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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MDPI AG
2020-04-01
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| Online Access: | https://www.mdpi.com/1996-1944/13/7/1776 |
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| author | Massimiliano Magro Davide Baratella Andrea Venerando Giulia Nalotto Caroline R. Basso Simone Molinari Gabriella Salviulo Juri Ugolotti Valber A. Pedrosa Fabio Vianello |
| author_facet | Massimiliano Magro Davide Baratella Andrea Venerando Giulia Nalotto Caroline R. Basso Simone Molinari Gabriella Salviulo Juri Ugolotti Valber A. Pedrosa Fabio Vianello |
| author_sort | Massimiliano Magro |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T20:34:27Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 1996-1944 |
| language | English |
| last_indexed | 2024-03-10T20:34:27Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Materials |
| spelling | doaj.art-fa1296d8395f450bb16455b3933fa6eb2023-11-19T21:11:59ZengMDPI AGMaterials1996-19442020-04-01137177610.3390/ma13071776Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for XanthineMassimiliano Magro0Davide Baratella1Andrea Venerando2Giulia Nalotto3Caroline R. Basso4Simone Molinari5Gabriella Salviulo6Juri Ugolotti7Valber A. Pedrosa8Fabio Vianello9Department of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell’Università 16, 35020 Legnaro (PD), ItalyDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell’Università 16, 35020 Legnaro (PD), ItalyDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell’Università 16, 35020 Legnaro (PD), ItalyDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell’Università 16, 35020 Legnaro (PD), ItalyDepartment of Chemistry and Biochemistry, Institute of Bioscience, Universidade Estadual Paulista, Botucatu, SP 18618-000, BrazilDepartment of Geoscience, University of Padua, via G. Gradenigo 6, 35131 Padua, ItalyDepartment of Geoscience, University of Padua, via G. Gradenigo 6, 35131 Padua, ItalyRegional Centre of Advanced Technologies and Materials, Palacky University in Olomouc, Slechtitelu 27, 783 71 Olomouc, Czech RepublicDepartment of Chemistry and Biochemistry, Institute of Bioscience, Universidade Estadual Paulista, Botucatu, SP 18618-000, BrazilDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell’Università 16, 35020 Legnaro (PD), ItalyGenerally, 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.https://www.mdpi.com/1996-1944/13/7/1776xanthine oxidasesenzyme immobilizationcatalytic propertiesmetal nanoparticles |
| spellingShingle | Massimiliano Magro Davide Baratella Andrea Venerando Giulia Nalotto Caroline R. Basso Simone Molinari Gabriella Salviulo Juri Ugolotti Valber A. Pedrosa Fabio Vianello Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine Materials xanthine oxidases enzyme immobilization catalytic properties metal nanoparticles |
| 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 | xanthine oxidases enzyme immobilization catalytic properties metal nanoparticles |
| url | https://www.mdpi.com/1996-1944/13/7/1776 |
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