DOI QR코드

DOI QR Code

Immobilization of oxidative enzymes onto Cu-activated zeolite to catalyze 4-chlorophenol decomposition

  • 투고 : 2020.01.11
  • 심사 : 2020.01.17
  • 발행 : 2020.05.25

초록

In this study, a biocatalyst composite was prepared by immobilizing oxidoreductases onto Cu-activated zeolite to facilitate biochemical decomposition of 4-chlorophenol (4-CP). 4-CP monooxygenase (CphC-I) was cloned from a 4-CP degrading bacterium, Pseudarthrobacter chlorophenolicus A6, and then overexpressed and purified. Type X zeolite was synthesized from non-magnetic coal fly ash using acetic acid treatment, and its surfaces were coated with copper ions via impregnation (Cu-zeolite). Then, the recombinant oxidative and reductive enzymes were immobilized onto Cu-zeolite. The enzymes were effectively immobilized onto the Cu-zeolite (79% of immobilization yield). The retained catalytic activity of CphC-I after immobilization was 0.3423 U/g-Cu-zeolite, which was 63.3% of the value of free enzymes. The results of this study suggest that copper can be used as an effective enzyme immobilization binder because it provides favorable metalhistidine binding between the enzyme and Cu-zeolite.

키워드

과제정보

This work was supported by the Korea Institute of Energy Technology Evaluation and Planning (KETEP) and the Ministry of Trade, Industry and Energy (MOTIE, 20194010201900), and the National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (2019R1A2C1008706).

참고문헌

  1. Agency for Toxic Substances and Diseases Registry (ATSDR) (1999), Toxicological Profile for Chlorophenols, U.S. Department of Health and Human Services, Public Service Health, Atlanta, U.S.
  2. Arora, P.K. and Bae, H. (2014), "Bacterial degradation of chlorophenols and their derivatives", Microb. Cell Fact., 13, 1-17. https://doi.org/10.1186/1475-2859-13-31.
  3. Basso, A. and Serban, S. (2019), "Industrial applications of immobilized enzymes-A review." Molecular Catalysis, 479, 110607. https://doi.org/10.1016/j.mcat.2019.110607.
  4. Baumer, J.D., Valerio, A., de Souza, S.M.A.G.U., Erzinger, G.S., Jr, A.F. and de Souza, A.A.U. (2018), "Toxicity of enzymatically decolored textile dyes solution by horseradish peroxidase", J. Hazard Mater. 360, 82-88. https://doi.org/10.1016/j.jhazmat.2018.07.102.
  5. Busse, H.J. (2016), "Review of the taxonomy of the genus Arthrobacter, emendation of the genus Arthrobacter sensu lato, proposal to reclassify selected species of the genus Arthrobacter in the novel general Glutamicibacter gen. nov., Paeniglutamicibacter gen. nov., Pseudoglutamicibacter gen. nov., Paenarthrobacter gen. nov. and Pseudarthrobacter gen. nov., and emended description of Arthrobacter roseus", Int. J. Syst. Evol. Microbiol., 66(1), 9-37. https://doi.org/10.1099/ijsem.0.000702.
  6. Balcke, G.U., Kulikova, N.A., Hesse, S., Kopinke, F.D., Perminova, I.V. and Frimmel, F.H. (2002), "Adsorption of humic substances onto kaolin clay related to their structural features", Soil Sci. Soc. Am. J. 66(6), 1805-1812. 10.2136/sssaj2002.1805.
  7. Chung, H. K., Kim, W. H., Park, J., Cho, J., Jeong, T. Y. and Park, P.K. (2015), "Application of Langmuir and Freundlich isotherms to predict adsorbate removal efficiency or required amount of adsorbent", J. Industrial Eng. Chem., 28, 241-246. https://doi.org/10.1016/j.jiec.2015.02.021.
  8. Cho, S. Y., Kwean, O. S., Yang, J. W., Cho, W., Kwak, S., Park, S., Lim, Y. and Kim, H.S. (2017), "Identification of the upstream 4-chlorophenol biodegradation pathway using a recombinant monooxygenase from Arthrobacter chlorophenolicus A6", Bioresource Technol., 245, 1800-1807. https://doi.org/10.1016/j.biortech.2017.05.006.
  9. Melo, C. F., Dezotti, M. and Marques, M.R.C. (2016), "A comparison between the oxidation with laccase and horseradish peroxidase for triclosan conversion", Environ. Technol., 37(3), 335-343. https://doi.org/10.1080/09593330.2015.1069897.
  10. Kang, C., Yang, J. W., Cho, W., Kwak, S., Park, S., Lim, Y., Choe, J.W. and Kim, H.S. (2017), "Oxidative biodegradation of 4-chlorophenol by using recombinant monooxygenase cloned and overexpressed from Arthrobacter chlorophenolicus A6", Bioresource Technol., 240, 123-129. https://doi.org/10.1016/j.biortech.2017.03.078.
  11. Kim, H. J., Suma, Y., Lee, S. H., Kim, J. A. and Kim, H.S. (2012), "Immobilization of horseradish peroxidase onto clay minerals using soil organic matter for phenol removal", J. Molecular Catalysis B Enzymatic, 83, 8-15. https://doi.org/10.1016/j.molcatb.2012.06.012.
  12. Kwean, O. S., Cho, S. Y., Yang, J. W., Cho, W., Park, S., Lim, Y., Shin, M., Kim, H., Park, J. and Kim, H.S. (2018), "4-Chlorophenol biodegradation facilitator composed of recombinant multi-biocatalysts immobilized onto montmorillonite", Bioresource Technol., 259, 268-275. https://doi.org/10.1016/j.biortech.2018.03.066.
  13. Lai, Y.C. and Lin, S.C. (2005), "Application of immobilized horseradish peroxidase for the removal of p-chlorophenol from aqueous solution", Process Biochem., 40(3-4), 1167-1174. https://doi.org/10.1016/j.procbio.2004.04.009.
  14. Lee, S.H., Lee, S.H., Ryu, S.J., Kang, C.S., Suma, Y. and Kim, H.S., (2013), "Effective biochemical decomposition of chlorinated aromatic hydrocarbons with a biocatalyst immobilized on a natural enzyme support", Bioresource Technol., 141, 89-96. https://doi.org/10.1016/j.biortech.2013.01.159.
  15. Lim, J. M., Park, J., Park, J. T., Bae, S., (2019), "Preparation of quasi-solid-state electrolytes using a coal fly ash derived zeolite-X and-A for dye-sensitized solar cells", J. Industrial Eng. Chem., 71, 378-386. https://doi.org/10.1016/j.jiec.2018.11.049.
  16. Lopes, G.R., Pinto, D.C.G.A. and Silva, A.M.S. (2014), "Horseradish peroxidase (HRP) as a tool in green chemistry", RSC Adv., 4, 37244-37265. 10.1039/C4RA06094F.
  17. Nordin, K. (2004), "4-Chlorophenol biodegradation by Arthrobacter chlorophenolicus A6", Ph.D. Dissertation, Stockholm University, Stockholm.
  18. Qayyum, H., Maroof, H., Yasha, K. (2009), "Remediation and treatment of organopollutants mediated by peroxidases: a review", Crit. Rev. Biotechnol., 29, 94-119. https://doi.org/10.1080/07388550802685306.
  19. Querol, X., Moreno, N., Umana, J. T., Alastuey, A., Hernandez, E., Lopez-Soler, A. and Plana, F. (2002), "Synthesis of zeolites from coal fly ash: an overview", Int. J. Coal Geology, 50(1-4), 413-423. https://doi.org/10.1016/S0166-5162(02)00124-6.
  20. Sheldon, R.A. and van Pelt, S. (2013), "Enzyme immobilisation in biocatalysis: why, what and how", Chem. Soc. Rev., 42, 6223-6235. 10.1039/C3CS60075K.
  21. Veitch, N.C. (2004), "Horseradish peroxidase: a modern view of a classic enzyme", Phytochemistry 65, 249-259. https://doi.org/10.1016/j.phytochem.2003.10.022.
  22. Westerberg, K., Elvang, A.M., Stackebrandt, E. and Jansson, J.K., (2000), "Arthrobacter chlorophenolicus sp. nov., a new species capable of degrading high concentration of 4-chlorophenol", Int. J. Syst. Evol. Microbiol., 50, 2083-2092. https://doi.org/10.1099/00207713-50-6-2083.
  23. Ye, X., Peng, T., Feng, J., Yang, Q., Pratush, A., Xiong, G., Huang, T. and Hu, Z., (2019), "A novel dehydrogenase 17b-HSDx from Rhodococcus sp. P14 with potential application in bioremediation of steroids contaminated environment", J. Hazard Mater., 362, 170-177. https://doi.org/10.1016/j.jhazmat.2018.09.023.