Improved expression of Catechol 1,2-dioxygenase gene from Burkholderia cepacia in Escherichia coli
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Keywords

Escherichia coli M15
CAT1
gene expression
dibenzofuran

How to Cite

1.
Dang VT, Hoang AT, Tran GCT, Pham THT, Ha Thanh LT, Nguyen HL. Improved expression of Catechol 1,2-dioxygenase gene from Burkholderia cepacia in Escherichia coli . HueUni-JNS [Internet]. 2020Nov.24 [cited 2021Mar.9];129(1D):61-5. Available from: http://jos.hueuni.edu.vn/index.php/HUJOS-NS/article/view/5974

Abstract

Catechol 1,2-dioxygenase (CAT1) is a key enzyme for the ortho-cleavage pathway involved in the degradation of dibenzofuran, a dioxin derivative, which is a highly toxic environmental pollutant. The present study aims to investigate appropriate culture conditions for enhancing the expression of the cat1 gene encoding CAT1 enzyme from Burkholderia cepacia DF4 in Escherichia coli M15. The optimized culture conditions for gene expression are cell density at the time of induction, shaking speed, induction temperature, induction time, and inducer concentration. The highest level for CAT1 was obtained at the IPTG concentration of 1.2 mM, 10 hours after induction at 35 °C, shaking speed 200 rpm with cell density at OD600 0.7.

https://doi.org/10.26459/hueunijns.v129i1D.5974
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References

  1. Thu NTT. Studying on the diversity of anaerobic bacteria community in bioremediated herbicide/dioxin cells [dissertation]. Hanoi: Vietnam Academy of Science and Technology; 2013.
  2. Ministry of Natural Resources and Environment of Vietnam. Dioxin contamination in Vietnam: Emissions from industries and levels in the environment. Hanoi: Ministry of Natural Resources and Environment of Vietnam; 2014.
  3. Montgomery JH. Groundwater Chemicals Desk Reference, 4th Ed. Florida (US): CRC Press; 2007. p. 328-330.
  4. Thakore KN, Mehendale HM. Dibenzofuran. In: Wexler P, editor. Encyclopedia of Toxicology (3th Ed.). Oxford: Academic Press; 2014. p. 67-69.
  5. Ali F, Hu H, Wang W, Zhou Z, Shah SB, Xu P, et al. Characterization of a dibenzofuran-degrading strain of Pseudomonas aeruginosa FA-HZ1. Environmental Pollution. 2019;250:262-273.
  6. Hiraishi A. Biodiversity of dioxin-degrading microorganisms and potential utilization in bioremediation. Microbes and Environments. 2003; 18(3):105-125.
  7. Giedraityte G, Kalėdienė L. Catechol 1,2-dioxygenase from α-naphthol degrading thermophilic Geobacillus sp. strain: purification and properties. Open Life Sciences. 2009;4(1):68-73.
  8. Schlüter R, Lippmann R, Hammer E, Gesell Salazar M, Schauer F. Novel insights into the fungal oxidation of monoaromatic and biarylic environmental pollutants by characterization of two new ring cleavage enzymes. Applied Microbiology and Biotechnology. 2013;97(11):5043-5053.
  9. Wang Z, Sun Y, Shi Y, Song W, Zhang C. Cloning, expression and characterization of a mesophilic catechol 1,2-dioxygenase from Rhodococcus ruber OA1. Science Alert. 2017;16(1):10-18.
  10. Silva AS, Jacques RJS, Andreazza R, Bento FM, Roesch LFW, Camargo FAO. Properties of catechol 1,2-dioxygenase in the cell free extract and immobilized extract of Mycobacterium fortuitum. Brazilian Journal of Microbiology. 2013;44(1):291-297.
  11. Zhang HB, Mao XQ, Wang YJ, Hu XQ. Optimization of culture conditions for high-level expression of dextransucrase in Escherichia coli. Journal of Food, Agriculture & Environment. 2009;7(3&4):75-78.
  12. Ribeiro VT, Asevedo EA, Vasconcelos LTCP, Filho MAO, Araújo JS, Macedo GR, et al. Evaluation of induction conditions for plasmid pQE-30 stability and 503 antigen of Leishmania i. chagasi expression in E. coli M15. Applied Microbiology and Biotechnology. 2019;103:6495-6504.
  13. Hariprasad G, Hariprasad R, Kumar L, Srinivasan A, Kola S, Kaushik A. Apolipoprotein A1 as a potential biomarker in the ascitic fluid for the differentiation of advanced ovarian cancers. Biomarkers. 2013;18(6):532-541.
  14. Ma D, Ma C, Pan L, Li G, Yang J, Hong J, et al. Vaccination of chickens with DNA vacxin encoding Eimeria acervulina 3-1E and chicken IL-15 offers protection against homologous challenge. Experimental Parasitology. 2011;127(1):208-214.
  15. Huong DT, Quy NT, Ha DTN, Hong LTT, Hai TN. Optimization of fermentation conditions for the expression of interleukin-3 in fusion with PelB in E. coli. Academia Journal of Biology. 2016;38(2):250-256.
  16. Gopal GJ, Kumar A. Strategies for the production of recombinant protein in Escherichia coli. The Protein Journal. 2013;32(6):419-425.
  17. Joseph BC, Pichaimuthu S, Srimeenakshi S, Murthy M, Selvakumar K, Genesan M, et al. An overview of the parameters for recombinant protein expression in Escherichia coli. Journal of Cell Science and Therapy. 2015;6(5).
  18. Ashayeri-Panah M, Eftekhar F, Kazemi B, Joseph J. Cloning, optimization of induction conditions and purification of Mycobacterium tuberculosis Rv1733c protein expressed in Escherichia coli. Iranian Journal of Microbiology. 2017;9(2):64-73.
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