Effects of Peroxidase Enzyme from Cauliflower Stems on Dicofol Removal
Keywords:
Peroxidase, Dicofol, Cauliflower Stem, Hydrogen Peroxide, EnzymeAbstract
This research aims to investigate dicofol removal by peroxidase extracted from cauliflower stem. The factors affecting dicofol removal such as concentration of the enzyme, dicofol concentration, pH value of the solution, temperature and concentration of hydrogen peroxide were tested. The results showed that changing in the enzyme concentration, the concentration of dicofol, the pH value of the solution, the temperature and the concentration of hydrogen peroxide affected the efficiency of dicofol removal. The optimum condition for removal in this study was peroxidase concentration 0.126 U/mL, dicofol 1 mg/L, the pH of the solution at 7, 30 0C and 1 mM hydrogen peroxide. The efficiency of dicofol removal was 94% at 6 h. The above results were used to calculate the amount of dicofol removed per unit of peroxidase and found that 1 unit of peroxidase was able to remove 0.104 mg of dicofol. Therefore, it can be concluded that peroxidase is effective in removing dicofol and the results of this study can be used as a fundamental data for further application.
References
C. R. Mourer, G. L. Hall, W. E. Whitehead, T. Shibamoto, L. R. Shull and S. E. Schwarzbach, “Chromatographic determination of dicofol and metabolites in egg yolks,” Archives of Environmental Contamination and Toxicology, vol. 19, no. 1, pp. 154–156, 1990, doi: 10.1007/bf01059825.
X. Yang, S. Wang, Y. Bian, F. Chen, G. Yu, C. Gu and X. Jiang, “Dicofol application resulted in high DDTs residue in cotton fields from northern Jiangsu province, China,” Journal of Hazardous Materials, vol. 150, no. 1, pp. 92–98, 2008, doi: 10.1016/j.jhazmat.2007.04.076.
A. H. Neilson, “An environmental perspective on the biodegradation of organochlorine xenobiotics,” International Biodeterioration & Biodegradation, vol. 37, no. 1, pp. 3–21, 1996, doi: 10.1016/0964-8305(95)00092-5.
J. Zhang, H. Yan, T. Yang and Y. Zong, “Removal of dicofol from water by immobilized cellulase and its reaction kinetics,” Journal of Environmental Management, vol. 92, no. 1, pp. 53–58, 2011, doi: 10.1016/j.jenvman.2010.08.008.
F. Wang, X. Zhang, C. Huangfu, M. Zhu, C. Li and L. Feng, “The BODIPY-based chemosensor for the fluorometric determination of organochlorine pesticide dicofol,” Food Chemistry, vol. 370, 2022, Art. no. 131033, doi: 10.1016/j.foodchem.2021.131033.
J. -Z. Yang, Z. -X. Wang, L. -H. Ma, X. -B. Shen, Y. Sun, D. -W. Hu and L. -X. Sun, “The organochlorine pesticides residues in the invasive ductal breast cancer patients,” Environmental Toxicology and Pharmacology, vol. 40, no. 3, pp. 698–703, 2015, doi: 10.1016/j.etap.2015.07.007.
N. Gaur, K. Narasimhulu, and P. Y, “Recent advances in the bio-remediation of persistent organic pollutants and its effect on environment,” Journal of Cleaner Production, vol. 198, pp. 1602–1631, 2018, doi: 10.1016/j.jclepro.2018.07.076.
A. A. Sari, S. Tachibana and K. Itoh, “Determination of co-metabolism for 1,1,1-trichloro-2,2-bis(4-chlorophenyl) ethane (DDT) degradation with enzymes from Trametes versicolor U97,” Journal of Bioscience and Bioengineering, vol. 114, no. 2, pp. 176–181, 2012, doi:10.1016/j.jbiosc.2012.03.006.
R. Zhuo and F. Fan, “A comprehensive insight into the application of white rot fungi and their lignocellulolytic enzymes in the removal of organic pollutants,” Science of The Total Environment, vol. 778, 2021, Art. no. 146132, doi: 10.1016/j.scitotenv.2021.146132.
J. Nie, Y. Sun, Y. Zhou, M. Kumar, M. Usman, J. Li, J. Shao, L. Wang and D. C. W. Tsang.,“Bioremediation of water containing pesticides by microalgae: Mechanisms, methods, and prospects for future research,” Science of The Total Environment, vol. 707, 2020, Art. no. 136080, doi: 10.1016/j.scitotenv.2019.136080.
A. Saravanan, P. S. Kumar, D. -V. N. Vo, S. Jeevanantham, S. Karishma and P. R. Yaashikaa, “A review on catalytic-enzyme degradation of toxic environmental pollutants: Microbial enzymes,” Journal of Hazardous Materials, vol. 419, 2021, Art. no. 126451, doi: 10.1016/j.jhazmat.2021.126451.
Q. Chang, J. Huang, Y. Ding and H. Tang, “Catalytic oxidation of phenol and 2,4-Dichlorophenol by using horseradish peroxidase immobilized on graphene oxide/Fe₃O₄,” Molecules, vol. 21, no. 8, 2016, Art. no. 1044, doi: 10.3390/molecules21081044.
M. Hamid and R. Khalil ur, “Potential applications of peroxidases,” Food Chemistry, vol. 115, no. 4, pp. 1177–1186, 2009, doi: 10.1016/j.foodchem.2009.02.035.
K. Sellami, A. Couvert, N. Nasrallah, R. Maachi, M. Abouseoud, and A. Amrane, “Peroxidase enzymes as green catalysts for bioremediation and biotechnological applications: A review,” Science of The Total Environment, vol. 806, 2022, Art. no. 150500, doi: 10.1016/j.scitotenv.2021.150500.
X. Qiu, T. Zhu, B. Yao, J. Hu and S. Hu, “Contribution of dicofol to the current DDT pollution in China,” Environmental Science & Technology, vol. 39, no. 12, pp. 4385–4390, 2005, doi:10.1021/es050342a.
M. C. Lakshmi and K. S. M. S. Raghavarao, “Downstream processing of soy hull peroxidase employing reverse micellar extraction,” Biotechnology and Bioprocess Engineering, vol. 15, pp. 937–945, 2010, doi: 10.1007/s12257-010-0071-6.
M. Svetozarević, N. Šekuljica, A. Onjia, N. Barać, M. Mihajlović, Z. Knežević-Jugović and D. Mijin, “Biodegradation of synthetic dyes by free and cross-linked peroxidase in microfluidic reactor,” Environmental Technology & Innovation, vol. 26, 2022, Art. no. 102373, doi:10.1016/j.eti.2022.102373.
A. Fatima and Q. Husain, “Purification and Characterization of a Novel Peroxidase from Bitter Gourd (Momordica charantia),” Protein & Peptide Letters, vol. 15, no. 4, pp. 377–384, 2008, doi: 10.2174/092986608784246452.
S. S. Kim and D. J. Lee, “Purification and characterization of a cationic peroxidase Cs in Raphanus sativus,” Journal of Plant Physiology, vol. 162, no. 6, pp. 609–617, 2005, doi: 10.1016/j.jplph.2004.10.004.
C. Billaud, L. Louarme and J. Nicolas, “Comparison of peroxidases from barley kernel (Hordeum vulgare L.) and wheat germ (Triticum aestivum L.): isolation and preliminary characterization,” Journal of Food Biochemistry, vol. 23, no. 2, pp. 145–172, 1999, doi: 10.1111/j.17454514.1999.tb00011.x.
T. Köktepe, S. Altın, H. Tohma, İ. Gülçin and E. Köksal, “Purification, characterization and selected inhibition properties of peroxidase from haricot bean (Phaseolus vulgaris L.),” International Journal of Food Properties, vol. 20, no. sup2, pp. 1944–1953, 2017, doi: 10.1080/10942912.2017.1360903.
J. L. Gómez, E. Gómez, J. Bastida, A. M. Hidalgo, M. Gómez and M. D. Murcia, “Experimental behaviour and design model of a continuous tank reactor for removing 4-chlorophenol with soybean peroxidase,” Chemical Engineering and Processing: Process Intensification, vol. 47, no. 9, pp. 1786–1792, 2008, doi: 10.1016/j.cep.2007.09.019.
N. Amini and M. Shamsipur, “Impedimetric mechanism study of horseradish peroxidase at low and high concentrations of hydrogen peroxide based on graphene/sol-gel/horseradish peroxidase,” International Journal of Biological Macromolecules, vol. 123, pp. 677–681, 2019, doi: 10.1016/j.ijbiomac.2018.11.091.
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2022 Faculty of Engineering, King Mongkut’s Institute of Technology Ladkrabang
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
The published articles are copyrighted by the School of Engineering, King Mongkut's Institute of Technology Ladkrabang.
The statements contained in each article in this academic journal are the personal opinions of each author and are not related to King Mongkut's Institute of Technology Ladkrabang and other faculty members in the institute.
Responsibility for all elements of each article belongs to each author; If there are any mistakes, each author is solely responsible for his own articles.
