Δ-FeOOH as support for immobilization peroxidase: optimization via a chemometric approach

dc.creatorTavares, Tássia Silva
dc.creatorRocha, Eduardo Pereira da
dc.creatorNogueira, Francisco Guilherme Esteves
dc.creatorTorres, Juliana Arriel
dc.creatorSilva, Maria Cristina
dc.creatorKuca, Kamil
dc.creatorRamalho, Teodorico de Castro
dc.date2020-09-25T21:04:11Z
dc.date2020-09-25T21:04:11Z
dc.date2020-01
dc.date.accessioned2023-09-28T20:03:20Z
dc.date.available2023-09-28T20:03:20Z
dc.identifierTAVARES, T. S. et al. Δ-FeOOH as support for immobilization peroxidase: optimization via a chemometric approach. Molecules, Basel, v. 25, n. 2, 2020. DOI:10.3390/molecules25020259.
dc.identifierhttps://www.mdpi.com/1420-3049/25/2/259
dc.identifierhttp://repositorio.ufla.br/jspui/handle/1/43216
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/9043332
dc.descriptionOwing 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%).
dc.languageen
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)
dc.rightsrestrictAccess
dc.sourceMolecules
dc.subjectHorseradish peroxidase
dc.subjectBioremediation
dc.subjectIron oxide hydroxide
dc.titleΔ-FeOOH as support for immobilization peroxidase: optimization via a chemometric approach
dc.typeArtigo


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