Evidence map›Paper›PMID 39102121›Full record

ArticleBioprocess and biosystems engineering2024

Adsorption of extracellular lipase in a packed-bed reactor: an alternative immobilization approach.

Amanda Noli Freitas, Daniela Remonatto, Rodney Helder Miotti Junior, João Francisco Cabral do Nascimento, Adriana Candido da Silva Moura, Valéria de Carvalho Santos Ebinuma, Ariela Veloso de Paula

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Article in Bioprocess and biosystems engineering, 2024. 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

7 authors.

Amanda Noli FreitasDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil.
Daniela RemonattoDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil.
Rodney Helder Miotti JuniorDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil.
João Francisco Cabral do NascimentoDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil.
Adriana Candido da Silva MouraDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil.
Valéria de Carvalho Santos EbinumaDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil.
Ariela Veloso de PaulaDepartment of Bioprocess Engineering and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, SP, 14800-903, Brazil. ariela.veloso@unesp.br.ORCID http://orcid.org/0000-0002-2454-9749

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 304399/2022-1Conselho Nacional de Desenvolvimento Científico e Tecnológico 312463/2021-9Fundação de Amparo à Pesquisa do Estado de São Paulo 2020/09592-1 and 2021/13147-6Fundação de Amparo à Pesquisa do Estado de São Paulo 2021/06686-8 and 2023/01368-3
6 · The paper itself

Abstract

In light of the growing demand for novel biocatalysts and enzyme production methods, this study aimed to evaluate the potential of Aspergillus tubingensis for producing lipase under submerged culture investigating the influence of culture time and inducer treatment. Moreover, this study also investigated conditions for the immobilization of A. tubingensis lipase by physical adsorption on styrene-divinylbenzene beads (Diaion HP-20), for these conditions to be applied to an alternative immobilization system with a packed-bed reactor. Furthermore, A. tubingensis lipase and its immobilized derivative were characterized in terms of their optimal ranges of pH and temperature. A. tubingensis was shown to be a good producer of lipase, obviating the need for inducer addition. The enzyme extract had a hydrolytic activity of 23 U mL

Indexed as

BioreactorsEnzymes, ImmobilizedLipaseAdsorptionAspergillusFungal ProteinsHydrogen-Ion ConcentrationTemperatureEnzymes, ImmobilizedFungal ProteinsLipaseAdsorptionCharacterizationEnzymeImmobilizationPacked bed reactor

Identifiers

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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.