Evidence map›Paper›PMID 32290055›Full record

ArticleMaterials (Basel, Switzerland)2020

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

Massimiliano Magro, Davide Baratella, Andrea Venerando, Giulia Nalotto, Caroline R Basso, Simone Molinari, Gabriella Salviulo, Juri Ugolotti, Valber A Pedrosa, Fabio Vianello

Abstract read
In one paragraph

Article in Materials (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Massimiliano MagroDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell'Università 16, 35020 Legnaro (PD), Italy.
Davide BaratellaDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell'Università 16, 35020 Legnaro (PD), Italy.
Andrea VenerandoDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell'Università 16, 35020 Legnaro (PD), Italy.ORCID 0000-0003-0379-2309
Giulia NalottoDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell'Università 16, 35020 Legnaro (PD), Italy.
Caroline R BassoDepartment of Chemistry and Biochemistry, Institute of Bioscience, Universidade Estadual Paulista, Botucatu, SP 18618-000, Brazil.
Simone MolinariDepartment of Geoscience, University of Padua, via G. Gradenigo 6, 35131 Padua, Italy.ORCID 0000-0001-8198-6913
Gabriella SalviuloDepartment of Geoscience, University of Padua, via G. Gradenigo 6, 35131 Padua, Italy.
Juri UgolottiRegional Centre of Advanced Technologies and Materials, Palacky University in Olomouc, Slechtitelu 27, 783 71 Olomouc, Czech Republic.
Valber A PedrosaDepartment of Chemistry and Biochemistry, Institute of Bioscience, Universidade Estadual Paulista, Botucatu, SP 18618-000, Brazil.
Fabio VianelloDepartment of Comparative Biomedicine and Food Science, University of Padua-Agripolis, Viale dell'Università 16, 35020 Legnaro (PD), Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

catalytic propertiesenzyme immobilizationmetal nanoparticlesxanthine oxidases

Identifiers

PMID32290055
PMCPMC7179010

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.