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

Autores
Morales Urrea, Diego Alberto; Haure, Patricia Mónica; García Einschlag, Fernando Sebastián; Contreras, Edgardo Martín
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Física
Ciencias Exactas
Horseradish peroxidase
Orange II
Hydrogen peroxide
Decolourization
Kinetic model
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/140336

id SEDICI_db967215e62303f443b29618c94d3c58
oai_identifier_str oai:sedici.unlp.edu.ar:10915/140336
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network_name_str SEDICI (UNLP)
spelling Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH valuesMorales Urrea, Diego AlbertoHaure, Patricia MónicaGarcía Einschlag, Fernando SebastiánContreras, Edgardo MartínFísicaCiencias ExactasHorseradish peroxidaseOrange IIHydrogen peroxideDecolourizationKinetic modelEnzymatic 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.Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2018-05-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf19989-20002http://sedici.unlp.edu.ar/handle/10915/140336enginfo:eu-repo/semantics/altIdentifier/issn/1614-7499info:eu-repo/semantics/altIdentifier/issn/0944-1344info:eu-repo/semantics/altIdentifier/doi/10.1007/s11356-018-2134-8info:eu-repo/semantics/altIdentifier/pmid/29744778info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:32:03Zoai:sedici.unlp.edu.ar:10915/140336Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:32:03.323SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
title Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
spellingShingle Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
Morales Urrea, Diego Alberto
Física
Ciencias Exactas
Horseradish peroxidase
Orange II
Hydrogen peroxide
Decolourization
Kinetic model
title_short Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
title_full Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
title_fullStr Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
title_full_unstemmed Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
title_sort Horseradish peroxidase-mediated decolourization of Orange II: modelling hydrogen peroxide utilization efficiency at different pH values
dc.creator.none.fl_str_mv Morales Urrea, Diego Alberto
Haure, Patricia Mónica
García Einschlag, Fernando Sebastián
Contreras, Edgardo Martín
author Morales Urrea, Diego Alberto
author_facet Morales Urrea, Diego Alberto
Haure, Patricia Mónica
García Einschlag, Fernando Sebastián
Contreras, Edgardo Martín
author_role author
author2 Haure, Patricia Mónica
García Einschlag, Fernando Sebastián
Contreras, Edgardo Martín
author2_role author
author
author
dc.subject.none.fl_str_mv Física
Ciencias Exactas
Horseradish peroxidase
Orange II
Hydrogen peroxide
Decolourization
Kinetic model
topic Física
Ciencias Exactas
Horseradish peroxidase
Orange II
Hydrogen peroxide
Decolourization
Kinetic model
dc.description.none.fl_txt_mv 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.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
description 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.
publishDate 2018
dc.date.none.fl_str_mv 2018-05-09
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info:eu-repo/semantics/publishedVersion
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info:eu-repo/semantics/altIdentifier/issn/0944-1344
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11356-018-2134-8
info:eu-repo/semantics/altIdentifier/pmid/29744778
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
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rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
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