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Vol. 26 No. 21 (2014): Vol 26 Issue 21

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Decolourization of Drimarene Orange KGL by Orange (Citrus reticulata) Peroxidase

https://doi.org/10.14233/ajchem.2014.16624
Nosheen Hafiz
Department of Chemistry, University of Agriculture, Faisalabad-38040, Pakistan
Haq Nawaz Bhatti
Department of Chemistry, University of Agriculture, Faisalabad-38040, Pakistan
Shazia Nouren
Department of Chemistry, University of Agriculture, Faisalabad-38040, Pakistan
Majid Munir
Department of Chemistry, Government College University, Faisalabad, Pakistan

Corresponding Author(s) : Haq Nawaz Bhatti

hnbhatti2005@yahoo.com; haq_nawaz@uaf.edu.pk

Asian Journal of Chemistry, Vol. 26 No. 21 (2014): Vol 26 Issue 21

Abstract

Reactive dyes are widely employed in textile industries and their removal from wastewaters is a relevant environmental problem. In addition to chemical and physical methods, several bioremediation approaches, involving intact micro-organisms or isolated enzymes have been proposed to decolourize dye solutions. The aim of this study was to evaluate the enzymatic action of partially purified orange (Citrus reticulata) peroxidase for the degradation of industrially important dye Drimarene orange KGL. Studies were carried out to understand the process parameters such as aqueous phase pH, temperature, time, H2O2 dose, dye and enzyme concentrations during enzyme-mediated dye degradation process. Experimental data revealed that 81.36 % degradation of 60 ppm Drimarene orange KGL solution was obtained within 160 min in the presence of 33 U/mL of orange peroxidase, 2 mM H2O2 at pH 4 and 60 °C temperature.

Keywords

Citrus reticulata Drimarene orange KGL Specific activity Ammonium sulphate Degradation
Hafiz, N., Nawaz Bhatti, H., Nouren, S., & Munir, M. (2014). Decolourization of Drimarene Orange KGL by Orange (Citrus reticulata) Peroxidase. Asian Journal of Chemistry, 26(21), 7307–7310. https://doi.org/10.14233/ajchem.2014.16624
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References
  1. T. Robinson, G. McMullan, R. Marchant and P. Nigam, Bioresour. Technol., 77, 247 (2001); doi:10.1016/S0960-8524(00)00080-8.
  2. F.I. Hai, K. Yamamoto and K. Fukushi, Crit. Rev. Environ. Sci. Technol., 37, 315 (2007); doi:10.1080/10643380601174723.
  3. A. Bhunia, S. Durani and P.P. Wangikar, Biotechnol. Bioeng., 72, 562 (2001); doi:10.1002/1097-0290(20010305)72:5<562::AID-BIT1020>3.0.CO;2-S.
  4. T.S. Shaffiqu, J.J. Roy, R.A. Nair and T.E. Abraham, Appl. Biochem. Biotechnol., 102-103, 315 (2002); doi:10.1385/ABAB:102-103:1-6:315.
  5. E. Torres, I. Bustos-Jaimes and S. Le Borgne, Appl. Catal. B, 46, 1 (2003); doi:10.1016/S0926-3373(03)00228-5.
  6. C. Lopez, M.T. Moreira, G. Feijoo and J.M. Lema, Biotechnol. Prog., 20, 74 (2004); doi:10.1021/bp030025c.
  7. Q. Husain, Crit. Rev. Biotechnol., 26, 201 (2006); doi:10.1080/07388550600969936.
  8. S. Akhtar and Q. Husain, Chemosphere, 65, 1228 (2006); doi:10.1016/j.chemosphere.2006.04.049.
  9. G. Boeuf, G. Bauw, B. Legrand and S. Rambour, Plant Physiol. Biochem., 38, 217 (2000); doi:10.1016/S0981-9428(00)00731-2.
  10. H. Chen, Curr. Protein Pept. Sci., 7, 101 (2006); doi:10.2174/138920306776359786.
  11. N. Duran and E. Esposito, Appl. Catal. B, 28, 83 (2000); doi:10.1016/S0926-3373(00)00168-5.
  12. X. Du and H. Liu, Huanjing Huaxue, 6, 12 (1991).
  13. H.N. Bhatti, A. Najma, M. Asgher, M.A. Hanif and M.A. Zia, Protein Pept. Lett., 13, 799 (2006); doi:10.2174/092986606777841271.
  14. A.A. Khan and Q. Husain, Bioresour. Technol., 98, 1012 (2007); doi:10.1016/j.biortech.2006.04.008.
  15. M.M. Bradford, Anal. Biochem., 72, 248 (1976); doi:10.1016/0003-2697(76)90527-3.
  16. W. Liu, J. Fang, W. Zhu and P. Gao, J. Sci. Food Agric., 79, 779 (1999); doi:10.1002/(SICI)1097-0010(199904)79:5<779::AID-JSFA252>3.0.CO;2-9.
  17. S.V. Mohan, K.K. Prasad, N.C. Rao and P.N. Sarma, Chemosphere, 58, 1097 (2005); doi:10.1016/j.chemosphere.2004.09.070.
  18. M.C. Silva, A.D. Corrêa, M.T.S.P. Amorim, P. Parpot, J.A. Torres and P.M.B. Chagas, J. Mol. Catal., B Enzym., 77, 9 (2012); doi:10.1016/j.molcatb.2011.12.006.
  19. C. Fernandez-Sanchez, T. Tzanov, G.M. Gubitz and A. Cavaco-Paulo, Bioelectrochemistry, 58, 149 (2002); doi:10.1016/S1567-5394(02)00119-6.
  20. G.S. Ghodake, S.D. Kalme, J.P. Jadhav and S.P. Govindwar, Appl. Biochem. Biotechnol., 152, 6 (2009); doi:10.1007/s12010-008-8258-4.
  21. F. Jamal, T. Qidwai, P.K. Pandey and D. Singh, Catal. Commun., 15, 93 (2011); doi:10.1016/j.catcom.2011.08.020.
  22. T. Marchis, P. Avetta, A. Bianco-Prevot, D. Fabbri, G. Viscardi and E. Laurenti, J. Inorg. Biochem., 105, 321 (2011); doi:10.1016/j.jinorgbio.2010.11.009.
  23. H.N. Bhatti, U. Kalsoom and A. Habib, J. Chem. Soc. Pak., 34, 257 (2012).
  24. M.S. Silva, J.A. Torres, L.R. Vasconcelos de Sá, P.M.B. Chagas, V.S. Ferreira-Leitão and A.D. Corrêa, J. Mol. Catal. B, 89, 122 (2013); doi:10.1016/j.molcatb.2013.01.004.
  25. S. Schmitt, R. De Souza, F. Bettin, A.J.P. Dillon, J.A.B. Valle and J. Andreaus, Biocatal. Biotransform., 30, 48 (2012); doi:10.3109/10242422.2012.645339.
  26. S.M.A.G. Ulson de Souza, E. Forgiarini and A.A. Ulson de Souza, J. Hazard. Mater., 147, 1073 (2007); doi:10.1016/j.jhazmat.2007.06.003.
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