Abstract
Xanthobacter autotrophicus GJ10 has been widely studied because of its ability to degrade halogenated compounds, especially 1,2-dichloroethane (1,2-DCA), which is achieved through chromosomal as well as plasmid pAUX1 encoded 1,2-DCA degrading genes. This work described the gene expression and enzyme activity profiles as well as the intermediates formed during the 1,2-DCA degradation by this organism. A correlation between gene expression, enzyme activity and metabolic intermediates, after the induction of GJ10 grown culture with 1,2-DCA, was established at different time intervals. Haloalkane dehalogenase (dhlA) and haloacid dehalogenase (dhlB) were constitutively expressed while the expression of alcohol dehydrogenase (max) and aldehyde dehydrogenase (ald) was found to be inducible. The DhlA and DhlB activities were relatively higher compared to that of the inducible enzymes, Max and Ald. To the best of our knowledge, this is the first study to correlate gene expression profiles with enzyme activity and metabolite formation during 1,2-DCA degradation process in GJ10. Findings from this study may assist in fully understanding the mechanism of 1,2-DCA degradation by GJ10. It could also assist in the design and implementation of appropriate bioaugmentation strategies for complete removal of 1,2-DCA from contaminated environment.
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References
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
Fetzner S, Lingens F (1994) Bacterial dehalogenases: biochemistry, genetics and biotechnological applications. Microbiol Rev 58:641–685
Govender A, Pillay B (2011a) Characterization of 1, 2-dichloroethane (DCA) degrading bacteria isolated from South African waste water. Afr J Biotechnol 10(55):11567–11573
Govender A, Pillay B (2011b) Biochemical activities of 1,2-dichloroethane (DCA) degrading bacteria. Afr J Biotechnol 10(55):11574–11581
Greet CW, Baumier D, Samson R (1989) Application of on-line sensors during growth of the DCA degrading bacterium Xanthobacter autotrophicus. J Biotechnol 12:261–274
Hage JC, Hartmans S (1999) Monooxygenase-mediated 1,2-dichloroethane degradation by Pseudomonas sp. strain DCA1. Appl Environ Microbiol 65:2466–2470
Janssen DB, Scheper A, Dijkhuizen L, Witaholt B (1985) Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10. Appl Environ Microbiol 49:673–677
Janssen DB, Keuning S, Witholt B (1987) Involvement of a quinoprotein alcohol dehydrogenase and an NAD-dependent aldehyde dehydrogenase in 2-chloroethanol metabolism in Xanthobacter autotrophicus GJ10. J Gen Microbiol 133:85–92
Janssen DB, Pries F, Van der Ploeg J, Kazemier B, Terpstra P, Witholt B (1989) Cloning of 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10, and expression and sequencing of the dhlA gene. J Bacteriol 171:6791–6799
Janssen DB, van der Ploeg JR, Pries F (1994) Genetics and biochemistry of 1,2-dichloroethane degradation. Biodegradation 5:249–257
Janssen DB, Oppentocht JE, Poelarends GJ (2001) Microbial dehalogenation. Curr Opin Biotechnol 12:254–258
Keuning S, Janssen DB, Witholt B (1985) Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J Bacteriol 163:635–639
Nagata Y, Futamura A, Miyauchi K, Takagi M (1999) Two different types of dehalogenases, LinA and LinB, involved in (γ)-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26 are localized in the periplasmic space without molecular processing. J Bacteriol 181:5409–5413
Nishino SF, Shin KA, Gossett JM, Spain JC (2013) Cytochrome p450 initiates degradation of cis-dichloroethene by Polaromonas sp. Strain JS666. Appl Environ Microbiol 79(7):2263–2272
Stucki G, Krebser U, Leisinger T (1983) Bacterial growth on 1,2-dichloroethane. Experientia 39:1271–1273
Tardif G, Greer CW, Labbe D, Lau PCK (1991) Involvement of a large plasmid in the degradation of 1,2-dichloroethane by Xanthobacter autotrophicus GJ10. Appl Environ Microbiol 57:1853–1857
Van den Wijngaard AJ, van der Kamp K, van der Ploeg J, Kazemier B, Pries F, Janssen DB (1992) Degradation of 1,2-dichloroethane by facultative methylotrophic bacteria. Appl Environ Microbiol 58:976–983
Van der Ploeg J, Smidt P, Landa AS, Janssen DB (1994) Identification of chloroacetaldehyde dehydrogenase involved in 1,2-dichloroethane degradation. Appl Environ Microbiol 60:1599–1605
Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW (1993) Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363:693–698
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This study was supported by the National Research Foundation, South Africa. The post-doctoral research fellowship awarded to Ajit Kumar by the University of KwaZulu-Natal is acknowledged.
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Kumar, A., Pillay, B. & Olaniran, A.O. Enzyme activity and gene expression profiles of Xanthobacter autotrophicus GJ10 during aerobic biodegradation of 1,2-dichloroethane. World J Microbiol Biotechnol 31, 1211–1216 (2015). https://doi.org/10.1007/s11274-015-1868-4
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DOI: https://doi.org/10.1007/s11274-015-1868-4