Evidence map›Paper›PMID 35474328›Full record

ArticleScientific reports2022

Impact of immobilization strategies on the activity and recyclability of lipases in nanomagnetic supports.

Thais de Andrade Silva, Wanderson Juvêncio Keijok, Marco Cesar Cunegundes Guimarães, Sérvio Túlio Alves Cassini, Jairo Pinto de Oliveira

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
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

15 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Biofunctionalization of Magneto-Plasmonic FeMolecules (Basel, Switzerland) · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

5 authors at 1 institution in 1 country.

Thais de Andrade SilvaFederal University of Espírito Santo, Av Marechal Campos 1468, Vitória, ES, 29040-090, Brazil.
Wanderson Juvêncio KeijokFederal University of Espírito Santo, Av Marechal Campos 1468, Vitória, ES, 29040-090, Brazil.
Marco Cesar Cunegundes GuimarãesFederal University of Espírito Santo, Av Marechal Campos 1468, Vitória, ES, 29040-090, Brazil.
Sérvio Túlio Alves CassiniFederal University of Espírito Santo, Av Fernando Ferrari 514, Vitória, ES, 29075-910, Brazil.
Jairo Pinto de OliveiraFederal University of Espírito Santo, Av Marechal Campos 1468, Vitória, ES, 29040-090, Brazil. jairo.oliveira@ufes.br.
Universidade Federal do Espírito Santo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The use of enzymes immobilized on nanomagnetic supports has produced surprising results in catalysis, mainly due to the increase in surface area and the potential for recovery and reuse. However, the meticulous control of the process and difficulties in reproducibility have made industrial-scale applications unfeasible. Furthermore, the role of conjugation strategies in the catalytic activity and recycling of catalysts is unclear. Therefore, the objective of this study was to compare the conjugation of enzymes on nanomagnetic supports through physical adsorption (naked) or covalent bonding with mercaptopropyltrimethoxysilane (MPTS) and aminopropyltriethoxysilane (APTS) ligands. The free lipase obtained from Rhizomucor miehei was used as a model enzyme. Total protein and enzyme activity were determined using spectrophotometry (UV-Vis) and the p-nitrophenyl palmitate (p-NPP) hydrolysis method. The results indicated that a more significant enzyme surface loading does not always mean better immobilization success. The physical adsorption binding strategy had higher surface loading and low catalytic activity. On the other hand, covalent coupling with free NH2 had an excellent catalytic activity with very low surface loading. Finally, we show that recyclability can be improved with conjugation mediated by disulfide bonds. The findings presented here are essential for developing nanoconjugates with high enzymatic activity, which can guarantee the success of several industrial applications.

Indexed as

Enzymes, ImmobilizedLipaseAdsorptionHydrolysisReproducibility of ResultsEnzymes, ImmobilizedLipase

Identifiers

PMID35474328
PMCPMC9042828
OpenAlexW4224482812

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.