Skip to main content
SpringerLink
Log in

Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values

Environmental Science and Pollution Research Aims and scope Submit manuscript

Abstract

Enzymatic decolourization of azo-dyes could be a cost-competitive alternative compared to physicochemical or microbiological methods. Stoichiometric and kinetic features of peroxidase-mediated decolourization of azo-dyes by hydrogen peroxide (P) are central for designing purposes. In this work, a modified version of the Dunford mechanism of peroxidases was developed. The proposed model takes into account the inhibition of peroxidases by high concentrations of P, the substrate-dependant catalatic activity of peroxidases (e.g. the decomposition of P to water and oxygen), the generation of oxidation products (OP) and the effect of pH on the decolourization kinetics of the azo-dye Orange II (OII). To obtain the parameters of the proposed model, two series of experiments were performed. In the first set, the effects of initial P concentration (0.01–0.12 mM) and pH (5–10) on the decolourization degree were studied at a constant initial OII concentration (0.045 mM). Obtained results showed that at pH 9–10 and low initial P concentrations, the consumption of P was mainly to oxidize OII. From the proposed model, an expression for the decolourization degree was obtained. In the second set of experiments, the effect of the initial concentrations of OII (0.023–0.090 mM), P (0.02–4.7 mM), HRP (34–136 mg/L) and pH (5–10) on the initial specific decolourization rate (q0) was studied. As a general rule, a noticeable increase in q0 was observed for pHs higher than 7. For a given pH, q0 increased as a function of the initial OII concentration. Besides, there was an inhibitory effect of high P concentrations on q0. To asses the possibility of reusing the enzyme, repeated additions of OII and P were performed. Results showed that the enzyme remained active after six reuse cycles. A satisfactory accordance between the change of the absorbance during these experiments and absorbances calculated using the proposed model was obtained. Considering that this set of data was not used during the fitting procedure of the model, the agreement between predicted and experimental absorbances provides a powerful validation of the model developed in the present work.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price includes VAT (Finland)

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Abbreviations

A :

absorbance

A f :

absorbance at the end of the a decolourization experiment

A min :

minimum absorbance obtained under the excess of hydrogen peroxide

E :

dissociated form of the enzyme

E 0 :

resting state of the enzyme

E 1 :

compound I of the enzyme

E 2 :

compound II of the enzyme

HE :

non-dissociated form of the enzyme

HRP :

horseradish peroxidase

OII :

Orange II

OP :

oxidation products of Orange II

P :

hydrogen peroxide

P C :

critical hydrogen peroxide concentration

q 0 :

initial specific decolourization rate

S :

reducing substrate

V S0 :

initial reducing substrate consumption rate

V D0 :

initial decolourization rate

V S :

reducing substrate consumption rate

V D :

decolourization rate

X :

oxidation products obtained at basic conditions

Y :

oxidation products obtained at acid conditions

Y P/S :

observable stoichiometric coefficient of decolourization

References

  • Ali L, Algaithi R, Habib HM, Souka U, Rauf MA, Ashraf SS (2013) Soybean peroxidase-mediated degradation of an azo dye- a detailed mechanistic study. BMC Biochem 14:35–41

    Article  CAS  Google Scholar 

  • Buchanan ID, Han YS (2000) Assessment of the potential of Arthromyces ramosus peroxidase to remove phenol from industrial wastewaters. Environ Technol 21:545–552

    Article  CAS  Google Scholar 

  • Buchanan ID, Nicell JA (1997) Model development for horseradish peroxidase catalyzed removal of aqueous phenol. Biotechnol Bioeng 54:251–261

    Article  CAS  Google Scholar 

  • Buchanan ID, Nicell JA (1999) A simplified model of peroxidase-catalyzed phenol removal from aqueous solution. J Chem Technol Biotechnol 74:669–674

    Article  CAS  Google Scholar 

  • Cabrera C, Cornaglia A, Córdoba A, Magario I, Ferreira ML (2017) Kinetic modelling of the hematin catalysed decolourization of Orange II solutions. Chem Eng Sci 161:127–137

    Article  CAS  Google Scholar 

  • Chahbane N, Popescu DL, Mitchell DA, Chanda A, Lenoir D, Ryabov AD, Schramma KW, Collins TJ (2007) FeIII–TAML-catalyzed green oxidative degradation of the azo dye Orange II by H2O2 and organic peroxides: products, toxicity, kinetics, and mechanisms. Green Chem 9:49–57

    Article  CAS  Google Scholar 

  • Cheng XB, Jia R, Li PS, Tu SQ, Zhu Q, Tang WZ, Li XD (2007) Studies on the properties and co-immobilization of manganese peroxidase. Enzym Microb Technol 41:258–264

    Article  CAS  Google Scholar 

  • Chiong T, Lau S, Lek ZH, Koh BY, Danquah MK (2016) Enzymatic treatment of methyl orange dye in synthetic wastewater by plant-based peroxidase enzymes. J Environ Chem Eng 4:2500–2509

    Article  CAS  Google Scholar 

  • Darwesh OM, Matter IA, Eida MF (2016) Application of nanotechnology to stabilize peroxidase enzyme and improve it in textile dyes removal from wastewater. Conference proceedings of the 7th International Conference on Water Resources and Arid Environments (ICWRAE 7), pp 465–473

  • Doumic LI, Haure PA, Cassanello MC, Ayude MA (2013) Mineralization and efficiency in the homogeneous Fenton Orange G oxidation. Appl Catal B Environ 142-143:214–221

    Article  CAS  Google Scholar 

  • Doumic LI, Salierno G, Cassanello MC, Haure PA, Ayude MA (2015) Efficient removal of Orange G using Prussian Blue nanoparticles supported over alumina. Catal Today 240:67–72

    Article  CAS  Google Scholar 

  • Dükkanci M, Vinatoru M, Mason TJ (2014) The sonochemical decolourization of textile azo dye Orange II: effects of Fenton type reagents and UV light. Ultrason Sonochem 21:846–853

    Article  CAS  Google Scholar 

  • Dunford HB (2010) Horseradish peroxidase. II. Two-electron reactions, ferrous peroxidase, compound III, the five oxidation states, oxygen evolution and inactivation. In: Dunford HB (ed) Peroxidases and catalases: Biochemistry, biophysics, biotechnology, and physiology, 2nd edn. Wiley, New Jersey, pp 41–57

    Google Scholar 

  • Dunford HB, Stillman JS (1976) On the function and mechanism of action of peroxidases. Coord Chem Rev 19:187–251

    Article  CAS  Google Scholar 

  • Forgacs E, Cserhatia T, Oros G (2004) Removal of synthetic dyes from wastewaters: a review. Environ Int 30:953–971

    Article  CAS  Google Scholar 

  • Franciscon E, Piubeli F, Garboggini FF, De Menezes CR, Silva IS, Paulo AC, Grossman MJ, Durrant LR (2010) Polymerization study of the aromatic amines generated by the biodegradation of azo dyes using the laccase enzyme. Enzym Microb Technol 46:360–365

    Article  CAS  Google Scholar 

  • Frey PA, Hegeman AD (2007) Enzymatic reaction mechanisms. Oxford University Press, Inc, Oxford

    Google Scholar 

  • Gómez JL, Bódalo A, Gómez E, Bastida J, Hidalgo AM, Gómez M (2008) A covered particle deactivation model and an expanded Dunford mechanism for the kinetic analysis of the immobilized SBP/phenol/hydrogen peroxide system. Chem Eng J 138:460–473

    Article  CAS  Google Scholar 

  • Inchaurrondo N, Font J, Ramos CP, Haure P (2016) Natural diatomites: efficient green catalyst for Fenton-like oxidation of Orange II. Appl Catal B Environ 181:481–494

    Article  CAS  Google Scholar 

  • Jakopitsch C, Wanasinghe A, Jantschko W, Furtmuller PG, Obinger C (2005) Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type Synechocystis catalase-peroxidase and Y249F. Proposal for the catalatic mechanism. J Biol Chem 280(10):9037–9042

    Article  CAS  Google Scholar 

  • Kalsoom U, Ashraf SS, Meetani MA, Rauf MA, Bhatti HN (2013) Mechanistic study of a diazo dye degradation by soybean peroxidase. Chem Cent J 7:1–10

    Article  CAS  Google Scholar 

  • Lau Y-Y, Wong Y-S, Teng T-T, Morad N, Rafatullah M, Ong S-A (2014) Coagulation-flocculation of azo dye Acid Orange 7 with green refined laterite soil. Chem Eng J 246:383–390

    Article  CAS  Google Scholar 

  • Li F, Li G, Zhang X (2014) Mechanism of enhanced removal of quinonic intermediates during electrochemical oxidation of Orange II under ultraviolet irradiation. J Environ Sci 26:708–715

    Article  CAS  Google Scholar 

  • Lin H, Zhang H, Wang X, Wang L, Wu J (2014) Electro-Fenton removal of Orange II in a divided cell: reaction mechanism, degradation pathway and toxicity evolution. Sep Purif Technol 122:533–540

    Article  CAS  Google Scholar 

  • Lopez C (2005) Oxidación del tinte azo Orange II mediante MnP en reactores enzimáticos operados en continuo. Ph.D. Thesis. Universidade de Santiago de Compostela. Santiago de Compostela

  • Lopez C, Valade AG, Combourieu B, Mielgo I, Bouchon B, Lema JM (2004) Mechanism of enzymatic degradation of the azo dye Orange II determined by ex situ 1H nuclear magnetic resonance and electrospray ionization-ion trap mass spectrometry. Anal Biochem 335:135–149

    Article  CAS  Google Scholar 

  • Mo JH, Lee YH, Kim J, Jeong JY, Jegal J (2008) Treatment of dye aqueous solutions using nanofiltration polyamide composite membranes for the dye wastewater reuse. Dyes Pigments 76:429–434

    Article  CAS  Google Scholar 

  • Nicell JA, Wright H (1997) A model of peroxidase activity with inhibition by hydrogen peroxide. Enzym Microb Technol 21:302–310

    Article  CAS  Google Scholar 

  • Oakes J, Gratton P (1998) Kinetic investigations of azo dye oxidation in aqueous media. J Chem Soc Perkin Trans 2:1857–1864

    Article  Google Scholar 

  • Olsen LF, Hauser MJB, Kummer U (2003) Mechanism of protection of peroxidase activity by oscillatory dynamics. Eur J Biochem 270:2796–2804

    Article  CAS  Google Scholar 

  • Rache ML, García AR, Zea HR, Silva AMT, Madeira LM, Ramírez JH (2014) Azo-dye orange II degradation by the heterogeneous Fenton-likeprocess using a zeolite Y-Fe catalyst—kinetics with a model based onthe Fermi’s equation. Appl Catal B Environ 146:192–200

    Article  CAS  Google Scholar 

  • Rauf MA, Ashraf SS (2012) Survey of recent trends in biochemically assisted degradation of dyes. Chem Eng J 209:520–530

    Article  CAS  Google Scholar 

  • Sahare P, Ayala M, Vazquez-Duhalt R, Pal U, Loni A, Canham LT, Osorio I, Agarwal V (2016) Enhancement of peroxidase stability against oxidative self-inactivation by co-immobilization with a redox-active protein in mesoporous silicon and silica microparticles. Nanoscale Res Lett 11:417–427

    Article  CAS  Google Scholar 

  • Saratale RG, Saratale GD, Chang JS, Govindwar SP (2011) Bacterial decolorization and degradation of azo dyes: a review. J Taiwan Inst Chem Eng 42:138–157

    Article  CAS  Google Scholar 

  • Satar R, Husain Q (2009) Applications of Celite-adsorbed white radish (Raphanus sativus) peroxidase in batch process and continuous reactor for the degradation of reactive dyes. Biochem Eng J 46:96–104

    Article  CAS  Google Scholar 

  • Sudha M, Saranya A, Selvakumar G, Sivakumar N (2014) Microbial degradation of azo dyes: a review. Int J Curr Microbiol App Sci 3(2):670–690

    CAS  Google Scholar 

  • Tijskens LMM, Greiner R, Biekman ESA, Konietzny U (2001) Modeling the effect of temperature and pH on activity of enzymes: the case of phytases. Biotechnol Bioeng 72(3):323–330

    Article  CAS  Google Scholar 

  • Tizaouia C, Grima N (2011) Kinetics of the ozone oxidation of reactive Orange 16 azo-dye in aqueous solution. Chem Eng J 173:463–473

    Article  CAS  Google Scholar 

  • Wu J, Taylor KE, Biswas N, Bewtra JK (1999) Kinetic model for removal of phenol by horseradish peroxidase with PEG. J Environ Eng 125:451–458

    Article  CAS  Google Scholar 

  • Zhang L, Chen L, Liu X, Zhang W (2015) Effective removal of azo-dye orange II from aqueous solution by zirconium-based chitosan microcomposite adsorbent. RSC Adv 5:93840–93849

    Article  CAS  Google Scholar 

  • Zhou G, Guo J, Zhou G, Wan X, Shi H (2016) Photodegradation of Orange II using waste paper sludge-derived heterogeneous catalyst in the presence of oxalate under ultraviolet light emitting diode irradiation. J Environ Sci 47:63–70

    Article  Google Scholar 

Download references

Acknowledgements

The authors gratefully acknowledge the financial support from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), by Universidad Nacional de la Plata (UNLP) and by Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT), Argentina.

Author information

Authors and Affiliations

  1. Instituto de Investigaciones en Ciencia y Tecnología de Materiales (INTEMA), CCT - Mar del Plata CONICET, Av. Juan B. Justo 4302 (7600), Mar del Plata, Argentina

    Diego Alberto Morales Urrea, Patricia Mónica Haure & Edgardo Martín Contreras

  2. Facultad de Ingeniería, Universidad Nacional de Mar del Plata (UNMdP), Av. Juan B. Justo 4302 (7600), Mar del Plata, Argentina

    Patricia Mónica Haure

  3. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (INIFTA), CCT - La Plata – CONICET, Diag 113 y 64 (1900), La Plata, Argentina

    Fernando Sebastián García Einschlag

  4. Facultad de Ingeniería, Universidad Nacional de La Plata (UNLP), Av. 1 #750 (1900), La Plata, Argentina

    Fernando Sebastián García Einschlag

Authors
  1. Diego Alberto Morales Urrea
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Patricia Mónica Haure
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Fernando Sebastián García Einschlag
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Edgardo Martín Contreras
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Edgardo Martín Contreras.

Additional information

Responsible editor: Vítor Pais Vilar

Electronic supplementary material

ESM 1

(DOCX 276 kb)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Morales Urrea, D.A., Haure, P.M., García Einschlag, F.S. et al. Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values. Environ Sci Pollut Res 25, 19989–20002 (2018). https://doi.org/10.1007/s11356-018-2134-8

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11356-018-2134-8

Keywords

Search

Navigation