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Environmental Science and Pollution Research

, Volume 25, Issue 20, pp 19989–20002 | Cite as

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

  • Diego Alberto Morales Urrea
  • Patricia Mónica Haure
  • Fernando Sebastián García Einschlag
  • Edgardo Martín Contreras
Research Article
  • 34 Downloads

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.

Keywords

Horseradish peroxidase Orange II Hydrogen peroxide Decolourization Kinetic model 

Nomenclature

A

absorbance

Af

absorbance at the end of the a decolourization experiment

Amin

minimum absorbance obtained under the excess of hydrogen peroxide

E

dissociated form of the enzyme

E0

resting state of the enzyme

E1

compound I of the enzyme

E2

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

PC

critical hydrogen peroxide concentration

q0

initial specific decolourization rate

S

reducing substrate

VS0

initial reducing substrate consumption rate

VD0

initial decolourization rate

VS

reducing substrate consumption rate

VD

decolourization rate

X

oxidation products obtained at basic conditions

Y

oxidation products obtained at acid conditions

YP/S

observable stoichiometric coefficient of decolourization

Notes

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.

Supplementary material

11356_2018_2134_MOESM1_ESM.docx (276 kb)
ESM 1 (DOCX 276 kb)

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Diego Alberto Morales Urrea
    • 1
  • Patricia Mónica Haure
    • 1
    • 2
  • Fernando Sebastián García Einschlag
    • 3
    • 4
  • Edgardo Martín Contreras
    • 1
  1. 1.Instituto de Investigaciones en Ciencia y Tecnología de Materiales (INTEMA)CCT - Mar del Plata CONICETMar del PlataArgentina
  2. 2.Facultad de IngenieríaUniversidad Nacional de Mar del Plata (UNMdP)Mar del PlataArgentina
  3. 3.Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (INIFTA)CCT - La Plata – CONICETLa PlataArgentina
  4. 4.Facultad de IngenieríaUniversidad Nacional de La Plata (UNLP)La PlataArgentina

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