Evidence map›Paper›PMID 40643884›Full record

ArticleFolia microbiologica2026

High-yield production and functional analysis of novel rhizobial-type glutaminase-free L-asparaginase from Paenibacillus thiaminolyticus.

Tomáš Podzimek, Karolína Loužecká, Veronika Urbánková, Jan Beránek, Petra Lipovová, Eva Benešová

Abstract read
In one paragraph

Article in Folia microbiologica, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Tomáš PodzimekDepartment of Biochemistry and Microbiology, University of Chemistry and Technology, Technická 5, 166 28, Prague 6, Czech Republic.ORCID http://orcid.org/0000-0002-9621-7516
Karolína LoužeckáDepartment of Biochemistry and Microbiology, University of Chemistry and Technology, Technická 5, 166 28, Prague 6, Czech Republic.ORCID http://orcid.org/0009-0002-8824-9355
Veronika UrbánkováDepartment of Biochemistry and Microbiology, University of Chemistry and Technology, Technická 5, 166 28, Prague 6, Czech Republic.ORCID http://orcid.org/0009-0005-6468-993X
Jan BeránekDepartment of Biochemistry and Microbiology, University of Chemistry and Technology, Technická 5, 166 28, Prague 6, Czech Republic.ORCID http://orcid.org/0000-0002-5347-3966
Petra LipovováDepartment of Biochemistry and Microbiology, University of Chemistry and Technology, Technická 5, 166 28, Prague 6, Czech Republic.ORCID http://orcid.org/0000-0003-2275-3479
Eva BenešováDepartment of Biochemistry and Microbiology, University of Chemistry and Technology, Technická 5, 166 28, Prague 6, Czech Republic. eva.benesova@vscht.cz.ORCID http://orcid.org/0000-0002-3696-3517

Funding

Ministerstvo Školství, Mládeže a Tělovýchovy LUC23140Technologická Agentura České Republiky TQ03000738Vysoká Škola Chemicko-technologická v Praze A1_FPBT_2024_001Vysoká Škola Chemicko-technologická v Praze A2_FPBT_2024_024
6 · The paper itself

Abstract

L-Asparaginases are enzymes known for decades due to their use in medicine for the treatment of acute lymphoblastic leukemia. Recently, they have also found application in the food industry, and other possibilities are emerging in the treatment of infectious diseases or in the design of biosensors. For this reason, an ongoing effort has been made to find and characterize new enzymes with properties suitable for these specific applications. In this work, L-asparaginase from Paenibacillus thiaminolyticus (isoenzyme 1) belonging to the least explored group of L-asparaginases derived from L-asparaginase from Rhizobium etli was recombinantly produced with high yields (335 mg per L of culture medium) in E. coli cells and characterized: K

Indexed as

AsparaginaseBacterial ProteinsPaenibacillusRhizobiumBiosensing TechniquesEnzyme StabilityEscherichia coliGlutaminaseHydrogen-Ion ConcentrationKineticsRecombinant ProteinsAsparaginaseBacterial ProteinsGlutaminaseRecombinant ProteinsAcrylamide mitigationAcute lymphoblastic leukemiaAsparaginaseBiosensorsFood industryPaenibacillus thiaminolyticus

Identifiers

PMID40643884
PMCPMC13541837

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.