Evidence map›Paper›PMID 27866936›Full record

ReviewBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2016

Current applications and different approaches for microbial l-asparaginase production.

Jorge Javier Muso Cachumba, Felipe Antonio Fernandes Antunes, Guilherme Fernando Dias Peres, Larissa Pereira Brumano, Júlio César Dos Santos, Silvio Silvério Da Silva

Open access · hybridAbstract readReview
In one paragraph

Review in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
16.1field-weighted citation impact, top 1% 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

55 citing papers in PubMed, 208 citations in OpenAlex.

  1. Article
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. In-silico comparison of fungal and bacterial asparaginase enzymes.Molecular biology research communications · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. A new extracellular glutaminase and urease-free L-asparaginase from Meyerozyma guilliermondii.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  17. Article
  18. Article
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Jorge Javier Muso CachumbaUniversidade de São Paulo, Escola de Engenharia de Lorena, São Paulo, SP, Brazil.
Felipe Antonio Fernandes AntunesUniversidade de São Paulo, Escola de Engenharia de Lorena, São Paulo, SP, Brazil.
Guilherme Fernando Dias PeresUniversidade de São Paulo, Escola de Engenharia de Lorena, São Paulo, SP, Brazil.
Larissa Pereira BrumanoUniversidade de São Paulo, Escola de Engenharia de Lorena, São Paulo, SP, Brazil.
Júlio César Dos SantosUniversidade de São Paulo, Escola de Engenharia de Lorena, São Paulo, SP, Brazil.
Silvio Silvério Da SilvaUniversidade de São Paulo, Escola de Engenharia de Lorena, São Paulo, SP, Brazil. Electronic address: silviosilverio@usp.com.
Universidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

l-asparaginase (EC 3.5.1.1) is an enzyme that catalysis mainly the asparagine hydrolysis in l-aspartic acid and ammonium. This enzyme is presented in different organisms, such as microorganisms, vegetal, and some animals, including certain rodent's serum, but not unveiled in humans. It can be used as important chemotherapeutic agent for the treatment of a variety of lymphoproliferative disorders and lymphomas (particularly acute lymphoblastic leukemia (ALL) and Hodgkin's lymphoma), and has been a pivotal agent in chemotherapy protocols from around 30 years. Also, other important application is in food industry, by using the properties of this enzyme to reduce acrylamide levels in commercial fried foods, maintaining their characteristics (color, flavor, texture, security, etc.) Actually, l-asparaginase catalyzes the hydrolysis of l-asparagine, not allowing the reaction of reducing sugars with this aminoacid for the generation of acrylamide. Currently, production of l-asparaginase is mainly based in biotechnological production by using some bacteria. However, industrial production also needs research work aiming to obtain better production yields, as well as novel process by applying different microorganisms to increase the range of applications of the produced enzyme. Within this context, this mini-review presents l-asparaginase applications, production by different microorganisms and some limitations, current investigations, as well as some challenges to be achieved for profitable industrial production.

Indexed as

Antineoplastic AgentsDrug IndustryFermentationIndustrial MicrobiologyAnimalsAsparaginaseFood IndustryHumansAntineoplastic AgentsAsparaginaseAcrylamideIndustrial productionl-asparaginaseMicrobial productionPharmaceutical application

Identifiers

PMID27866936
PMCPMC5156506
OpenAlexW2541637601

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.