Evidence map›Paper›PMID 35974197›Full record

ArticleBioprocess and biosystems engineering2022

Aliivibrio fischeri L-Asparaginase production by engineered Bacillus subtilis: a potential new biopharmaceutical.

Heitor B S Bento, Gabriela B Paiva, Mafalda R Almeida, Claúdia G Silva, Pedro J Carvalho, Ana P M Tavares, Danielle B Pedrolli, Valéria C Santos-Ebinuma

Abstract read
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In one paragraph

Article in Bioprocess and biosystems engineering, 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
–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

1 citing paper in PubMed.

  1. Review
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.

Heitor B S BentoSchool of Pharmaceutical Sciences, Department of Bioprocess Engineering and Biotechnology, São Paulo State University (UNESP), Araraquara, São Paulo, 14800-903, Brazil. heitor.bento@unesp.br.ORCID http://orcid.org/0000-0002-0629-3196
Gabriela B PaivaSchool of Pharmaceutical Sciences, Department of Bioprocess Engineering and Biotechnology, São Paulo State University (UNESP), Araraquara, São Paulo, 14800-903, Brazil.
Mafalda R AlmeidaDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193, Aveiro, Portugal.
Claúdia G SilvaLSRE-LCM-Laboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, 4200-465, Porto, Portugal.
Pedro J CarvalhoDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193, Aveiro, Portugal.
Ana P M TavaresDepartment of Chemistry, CICECO-Aveiro Institute of Materials, University of Aveiro, 3810-193, Aveiro, Portugal.
Danielle B PedrolliSchool of Pharmaceutical Sciences, Department of Bioprocess Engineering and Biotechnology, São Paulo State University (UNESP), Araraquara, São Paulo, 14800-903, Brazil.
Valéria C Santos-EbinumaSchool of Pharmaceutical Sciences, Department of Bioprocess Engineering and Biotechnology, São Paulo State University (UNESP), Araraquara, São Paulo, 14800-903, Brazil. valeria.ebinuma@unesp.br.ORCID http://orcid.org/0000-0002-6666-6695

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 312463/2021-9Coordenação de Aperfeiçoamento de Pessoal de Nível Superior 001Fundação de Amparo à Pesquisa do Estado de São Paulo 2018/06908-8Fundação de Amparo à Pesquisa do Estado de São Paulo 2020/15513-7Fundação de Amparo à Pesquisa do Estado de São Paulo 2021/01284-9Fundação de Amparo à Pesquisa do Estado de São Paulo 2021/06686-8Fundação para a Ciência e a Tecnologia LA/P/0006/2020Fundação para a Ciência e a Tecnologia LA/P/0045/2020Fundação para a Ciência e a Tecnologia UIDB/50011/2020Fundação para a Ciência e a Tecnologia UIDB/50020/2020Fundação para a Ciência e a Tecnologia UIDP/50011/2020Fundação para a Ciência e a Tecnologia UIDP/50020/2020
6 · The paper itself

Abstract

L-Asparaginase (L-ASNase) is an enzyme applied in the treatment of lymphoid malignancies. However, an innovative L-ASNase with high yield and lower side effects than the commercially available preparations are still a market requirement. Here, a new-engineered Bacillus subtilis strain was evaluated for Aliivibrio fischeri L-ASNase II production, being the bioprocess development and the enzyme characterization studied. The pBS0E plasmid replicative in Bacillus sp and containing PxylA promoter inducible by xylose and its repressive molecule sequence (XylR) was used for the genetic modification. Initially, cultivations were carried out in orbital shaker, and then the process was scaled up to stirred tank bioreactor (STB). After the bioprocess, the cells were recovered and submitted to ultrasound sonication for cells disruption and intracellular enzyme recovery. The enzymatic extract was characterized to assess its biochemical, kinetic and thermal properties using L-Asparagine and L-Glutamine as substrates. The results indicated the potential enzyme production in STB achieving L-ASNase activity up to 1.539 U mL

Indexed as

Antineoplastic AgentsBiological ProductsAliivibrio fischeriAsparaginaseAsparagineBacillus subtilisGlutaminaseGlutaminePharmaceutical PreparationsXyloseAntineoplastic AgentsAsparaginaseAsparagineBiological ProductsGlutaminaseGlutaminePharmaceutical PreparationsXyloseBacillus subtilisEnzymatic characterizationEnzymatic thermal inactivationL-AsparaginaseStirred tank bioreactor

Identifiers

What OpenQuestion holds

Textmetadata
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.