Evidence map›Paper›PMID 38878205›Full record

ArticleMolecular biology reports2024

Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity.

Adriana S da Silva, Patricia P Adriani, Gabriel S de Oliveira, Adriana Rios Lopes Rocha, Elen A Perpétuo, Marcio V B Dias, Felipe S Chambergo

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Article in Molecular biology reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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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

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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.

Adriana S da SilvaEscola de Artes, Ciências e HumanidadesErmelino Matarazzo, Universidade de São Paulo, 1000 Av. Arlindo Bettio, São Paulo, CEP: 3828-000, Brazil.
Patricia P AdrianiDepartamento de Farmacologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.
Gabriel S de OliveiraDepartamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.
Adriana Rios Lopes RochaLaboratory of Biochemistry, Instituto Butantan, Av. Vital Brasil, São Paulo, 1500, Brazil.
Elen A PerpétuoBio4Tec, Centro de Capacitação e Pesquisa em Meio Ambiente, CEPEMA-POLI-USP, Universidade de São Paulo, Cubatão, Brazil.
Marcio V B DiasDepartamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.
Felipe S ChambergoEscola de Artes, Ciências e HumanidadesErmelino Matarazzo, Universidade de São Paulo, 1000 Av. Arlindo Bettio, São Paulo, CEP: 3828-000, Brazil. fscha@usp.br.

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 142311/2016-2Conselho Nacional de Desenvolvimento Científico e Tecnológico 308223/2023-3Fundação de Amparo à Pesquisa do Estado de São Paulo 2017/25705-8Fundação de Amparo à Pesquisa do Estado de São Paulo 2022/12234-5
6 · The paper itself

Abstract

backgroundEsterases (EC 3.1.1.X) are enzymes that catalyze the hydrolysis ester bonds. These enzymes have large potential for diverse applications in fine industries, particularly in pharmaceuticals, cosmetics, and bioethanol production. METHODS AND

resultsIn this study, a gene encoding an esterase from Thermobifida fusca YX (TfEst) was successfully cloned, and its product was overexpressed in Escherichia coli and purified using affinity chromatography. The TfEst kinetic assay revealed catalytic efficiencies of 0.58 s

conclusionsThe enzyme stability over a broad pH range and its activity at elevated temperatures make it an appealing candidate for industrial processes. Overall, TfEst emerges as a promising enzymatic tool with significant implications for the advancement of biotechnology and biofuels industries.

Indexed as

AcetylesteraseEsterasesThermobifidaBacterial ProteinsButyratesCloning, MolecularEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationHydrolysisKineticsNitrophenolsSubstrate SpecificityTemperatureXylans4-nitrophenyl acetate4-nitrophenyl butyrateAcetylesteraseacetylxylan esteraseBacterial ProteinsButyratesEsterasesNitrophenolsXylansAcetyl xylan esterase activityEsteraseThermobifida fuscaThermostable enzyme

Identifiers

PMID38878205

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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.