Evidence map›Paper›PMID 41991885›Full record

ArticleWorld journal of microbiology & biotechnology2026

Production of an enzymatic cocktail by Aspergillus japonicus in a stirred-tank bioreactor for application in animal feed.

Ana Lorena de Oliveira Simas, Aline Pereira Almeida, Nathalia Nunes Glienke, Quézia de Melo Santana, Rodrigo Mattos Silva Galeano, Charles Kiefer, Karina Márcia Ribeiro de Souza Nascimento, Maria de Lourdes Teixeira de Moraes Polizeli, Douglas Chodi Masui, Fabiana Fonseca Zanoelo and 1 more

Abstract read
In one paragraph

Article in World journal of microbiology & biotechnology, 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

11 authors.

Ana Lorena de Oliveira SimasPrograma Multicêntrico de Pós-Graduação em Bioquímica e Biologia Molecular, Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil.ORCID http://orcid.org/0000-0002-8736-6659
Aline Pereira AlmeidaDepartamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, 14040-901, Brazil.ORCID http://orcid.org/0000-0003-4015-7996
Nathalia Nunes GlienkePrograma Multicêntrico de Pós-Graduação em Bioquímica e Biologia Molecular, Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil.ORCID http://orcid.org/0000-0001-7730-8298
Quézia de Melo SantanaLaboratório de Bioquímica Geral e de Microrganismos (LBq), Instituto de Biociências (INBIO), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, 79070-900, Brazil.ORCID http://orcid.org/0009-0007-3320-7285
Rodrigo Mattos Silva GaleanoLaboratório de Bioquímica Geral e de Microrganismos (LBq), Instituto de Biociências (INBIO), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, 79070-900, Brazil.ORCID http://orcid.org/0000-0002-9546-7177
Charles KieferFaculdade de Medicina Veterinária e Zootecnia (FAMEZ), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil.ORCID http://orcid.org/0000-0001-9622-2844
Karina Márcia Ribeiro de Souza NascimentoFaculdade de Medicina Veterinária e Zootecnia (FAMEZ), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil.ORCID http://orcid.org/0000-0003-0482-0666
Maria de Lourdes Teixeira de Moraes PolizeliDepartamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, 14040-901, Brazil.ORCID http://orcid.org/0000-0002-9999-7212
Douglas Chodi MasuiPrograma Multicêntrico de Pós-Graduação em Bioquímica e Biologia Molecular, Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil.ORCID http://orcid.org/0000-0002-3858-1467
Fabiana Fonseca ZanoeloPrograma Multicêntrico de Pós-Graduação em Bioquímica e Biologia Molecular, Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil.ORCID http://orcid.org/0000-0002-5778-0322
Giovana Cristina GiannesiPrograma Multicêntrico de Pós-Graduação em Bioquímica e Biologia Molecular, Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), Universidade Federal de Mato Grosso do Sul, Campo Grande, MS, Brazil. giannesigiovana@hotmail.com.ORCID http://orcid.org/0000-0001-8256-9441

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

New enzymatic sources need to be explored to meet the increasing demand for bioactives used in the supplementation of non-ruminant animals. Phytase and xylanase are widely used in animal nutrition due to their ability to degrade phytic acid and xylan, respectively. This study aimed to (i) produce phytase and xylanase by culturing Aspergillus japonicus on medium containing wheat bran + soybean bran (1:1 w/w) as alternative carbon sources in a stirred-tank bioreactor and (ii) compare this process with that conducted in Erlenmeyer flasks. The resulting enzymatic cocktails and commercial enzymes were evaluated for their ability to hydrolyze poultry diets (D1–D9). The production peaks of phytase and xylanase in the bioreactor occurred at 120 h (842.30 ± 43.62 U/L) and 144 h (3211.29 ± 274.98 U/L), respectively. After 144 h of cultivation, protein concentration in the bioreactor was approximately twice that observed in Erlenmeyer flasks. ECPAjBr displayed the highest hydrolytic activity for inorganic phosphate in diet D6 (42.34 ± 2.20 mg/g), followed by diet D7 (38.67 ± 0.46 mg/g). Regarding reducing sugars, ECXAjBr exhibited the highest activity in diets D1 and D8, releasing 147.71 ± 18.18 mg/g and 145.83 ± 11.39 mg/g, respectively. All tested diets, regardless of their composition, indicated a synergistic interaction between commercial enzymes and those present in the A. japonicus enzyme cocktail, which exhibits a broad spectrum of hydrolytic activities, including high levels of accessory enzymes. The application of this cocktail in animal diets holds great potential for increasing nutrient bioavailability in non-ruminant animal production.

Indexed as

6-PhytaseAnimal FeedAspergillusBioreactorsEndo-1,4-beta XylanasesAnimalsCulture MediaDietary FiberFermentationGlycine maxHydrolysisPhytic Acid6-PhytaseCulture MediaDietary FiberEndo-1,4-beta XylanasesPhytic AcidAnimal dietBench-scale bioreactorEnzymesSubmerged cultivationSynergism

Identifiers

PMID41991885
PMCPMC13086882

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.