Evidence map›Paper›PMID 39073555›Full record

ArticleBioresources and bioprocessing2024

Recombinant GH3 β-glucosidase stimulated by xylose and tolerant to furfural and 5-hydroxymethylfurfural obtained from Aspergillus nidulans.

Diandra de Andrades, Robson C Alnoch, Gabriela S Alves, Jose C S Salgado, Paula Z Almeida, Gabriela Leila Berto, Fernando Segato, Richard J Ward, Marcos S Buckeridge, Maria de Lourdes T M Polizeli

Abstract read
In one paragraph

Article in Bioresources and bioprocessing, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
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.

Diandra de Andrades *Department of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14040-901, Brazil.
Robson C Alnoch *Department of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14040-901, Brazil.
Gabriela S AlvesDepartment of Biochemistry and Immunology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14049-900, Brazil.
Jose C S SalgadoDepartment of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14040-901, Brazil.
Paula Z AlmeidaDepartment of Biochemistry and Immunology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14049-900, Brazil.
Gabriela Leila BertoDepartment of Biotechnology, Lorena School of Engineering, University of São Paulo, Lorena, 12602-810, Brazil.
Fernando SegatoDepartment of Biotechnology, Lorena School of Engineering, University of São Paulo, Lorena, 12602-810, Brazil.
Richard J WardDepartment of Chemistry, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14040-901, Brazil.
Marcos S BuckeridgeBioscience Institute, University of São Paulo, São Paulo, 05508-090, Brazil.
Maria de Lourdes T M PolizeliDepartment of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, SP, 14040-901, Brazil. polizeli@ffclrp.usp.br.ORCID http://orcid.org/0000-0002-5026-6363

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 151187/2023-1Conselho Nacional de Desenvolvimento Científico e Tecnológico 310340/2021-7Conselho Nacional de Desenvolvimento Científico e Tecnológico 384465/2023-4Conselho Nacional de Desenvolvimento Científico e Tecnológico 465319/2014-9Coordenação de Aperfeiçoamento de Pessoal de Nível Superior Financial Code 001Fundação de Amparo à Pesquisa do Estado de São Paulo 2014/50884-5Fundação de Amparo à Pesquisa do Estado de São Paulo 2018/07522-6Fundação de Amparo à Pesquisa do Estado de São Paulo 2019/21989-7Fundação de Amparo à Pesquisa do Estado de São Paulo 2020/15510-8Fundação de Amparo à Pesquisa do Estado de São Paulo 2021/06679-1Fundação de Amparo à Pesquisa do Estado de São Paulo 2022/00539-6Fundação de Amparo à Pesquisa do Estado de São Paulo 2023/01338-7Fundação de Amparo à Pesquisa do Estado de São Paulo 2023/01547-5Fundação de Amparo à Pesquisa do Estado de São Paulo 2023/09627-8Fundação para a Ciência e a Tecnologia POCI-01-0145-FEDER-032206
6 · The paper itself

Abstract

The β-glucosidase gene from Aspergillus nidulans FGSC A4 was cloned and overexpressed in the A. nidulans A773. The resulting purified β-glucosidase, named AnGH3, is a monomeric enzyme with a molecular weight of approximately 80 kDa, as confirmed by SDS-PAGE. Circular dichroism further validated its unique canonical barrel fold (β/α), a feature also observed in the 3D homology model of AnGH3. The most striking aspect of this recombinant enzyme is its robustness, as it retained 100% activity after 24 h of incubation at 45 and 50 ºC and pH 6.0. Even at 55 °C, it maintained 72% of its enzymatic activity after 6 h of incubation at the same pH. The kinetic parameters V

Indexed as

Enzymatic hydrolysisHomologous expressionTolerant to biomass productsXylose-stimulated

Identifiers

PMID39073555
PMCPMC11286919

What OpenQuestion holds

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Registered trials

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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.