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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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. |
format | Online Article Text |
id | pubmed-7179010 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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