Evidence map›Paper›PMID 35164193›Full record

ArticleMolecules (Basel, Switzerland)2022

Enhanced Enzyme Reuse through the Bioconjugation of L-Asparaginase and Silica-Based Supported Ionic Liquid-like Phase Materials.

João C F Nunes, Mafalda R Almeida, Rui M F Bento, Matheus M Pereira, Valéria C Santos-Ebinuma, Márcia C Neves, Mara G Freire, Ana P M Tavares

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

1 citing paper in PubMed, 14 citations in OpenAlex.

  1. 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

8 authors at 2 institutions in 2 countries.

João C F NunesCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0003-2028-586X
Mafalda R AlmeidaCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0003-2101-8309
Rui M F BentoCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.
Matheus M PereiraCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0003-3524-6900
Valéria C Santos-EbinumaDepartment of Engineering of Bioprocesses and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara 14800-903, Brazil.ORCID 0000-0002-6666-6695
Márcia C NevesCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.
Mara G FreireCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0001-8895-0614
Ana P M TavaresCICECO-Aveiro Institute of Materials, Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0001-9128-6275
University of Aveiro · PTUniversidade Estadual Paulista (Unesp) · BR

Funding

Fundação para a Ciência e Tecnologia CEECIND/00383/2017Fundação para a Ciência e Tecnologia CEECIND/2020/01867Fundação para a Ciência e Tecnologia POCI-01-0145-FEDER-031268Fundação para a Ciência e Tecnologia SFRH/BD/150671/2020Fundação para a Ciência e Tecnologia UIDB/50011/2020 & UIDP/50011/2020São Paulo Research Foundation 2018/06908-8
6 · The paper itself

Abstract

L-asparaginase (ASNase) is an amidohydrolase that can be used as a biopharmaceutical, as an agent for acrylamide reduction, and as an active molecule for L-asparagine detection. However, its free form displays some limitations, such as the enzyme's single use and low stability. Hence, immobilization is one of the most effective tools for enzyme recovery and reuse. Silica is a promising material due to its low-cost, biological compatibility, and tunable physicochemical characteristics if properly functionalized. Ionic liquids (ILs) are designer compounds that allow the tailoring of their physicochemical properties for a given task. If properly designed, bioconjugates combine the features of the selected ILs with those of the support used, enabling the simple recovery and reuse of the enzyme. In this work, silica-based supported ionic liquid-like phase (SSILLP) materials with quaternary ammoniums and chloride as the counterion were studied as novel supports for ASNase immobilization since it has been reported that ammonium ILs have beneficial effects on enzyme stability. SSILLP materials were characterized by elemental analysis and zeta potential. The immobilization process was studied and the pH effect, enzyme/support ratio, and contact time were optimized regarding the ASNase enzymatic activity. ASNase-SSILLP bioconjugates were characterized by ATR-FTIR. The bioconjugates displayed promising potential since [Si][N

Indexed as

AsparaginaseHydrophobic and Hydrophilic InteractionsIonic LiquidsMolecular Docking SimulationSilicon DioxideSpectroscopy, Fourier Transform InfraredAsparaginaseIonic LiquidsSilicon Dioxidebioconjugationenzyme immobilizationL-asparaginasemolecular dockingphysical adsorptionsilica-based supported ionic liquid-like phase materials

Identifiers

PMID35164193
PMCPMC8838661
OpenAlexW4213165193

What OpenQuestion holds

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LicenceCC BY
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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.