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De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications

Natural enzyme mimics have attracted considerable attention due to leakage of enzymes and their easy denaturation during their storage and immobilization procedure. Here in this study, for the first time, a new iron oxide hydroxide, ferrihydrite – Fe(1.44)O(0.32) (OH) (3.68) magnetic nanoparticles w...

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Autores principales: Ahmed, Amany, Abagana, Adam, Cui, Daizong, Zhao, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6458858/
https://www.ncbi.nlm.nih.gov/pubmed/31032360
http://dx.doi.org/10.1155/2019/7127869
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author Ahmed, Amany
Abagana, Adam
Cui, Daizong
Zhao, Min
author_facet Ahmed, Amany
Abagana, Adam
Cui, Daizong
Zhao, Min
author_sort Ahmed, Amany
collection PubMed
description Natural enzyme mimics have attracted considerable attention due to leakage of enzymes and their easy denaturation during their storage and immobilization procedure. Here in this study, for the first time, a new iron oxide hydroxide, ferrihydrite – Fe(1.44)O(0.32) (OH) (3.68) magnetic nanoparticles were synthesized by bacterial strain named Comamonas testosteroni. The characterization of the produced magnetic nanoparticles was confirmed by transmission electron microscopy (TEM), Fourier-transform spectroscopy (FTIR), X-ray diffraction (XRD), and magnetization hysteresis loops. Further, these extracted nanoparticles were proven to have biogenic magnetic behavior and to exhibit enhanced peroxidase-like activity. It is capable of catalyzing the oxidation of 3, 3′, 5, 5′-Tetramethylbenzidine (TMB) by H(2)O(2) to produce blue color (typical color reactions). Catalysis was examined to follow Michaelis-Menton kinetics and the good affinity to both H(2)O(2) and TMB. The K(m) value of the Fe(1.44)O(0.32) (OH) (3.68) with H(2)O(2) and TMB as the substrate was 0.0775 and 0.0155 mM, respectively, which were lower than that of the natural enzyme (HRP). Experiments of electron spin resonance (ESR) spectroscopy proved that the BMNPs could catalyze H(2)O(2) to produce hydroxyl radicals. As a new peroxidase mimetic, the BMNPs were exhibited to offer a simple, sensitive, and selective colorimetric method for determination of H(2)O(2) and glucose and efficiently catalyze the detection of glucose in real blood samples.
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spelling pubmed-64588582019-04-28 De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications Ahmed, Amany Abagana, Adam Cui, Daizong Zhao, Min Biomed Res Int Research Article Natural enzyme mimics have attracted considerable attention due to leakage of enzymes and their easy denaturation during their storage and immobilization procedure. Here in this study, for the first time, a new iron oxide hydroxide, ferrihydrite – Fe(1.44)O(0.32) (OH) (3.68) magnetic nanoparticles were synthesized by bacterial strain named Comamonas testosteroni. The characterization of the produced magnetic nanoparticles was confirmed by transmission electron microscopy (TEM), Fourier-transform spectroscopy (FTIR), X-ray diffraction (XRD), and magnetization hysteresis loops. Further, these extracted nanoparticles were proven to have biogenic magnetic behavior and to exhibit enhanced peroxidase-like activity. It is capable of catalyzing the oxidation of 3, 3′, 5, 5′-Tetramethylbenzidine (TMB) by H(2)O(2) to produce blue color (typical color reactions). Catalysis was examined to follow Michaelis-Menton kinetics and the good affinity to both H(2)O(2) and TMB. The K(m) value of the Fe(1.44)O(0.32) (OH) (3.68) with H(2)O(2) and TMB as the substrate was 0.0775 and 0.0155 mM, respectively, which were lower than that of the natural enzyme (HRP). Experiments of electron spin resonance (ESR) spectroscopy proved that the BMNPs could catalyze H(2)O(2) to produce hydroxyl radicals. As a new peroxidase mimetic, the BMNPs were exhibited to offer a simple, sensitive, and selective colorimetric method for determination of H(2)O(2) and glucose and efficiently catalyze the detection of glucose in real blood samples. Hindawi 2019-03-28 /pmc/articles/PMC6458858/ /pubmed/31032360 http://dx.doi.org/10.1155/2019/7127869 Text en Copyright © 2019 Amany Ahmed et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Ahmed, Amany
Abagana, Adam
Cui, Daizong
Zhao, Min
De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications
title De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications
title_full De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications
title_fullStr De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications
title_full_unstemmed De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications
title_short De Novo Iron Oxide Hydroxide, Ferrihydrite Produced by Comamonas testosteroni Exhibiting Intrinsic Peroxidase-Like Activity and Their Analytical Applications
title_sort de novo iron oxide hydroxide, ferrihydrite produced by comamonas testosteroni exhibiting intrinsic peroxidase-like activity and their analytical applications
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6458858/
https://www.ncbi.nlm.nih.gov/pubmed/31032360
http://dx.doi.org/10.1155/2019/7127869
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