Evidence map›Paper›PMID 33321857›Full record

ReviewMolecules (Basel, Switzerland)2020

Recent Strategies and Applications for l-Asparaginase Confinement.

João C F Nunes, Raquel O Cristóvão, Mara G Freire, Valéria C Santos-Ebinuma, Joaquim L Faria, Cláudia G Silva, Ana P M Tavares

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

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  20. Thermostability Improvement of L-Asparaginase fromMolecules (Basel, Switzerland) · 2022
    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

7 authors.

João C F NunesLaboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials (LSRE-LCM), Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua do Dr. Roberto Frias, 4200-465 Porto, Portugal.ORCID 0000-0003-2028-586X
Raquel O CristóvãoLaboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials (LSRE-LCM), Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua do Dr. Roberto Frias, 4200-465 Porto, Portugal.ORCID 0000-0001-5165-4766
Mara G FreireDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193 Aveiro, Portugal.ORCID 0000-0001-8895-0614
Valéria C Santos-EbinumaSchool of Pharmaceutical Sciences, Universidade Estadual Paulista-UNESP, Araraquara 14800-903, Brazil.
Joaquim L FariaLaboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials (LSRE-LCM), Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua do Dr. Roberto Frias, 4200-465 Porto, Portugal.ORCID 0000-0002-6531-3978
Cláudia G SilvaLaboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials (LSRE-LCM), Department of Chemical Engineering, Faculty of Engineering, University of Porto, Rua do Dr. Roberto Frias, 4200-465 Porto, Portugal.ORCID 0000-0001-6469-4871
Ana P M TavaresDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193 Aveiro, Portugal.

Funding

Fundação para a Ciência e a Tecnologia DL57/2016Fundação para a Ciência e a Tecnologia IF/01634/2015Fundação para a Ciência e a Tecnologia POCI-01-0145-FEDER-031268Fundação para a Ciência e a Tecnologia SFRH/BD/150671/2020Fundação para a Ciência e a Tecnologia UIDB/50011/2020 & UIDP/50011/2020
6 · The paper itself

Abstract

l-asparaginase (ASNase, EC 3.5.1.1) is an aminohydrolase enzyme with important uses in the therapeutic/pharmaceutical and food industries. Its main applications are as an anticancer drug, mostly for acute lymphoblastic leukaemia (ALL) treatment, and in acrylamide reduction when starch-rich foods are cooked at temperatures above 100 °C. Its use as a biosensor for asparagine in both industries has also been reported. However, there are certain challenges associated with ASNase applications. Depending on the ASNase source, the major challenges of its pharmaceutical application are the hypersensitivity reactions that it causes in ALL patients and its short half-life and fast plasma clearance in the blood system by native proteases. In addition, ASNase is generally unstable and it is a thermolabile enzyme, which also hinders its application in the food sector. These drawbacks have been overcome by the ASNase confinement in different (nano)materials through distinct techniques, such as physical adsorption, covalent attachment and entrapment. Overall, this review describes the most recent strategies reported for ASNase confinement in numerous (nano)materials, highlighting its improved properties, especially specificity, half-life enhancement and thermal and operational stability improvement, allowing its reuse, increased proteolysis resistance and immunogenicity elimination. The most recent applications of confined ASNase in nanomaterials are reviewed for the first time, simultaneously providing prospects in the described fields of application.

Indexed as

BiotechnologyAsparaginaseBiosensing TechniquesDrug DevelopmentFood IndustryHumansNanotechnologyProtein EngineeringStructure-Activity RelationshipAsparaginaseacrylamide mitigationbiosensorsconfinement strategiesl-asparaginasenanomaterialstherapeutic agents

Identifiers

PMID33321857
PMCPMC7764279

What OpenQuestion holds

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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.