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Articles

Statistical optimization for enhanced decolorization of Golden Yellow PRA by Citrus reticulata var. kinnow peroxidase and phytotoxicity evaluation of its degraded products

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Pages 16981-16994 | Received 12 Dec 2014, Accepted 10 Aug 2015, Published online: 01 Sep 2015

References

  • C. Ashoka, M.S. Geetha, S.B. Sullia, Bioleaching of composite textile dye effluent using bacterial consortia, Asian J. Microbiol. Biotechnol. Environ. Sci. 4 (2002) 65–68.
  • F. Rafii, W. Freankalin, C.E. Cerniglia, Azo-reductase activity of anaerobic bacteria isolated from human intestinal microflora, Appl. Environ. Microbiol. 56 (1990) 2146–2151.
  • A.A. Dias, M.R. Bezerra, M.P. Lemos, N.A. Pereira, In vivo and lacasse catalysed decolorization of xenobiotic azo dyes by a basidiomycetous fungus: Characterization of its ligninolytic system, World J. Microbiol. Biotechnol. 19 (2003) 969–975.
  • C. Allege, P. Moulin, M. Maisseu, F. Charbit, Treatment and reuse of reactive dyeing effluents, J. Membr. Sci. 269(1–2) (2006) 15–34.
  • A. Bhunia, D. Susheel, P.P. Wangikar, Horseradish peroxidase catalyzed degradation of industrially important dyes, Biotechnol. Bioeng. 72 (2001) 562–567.
  • N. Boucherit, M. Abouseoud, L. Adour, Degradation of direct azo dye by Cucurbita pepo free and immobilized peroxidase, J. Environ. Sci. 25(6) (2013) 1235–1244.
  • M. Celebi, A. Kaya, M. Altikatoglu, H. Yıldırım, Enzymatic decolorization of anthraquinone and diazo dyes using Horseradish peroxidase enzyme immobilized on to various polusulfone supports, Appl. Biochem. Biotechnol. 171(3) (2013) 716–730.
  • T. Chanwun, N. Muhamad, N. Chirapongsatonkul, N. Churngchow, Heveabra siliensis cell suspension peroxidase: Purification, characterization and application for dye decolorization, AMB Express 3 (2013) 14.
  • P. Verma, D. Madamwar, Production of ligninolytic enzymes for dye decolorization by co cultivation of white-rot fungi Pleurotus ostreatus and Phanerochaete chryosporium under solid-state fermentation, Appl. Biochem. Biotechnol. 102–103 (2002) 109–118.
  • I. Mielgo, C. López, M.T. Moreira, G. Feijoo, J.M. Lema, Oxidative degradation of azo dyes by manganese peroxidase under optimized conditions, Biotechnol. Prog. 19 (2003) 325–331.
  • Q. Husain, Peroxidase mediated decolorization and remediation of wastewater containing industrial dyes: A review, Rev. Environ. Sci. Biotechnol. 9 (2010) 117–140.
  • J.N. Rodriguez-Lopez, J.C. Espin, F. del Amor, J. Tudela, V. Martinez, A. Cerda, F. Garcia-Canovas, Purification and kinetic characterization of an anionic peroxidase from melon (Cucumismelo L.) cultivated under different salinity conditions, J. Agric. Food Chem. 48 (2000) 1537–1541.
  • A. Neves, Ionically bound peroxidase from peach fruit, Braz. Arch. Biol. Technol. 45(1) (2002) 7–16.
  • H. Gülen, C. Çetinkaya, M. Kadıoğlu, M. Kesici, A. Cansev, A. Eriş, Peroxidase activity and lipid peroxidation in strawberry (Fragaria ananassa) plants under low temperature, J. Biol. Environ. Sci. 2(6) (2008) 95–100.
  • J. Singh, A. Dubey, S.K. Diwakar, S.K. Rawat, N. Batra, A. Joshi, Characterization of ionically bound peroxidases from apple (Malluspumilus) Fruits, Int. Res. J. Biotechnol. 1(4) (2010) 050–058.
  • V.P. Pandey, S. Singh, R. Singh, U.N. Dwivedi, Purification and characterization of peroxidase from papaya (Carica papaya) Fruit, Appl. Biochem. Biotechnol. 167 (2012) 367–376.
  • S. Nouren, H.N. Bhatti, I.A. Bhatti, M. Asgher, Kinetic and thermal characterization of peroxidase from peels of Citrus reticulate var Kinnow, J. Anim. Plant Sci. 23(2) (2013) 430–435.
  • S. Nouren, H.N. Bhatti, Mechanistic study of degradation of Basic violet 3 by Citrus limon peroxidase and phytotoxicity assessment of its degradation products, Biochem. Eng. J. 95 (2015) 9–19.
  • H.N. Bhatti, A. Najma, M. Asgher, M.A. Hanif, M.A. Zia, Purification and thermal characterization of a novel peroxidase from a local chick pea cultivar, Protein Pept. Lett. 8(13) (2006) 799–804.
  • W. Liu, J. Fang, W.M. Zhu, P.J. Gao, Isolation, purification and properties of the peroxidase from the hull of Glycine max var HH2 J. Sci. Food Agri. 79 (1999) 779–785.
  • H. Cho, K.D. Zoh, Photocatalytic degradation of azo dye (reactive red 120) in TiO2/UV system: Optimization and modeling using a response surface methodology (RSM) based on the central composite design, Dyes Pigm. 75 (2007) 533–543.
  • M.B. Kasiri, H. Aleboyeh, A. Aleboyeh, Modeling and optimization of heterogeneous photo-fenton process with response surface methodology and artificial neural networks, Environ. Sci. Technol. 42 (2008) 7970–7975.
  • Y. Goksungur, S. Uren, U. Guvenc, Biosorption of cadmium and lead ions by ethanol treated waste baker’s yeast biomass, Bioresour. Technol. 96 (2005) 103–109.
  • Z. Aksu, F. Gonen, Binary biosorption of phenol and chromium(VI) onto immobilized activated sludge in a packed bed: Prediction of kinetic parameters and breakthrough curves, Sep. Purif. Technol. 49 (2006) 205–216.
  • Z. Aksu, F. Gonen, Z. Demircan, Biosorption of chromium(VI) ions by Mowital B3OH resin immobilized activated sludge in a packed bed: Comparison with granular activated carbon, Process Biochem. 38 (2002) 175–186.
  • F. Zucconi, A. Monaco, M. Forte, M. De-Bertoldi, Phytotoxins during the stabilization of organic matter, in: J.K.R. Gasser, Commission European Communities (Ed.), Composting of Agricultural and Other Wastes, Elsevier Applied Science Publishers, London, 1985, pp. 73–86.
  • D. Voet, J.G. Voet, Mechanisms of enzyme action, in: Woolsey (Ed.), Biochemistry, first ed., Wiley, New York, NY, 1990, p. 344.
  • Y. Dong, J. Chen, C. Li, H. Zhu, Decoloration of three azo dyes in water by photocatalysis of Fe(III)-oxalate complexes/H2O2 in the presence of inorganic salts, Dyes Pigm. 73 (2007) 261–268.
  • S.V. Mohan, K.K. Prasad, N.C. Rao, P.N. Sarma, Acid azo dye degradation by free and immobilized horseradish peroxidase catalyzed process, Chemosphere 58 (2005) 1097–1105.
  • F. Jamal, T. Qidwai, P.K. Pandey, D. Singh, Catalytic potential of cauliflower (Brassica oleracea) bud peroxidase in decolorization of synthetic recalcitrant dyes using redox mediator, Catal. Commun. 15 (2011) 93–98.
  • R. Satar, Q. Husain, Catalyzed degradation of disperse dyes by calcium alginate-pectin entrapped bitter gourd (Momordica charantia) peroxidase, J. Environ. Sci. 23(7) (2011) 1135–1142.
  • M. Celebi, M. Altikatoglu, Z.M. Akdeste, Z. Mustafaeva, H. Yıldırım, Determination of decolorization properties of Reactive Blue 19 dye using Horseradish Peroxidase enzyme, Turk. J. Biochem. 37(2) (2012) 200–206.
  • M.L. Shuler, F. Kargi, Bioprocess Engineering—Basic Concepts, Prentice Hall PTR, Englewood Cliffs, NJ, 1992, pp. 58–102.
  • F.M. Reis da Silva, L.R. Vasconcelos de Sa′, C. Russo, E. Scio, V.S. Ferreira-Leit˜ao, The use of HRP in decolorization of Reactive dyes and toxicological evaluation of their products, Enzyme Res. 1–7 (2010), doi: 10.4061/2010/703824.
  • F. Jamal, T. Qidwai, P.K. Pandey, R. Singh, S. Singh, Azo and anthraquinone dye decolorization in relation to its molecular structure using soluble Trichosanthes dioica peroxidase supplemented with redox mediator, Catal. Commun. 12 (2011) 1218–1223.
  • J.Z. Liu, T.L. Wang, L.N. Ji, Enhanced dye decolorization efficiency by citraconic anhydride-modified horseradish peroxidase, J. Mol. Catal. B: Enzym. 41 (2006) 81–86.
  • S. Akhtar, A.A. Khan, Q. Husain, Potential of immobilized bitter gourd (Momordica charantia) peroxidases in the decolorization and removal of textile dyes from polluted wastewater and dyeing effluent, Chemosphere 60 (2005) 291–301.
  • S.M.A.G. Ulson de Souza, E. Forgiarini, A.A. Ulson de Souza, Toxicity of textile dyes and their degradation by the enzyme horseradish peroxidase (HRP), J. Hazard. Mater. 147 (2007) 1073–1078.
  • M.C. Silva, A.D. Corrêa, M.T.S.P. Amorim, P. Parpot, J.A. Torres, P.M.B. Chagas, Decolorization of the phthalocyanine dye reactive blue 21 by turnip peroxidase and assessment of its oxidation products, J. Mol. Catal. B: Enzym. 77 (2012) 9–14.
  • B.J. Dutka, Methods for Microbiological and Toxicological Analysis of Waters, Wastewaters, and Sediments, Environment Canada, Burlington, 1989.
  • J. Wu, J.K. Bewtra, N. Biswas, K.E. Taylor, Effect of H2O2 addition mode on enzymatic removal of phenol from wastewater in the presence of polyethylene glycol, Can. J. Chem. Eng. 72 (1994) 881–886.
  • L.M. Vasantha, H.B. Vuringi, A. Yerramilli, Degradation of azo dye with horseradish peroxidase (HRP), J. Indian Inst. Sci. 86(5) (2006) 507–514.
  • A.C. Osuji, S.O.O. Eze, E.E. Osayi, F.C. Chilaka, Biobleaching of industrial important dyes with peroxidase partially purified from garlic, Sci. World J. (2014), doi: 10.1155/2014/183163.
  • S. Pirillo, F.S.G. Einschlag, M.L. Ferreira, E.H. Rueda, Eriochrome Blue Black R and Fluorescein degradation by hydrogen peroxide oxidation with horseradish peroxidase and hematin as biocatalyst, J. Mol. Catal. B: Enzym. 66 (2010) 63–71.
  • F. Jamal, T. Qidwai, P.K. Pandey, Soluble Fraction of Trichosanthes diocia peroxidase in decolorization of Reactive Orange 15, J. Ecobiotechnol. 2(5) (2010) 36–41.
  • F. d’Acunzo, C. Galli, P. Gentili, F. Sergi, Mechanistic and steric issues in the oxidation of phenolic and non-phenolic compounds by laccase or laccase-mediator systems, the case of bifunctional substrates, New J. Chem. 30 (2006) 583–591.
  • P. Baiocco, A.M. Barreca, M. Fabbrini, C. Galli, P. Gentili, Promoting laccase activity towards non-phenolic substrates: A mechanistic investigation with some laccase-mediator systems, Org. Biomol. Chem. 1 (2003) 191–197.
  • F. Xu, H.J.W. Deussen, B. Lopez, L. Lam, K. Li, Enzymatic and electrochemical oxidation of N-hydroxy compounds: Redox potential, electron-transfer kinetics, and radical stability, Eur. J. Biochem. 268 (2001) 4169–4176.
  • M. Fabbrini, C. Galli, P. Gentili, Comparing the catalytic efficiency of some mediators of laccase, J. Mol. Catal. B: Enzym. 16 (2002) 231–240.
  • M. Matto, Q. Husain, Decolorization of direct dyes by salt fractionated turnip proteins enhanced in the presence of hydrogen peroxide and redox mediators, Chemosphere 69 (2007) 338–345.
  • M.B. Kurade, T.R. Waghmode, S.P. Govindwar, Preferential biodegradation of structurally dissimilar dyes from a mixture by Brevibacillus laterosporus, J. Hazard. Mater. 192 (2011) 1746–1755.
  • F. Gönen, Z. Aksu, Single and binary dye and heavy metal bioaccumulation properties of Candida tropicalis: Use of response surface methodology (RSM) for the estimation of removal yields, J. Hazard. Mater. 172 (2009) 1512–1519.
  • S.C.R. Santos, R.A.R. Boaventura, Adsorption modelling of textile dyes by sepiolite, Appl. Clay Sci. 42 (2008) 137.
  • V. Pujari, T.S. Chandra, Statistical optimization of medium components for enhanced riboflavin production by a UV-mutant of Eremothecium ashbyii, Process Biochem. 36 (2000) 31–37.
  • H.F. Pan, Z.P. Xie, W.N. Bao, J.G. Zhang, Optimization of culture conditions to enhance cis-epoxysuccinate hydrolase production in Escherichia coli by response surface methodology, Biochem. Eng. J. 42 (2008) 133–138.
  • U.K. Garg, M.P. Kaur, V.K. Garg, D. Sud, Removal of nickel(II) from aqueous solution by adsorption on agricultural waste biomass using a response surface methodological approach, Bioresour. Technol. 99 (2008) 1325–1331.
  • M. Amini, H. Younesi, N. Bahramifar, A.A. Lorestani, F. Ghorbani, A. Daneshi, M. Sharifzadeh, Application of response surface methodology for optimization of lead biosorption in an aqueous solution by Aspergillus niger, J. Hazard. Mater. 154 (2008) 694–702.
  • A.R. Khataee, G. Dehghan, Optimization of biological treatment of a dye solution by macroalgae Cladophora sp. using response surface methodology, J. Taiwan Inst. Chem. Eng. 42 (2011) 26–33.
  • R.H. Myers, D.C. Montgomery, Response Surface Methodology: Process and Product Optimization Using Designed Experiments, second ed., John Wiley & Sons Inc., USA, 2002.
  • L. Zhao, J. Zhou, Y. Jia, J. Chen, Biodecolorization of Acid Red GR by a newly isolated Dyellagin sengisoli LA-4 using response surface methodology, J. Hazard. Mater. 181 (2010) 602–608.
  • P. Sharma, L. Singh, N. Dilbaghi, Optimization of process variables for decolorization of disperse yellow 211 by Bacillus subtilis using Box–Behnken design, J. Hazard. Mater. 164 (2009) 1024–1029.
  • Y. Kulshrestha, Q. Husain, Decolorization and degradation of acid dyes mediated by salt fractionated turnip (Brassica rapa) peroxidases, Toxicol. Environ. Chem. 89(2) (2007) 255–267.
  • R. Satar, Q. Husain, Applications of Celite-adsorbed white radish (Raphanus sativus) peroxidase in batch process and continuous reactor for the degradation of reactive dyes, Biochem. Eng. J. 46(2) (2009) 96–104.
  • E. Abadulla, T. Tzanov, S. Costa, K.H. Robra, A. Cavaco-Paulo, G.M. Gubitz, Decolorization and detoxification of textile dyes with a laccase from Trametes hirsute, Appl. Environ. Microbiol. 66 (2000) 3357–3362.
  • L. Pereira, A.V. Coelho, C.A. Viegas, M.M.C. dos Santos, M.P. Robalo, L. Martins, Enzymatic biotransformation of the azo dye Sudan Orange G with bacterial CotA-laccase, J. Biotechnol. 139 (2009) 68–77.

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