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Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine

Generally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase...

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Autores principales: Magro, Massimiliano, Baratella, Davide, Venerando, Andrea, Nalotto, Giulia, Basso, Caroline R., Molinari, Simone, Salviulo, Gabriella, Ugolotti, Juri, Pedrosa, Valber A., Vianello, Fabio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7179010/
https://www.ncbi.nlm.nih.gov/pubmed/32290055
http://dx.doi.org/10.3390/ma13071776
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author Magro, Massimiliano
Baratella, Davide
Venerando, Andrea
Nalotto, Giulia
Basso, Caroline R.
Molinari, Simone
Salviulo, Gabriella
Ugolotti, Juri
Pedrosa, Valber A.
Vianello, Fabio
author_facet Magro, Massimiliano
Baratella, Davide
Venerando, Andrea
Nalotto, Giulia
Basso, Caroline R.
Molinari, Simone
Salviulo, Gabriella
Ugolotti, Juri
Pedrosa, Valber A.
Vianello, Fabio
author_sort Magro, Massimiliano
collection PubMed
description Generally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase (XO) was immobilized by self-assembly on peculiar naked iron oxide nanoparticles (surface active maghemite nanoparticles, SAMNs). The catalytic activity of the nanostructured conjugate (SAMN@XO) was assessed by optical spectroscopy and compared to the parent enzyme. SAMN@XO revealed improved catalytic features with respect to the parent enzyme and was applied for the electrochemical studies of xanthine. The present example supports the nascent knowledge concerning protein conjugation to nanoparticle as a means for the modulation of biological activity.
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spelling pubmed-71790102020-04-28 Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine Magro, Massimiliano Baratella, Davide Venerando, Andrea Nalotto, Giulia Basso, Caroline R. Molinari, Simone Salviulo, Gabriella Ugolotti, Juri Pedrosa, Valber A. Vianello, Fabio Materials (Basel) Article Generally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase (XO) was immobilized by self-assembly on peculiar naked iron oxide nanoparticles (surface active maghemite nanoparticles, SAMNs). The catalytic activity of the nanostructured conjugate (SAMN@XO) was assessed by optical spectroscopy and compared to the parent enzyme. SAMN@XO revealed improved catalytic features with respect to the parent enzyme and was applied for the electrochemical studies of xanthine. The present example supports the nascent knowledge concerning protein conjugation to nanoparticle as a means for the modulation of biological activity. MDPI 2020-04-10 /pmc/articles/PMC7179010/ /pubmed/32290055 http://dx.doi.org/10.3390/ma13071776 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
Magro, Massimiliano
Baratella, Davide
Venerando, Andrea
Nalotto, Giulia
Basso, Caroline R.
Molinari, Simone
Salviulo, Gabriella
Ugolotti, Juri
Pedrosa, Valber A.
Vianello, Fabio
Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine
title Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine
title_full Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine
title_fullStr Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine
title_full_unstemmed Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine
title_short Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine
title_sort enzyme immobilization on maghemite nanoparticles with improved catalytic activity: an electrochemical study for xanthine
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7179010/
https://www.ncbi.nlm.nih.gov/pubmed/32290055
http://dx.doi.org/10.3390/ma13071776
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