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Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach

Owing to their high surface area, stability, and functional groups on the surface, iron oxide hydroxide nanoparticles have attracted attention as enzymatic support. In this work, a chemometric approach was performed, aiming at the optimization of the horseradish peroxidase (HRP) immobilization proce...

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Autores principales: Tavares, Tássia Silva, da Rocha, Eduardo Pereira, Esteves Nogueira, Francisco Guilherme, Torres, Juliana Arriel, Silva, Maria Cristina, Kuca, Kamil, Ramalho, Teodorico C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024332/
https://www.ncbi.nlm.nih.gov/pubmed/31936386
http://dx.doi.org/10.3390/molecules25020259
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author Tavares, Tássia Silva
da Rocha, Eduardo Pereira
Esteves Nogueira, Francisco Guilherme
Torres, Juliana Arriel
Silva, Maria Cristina
Kuca, Kamil
Ramalho, Teodorico C.
author_facet Tavares, Tássia Silva
da Rocha, Eduardo Pereira
Esteves Nogueira, Francisco Guilherme
Torres, Juliana Arriel
Silva, Maria Cristina
Kuca, Kamil
Ramalho, Teodorico C.
author_sort Tavares, Tássia Silva
collection PubMed
description Owing to their high surface area, stability, and functional groups on the surface, iron oxide hydroxide nanoparticles have attracted attention as enzymatic support. In this work, a chemometric approach was performed, aiming at the optimization of the horseradish peroxidase (HRP) immobilization process on Δ-FeOOH nanoparticles (NPs). The enzyme/NPs ratio (X1), pH (X2), temperature (X3), and time (X4) were the independent variables analyzed, and immobilized enzyme activity was the response variable (Y). The effects of the factors were studied using a factorial design at two levels (−1 and 1). The biocatalyst obtained was evaluated for the ferulic acid (FA) removal, a pollutant model. The materials were characterized by X-ray powder diffraction (XRD), Fourier transform infrared spectroscopy (FTIR), and scanning electron microscopy (SEM). The SEM images indicated changes in material morphology. The independent variables X1 (−0.57), X2 (0.71), and X4 (0.42) presented the significance effects estimate. The variable combinations resulted in two significance effects estimates, X1*X2 (−0.57) and X2*X4 (0.39). The immobilized HRP by optimized conditions (X1 = 1/63 (enzyme/NPs ratio, X2 = pH 8, X4 = 60 °C, and 30 min) showed high efficiency for FA oxidation (82%).
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spelling pubmed-70243322020-03-11 Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach Tavares, Tássia Silva da Rocha, Eduardo Pereira Esteves Nogueira, Francisco Guilherme Torres, Juliana Arriel Silva, Maria Cristina Kuca, Kamil Ramalho, Teodorico C. Molecules Article Owing to their high surface area, stability, and functional groups on the surface, iron oxide hydroxide nanoparticles have attracted attention as enzymatic support. In this work, a chemometric approach was performed, aiming at the optimization of the horseradish peroxidase (HRP) immobilization process on Δ-FeOOH nanoparticles (NPs). The enzyme/NPs ratio (X1), pH (X2), temperature (X3), and time (X4) were the independent variables analyzed, and immobilized enzyme activity was the response variable (Y). The effects of the factors were studied using a factorial design at two levels (−1 and 1). The biocatalyst obtained was evaluated for the ferulic acid (FA) removal, a pollutant model. The materials were characterized by X-ray powder diffraction (XRD), Fourier transform infrared spectroscopy (FTIR), and scanning electron microscopy (SEM). The SEM images indicated changes in material morphology. The independent variables X1 (−0.57), X2 (0.71), and X4 (0.42) presented the significance effects estimate. The variable combinations resulted in two significance effects estimates, X1*X2 (−0.57) and X2*X4 (0.39). The immobilized HRP by optimized conditions (X1 = 1/63 (enzyme/NPs ratio, X2 = pH 8, X4 = 60 °C, and 30 min) showed high efficiency for FA oxidation (82%). MDPI 2020-01-08 /pmc/articles/PMC7024332/ /pubmed/31936386 http://dx.doi.org/10.3390/molecules25020259 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tavares, Tássia Silva
da Rocha, Eduardo Pereira
Esteves Nogueira, Francisco Guilherme
Torres, Juliana Arriel
Silva, Maria Cristina
Kuca, Kamil
Ramalho, Teodorico C.
Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach
title Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach
title_full Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach
title_fullStr Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach
title_full_unstemmed Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach
title_short Δ-FeOOH as Support for Immobilization Peroxidase: Optimization via a Chemometric Approach
title_sort δ-feooh as support for immobilization peroxidase: optimization via a chemometric approach
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024332/
https://www.ncbi.nlm.nih.gov/pubmed/31936386
http://dx.doi.org/10.3390/molecules25020259
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