1997.\r\n[7] L.C. Strong, C. Rosendahl, G. Johnson, M.J. Sadowsky, and L.P.\r\nWackett, \"Arthrobacter aurescens TC1 metabolizes diverse s-triazine\r\nring compounds,\" Appl Environ Microbiol, vol. 68, pp.5973-5980,2002.\r\n[8] R.T. Mandelbaum, D.L. Allan, and L.P. Wackett, \"Isolation and\r\ncharacterization of a Pseudomonas sp. that mineralizes the s-triazine\r\nherbicide atrazine,\" Appl Environ Microbiol, vol. 61, pp.1451-1457,\r\n1995.\r\n[9] K.L. Boundy-Mills, M.L. de Souza, R.T. Mandelbaum, L.P. Wackett,\r\nAnd M.J. Sadowsky, \"The atzB gene of Pseudomonas sp. strain ADP\r\nencodes the second enzyme of a novel atrazine degradation pathway,\"\r\nAppl Environ Microbiol, vol. 63, pp. 916-923, 1997.\r\n[10] M.L. de Souza, M.J. Sadowsky, and L.P. Wackett, \"Atrazine\r\nChlorohydrolase from Pseudomonas sp. Strain ADP:Gene Sequence,\r\nEnzyme Purification, and Protein Characterization,\" J Bacteriol, vol.\r\n178, pp. 4894-4900, 1996.\r\n[11] M.J. Sadowsky, Z. Tong, M. de Souza, L.P. Wackett, \"AtzC is a new\r\nmember of the amidohydrolase protein superfamily and is homologous\r\nto other atrazine-metabolizing enzymes,\" J Bacteriol, vol. 180, pp. 152-\r\n158, 1998.\r\n[12] R.W. Eaton, and D.W. Ribbons, \"The metabolism of dimethylphthalate\r\nby Micrococcus sp. strain 12B,\" J Bacteriol, vol. 151, pp. 465-467,\r\n1982.\r\n[13] J. Sambrook, E.F. Fritsch, and T. Maniatis, \"Molecular Cloning: A\r\nLaboratory Manual,\" Cold Spring Harbor Laboratory, New York,\r\n545 p, 1989.\r\n[14] J.D. Thompson, D.G. Higgins, and T.J. Gibson, \"CLUSTAL W:\r\nImproving the sensitivity of progressive multiple sequence alignment\r\nthrough sequence weighting, position-specific gap penalties and weight\r\nmatrix choice,\" Nucleic Acids Res, vol. 22, pp. 4673-4680, 1994.","publisher":"World Academy of Science, Engineering and Technology","index":"Open Science Index 68, 2012"}