Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/43216
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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.date.accessioned2020-09-25T21:04:11Z-
dc.date.available2020-09-25T21:04:11Z-
dc.date.issued2020-01-
dc.identifier.citationTAVARES, 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.pt_BR
dc.identifier.urihttps://www.mdpi.com/1420-3049/25/2/259pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/43216-
dc.description.abstractOwing 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%).pt_BR
dc.languageenpt_BR
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)pt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceMoleculespt_BR
dc.subjectHorseradish peroxidasept_BR
dc.subjectBioremediationpt_BR
dc.subjectIron oxide hydroxidept_BR
dc.titleΔ-FeOOH as support for immobilization peroxidase: optimization via a chemometric approachpt_BR
dc.typeArtigopt_BR
Appears in Collections:DQI - Artigos publicados em periódicos

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