Evidence map›Paper›PMID 42249953›Full record

ArticleArchives of microbiology2026

Biochemical characterisation of a new thermotolerant L-asparaginase produced by Cunninghamella echinulata PA3S12MM isolated from the Atlantic Forest.

Simone Von Groll, Leticia Claudia da Silva, Pedro Henrique Nascimento Souza, Wállison Justino da Silva, Thaís Duarte Bifano, José Luis da Conceição Silva, Rita de Cássia Garcia Simão, Simão, Marina Kimiko Kadowaki, Alexandre Maller

Abstract read
In one paragraph

Article in Archives of microbiology, 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

10 authors.

Simone Von GrollCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Leticia Claudia da SilvaCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Pedro Henrique Nascimento SouzaCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Wállison Justino da SilvaCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Thaís Duarte BifanoCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
José Luis da Conceição SilvaCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Rita de Cássia Garcia SimãoCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
SimãoCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Marina Kimiko KadowakiCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil.
Alexandre MallerCentro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 2069 Universitária Street, Faculdade, Cascavel, Paraná, 85819-110, Brazil. alexandre.maller@unioeste.br.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-asparaginase is an amidohydrolase enzyme that catalyses the hydrolysis of L-asparagine into L-aspartic acid and ammonia. This enzyme has significant biotechnological applications, functioning as an antineoplastic agent in the pharmaceutical industry and as a tool for reducing acrylamide formation in the food industry. This study aimed to identify a filamentous fungus strain capable of synthesizing a new L-asparaginase and to perform its biochemical characterisation. Among the fungal isolates screened using plate assays and submerged fermentation, Cunninghamella echinulata strain PA3S12MM was identified as a promising L-asparaginase producer. The highest enzymatic induction was achieved using 5% (w/v) glucose as the carbon source and 0.4% (w/v) chicken feather as an agro-industrial nitrogen source, under incubation for 120 h. The enzyme exhibited an apparent K

Indexed as

AsparaginaseCunninghamellaAnimalsAsparagineCarbonEnzyme StabilityFermentationGlucoseHydrogen-Ion ConcentrationKineticsSubstrate SpecificityTemperatureAsparaginaseAsparagineCarbonGlucoseFilamentous fungiFood industryL-asparaginasePharmaceutical industry

Identifiers

PMID42249953
PMCPMC13242390

What OpenQuestion holds

Textmetadata
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.