Evidence map›Paper›PMID 30014242›Full record

ArticleExtremophiles : life under extreme conditions2018

Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions.

Patricia S Kumagai, Raissa F Gutierrez, Jose L S Lopes, Julia M Martins, David M Jameson, Aline M Castro, Luiz F Martins, Ricardo DeMarco, Nelma R S Bossolan, B A Wallace and 1 more

Open access · greenAbstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2018. 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
0.6field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 14 citations in OpenAlex.

  1. The Biodegradation of Acrylic-Coated Woven Fabrics byMaterials (Basel, Switzerland) · 2025
    Article
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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 at 5 institutions in 3 countries.

Patricia S KumagaiDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, Av João Dagnone 1100, São Carlos, SP, 13563-120, Brazil.ORCID http://orcid.org/0000-0001-7546-3091
Raissa F GutierrezDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, Av João Dagnone 1100, São Carlos, SP, 13563-120, Brazil.ORCID http://orcid.org/0000-0002-7017-8061
Jose L S LopesDepartamento de Física Aplicada, Instituto de Física, Universidade de São Paulo, Rua do Matão 1371, São Paulo, SP, 05508-090, Brazil.ORCID http://orcid.org/0000-0003-1281-0521
Julia M MartinsDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, Av João Dagnone 1100, São Carlos, SP, 13563-120, Brazil.
David M JamesonDepartment of Cell and Molecular Biology, University of Hawaii at Manoa, 1960 East-West Road, Honolulu, HI, 96822, USA.
Aline M CastroGerência de Biotecnologia, Centro de Pesquisas e Desenvolvimento (CENPES), Petrobrás, Av Horácio Macedo 950, Ilha do Fundão, Rio de Janeiro, RJ, 21941-915, Brazil.
Luiz F MartinsGerência de Biotecnologia, Centro de Pesquisas e Desenvolvimento (CENPES), Petrobrás, Av Horácio Macedo 950, Ilha do Fundão, Rio de Janeiro, RJ, 21941-915, Brazil.
Ricardo DeMarcoDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, Av João Dagnone 1100, São Carlos, SP, 13563-120, Brazil.ORCID http://orcid.org/0000-0001-8944-1301
Nelma R S BossolanDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, Av João Dagnone 1100, São Carlos, SP, 13563-120, Brazil.ORCID http://orcid.org/0000-0002-5484-9283
B A WallaceInstitute of Structural and Molecular Biology, Birkbeck College, University of London, Malet St, London, WC1E 7HX, UK.
Ana P U AraujoDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, Av João Dagnone 1100, São Carlos, SP, 13563-120, Brazil. anapaula@ifsc.usp.br.ORCID http://orcid.org/0000-0001-5455-084X
Universidade de São Paulo · BRPetrobras (Brazil) · BRInstitute of Structural and Molecular Biology · GBUniversidade Federal de São Carlos · BRUniversity of Hawaiʻi at Mānoa · US

Funding

Agência Nacional do Petróleo, Gás Natural e Biocombustíveis 05/2015Biotechnology and Biological Sciences Research Council N012763Conselho Nacional de Desenvolvimento Científico e Tecnológico 150417/2016-0Conselho Nacional de Desenvolvimento Científico e Tecnológico 303513/2016-0Conselho Nacional de Desenvolvimento Científico e Tecnológico 406429/2016-2Conselho Nacional de Desenvolvimento Científico e Tecnológico 407337/2013-0Fundação de Amparo à Pesquisa do Estado de São Paulo 15/50347-2Petrobras 0050.0079046.12.9
6 · The paper itself

Abstract

The biotechnological and industrial uses of thermostable and organic solvent-tolerant enzymes are extensive and the investigation of such enzymes from microbiota present in oil reservoirs is a promising approach. Searching sequence databases for esterases from such microbiota, we have identified in silico a potentially secreted esterase from Acetomicrobium hydrogeniformans, named AhEst. The recombinant enzyme was produced in E. coli to be used in biochemical and biophysical characterization studies. AhEst presented hydrolytic activity on short-acyl-chain p-nitrophenyl ester substrates. AhEst activity was high and stable in temperatures up to 75 °C. Interestingly, high salt concentration induced a significant increase of catalytic activity. AhEst still retained ~ 50% of its activity in 30% concentration of several organic solvents. Synchrotron radiation circular dichroism and fluorescence spectroscopies confirmed that AhEst displays high structural stability in extreme conditions of temperature, salinity, and organic solvents. The enzyme is a good emulsifier agent and is able to partially reverse the wettability of an oil-wet carbonate substrate, making it of potential interest for use in enhanced oil recovery. All the traits observed in AhEst make it an interesting candidate for many industrial applications, such as those in which a significant hydrolytic activity at high temperatures is required.

Indexed as

Extreme EnvironmentsProtein DenaturationBacterial ProteinsEnzyme StabilityEscherichia coliEsterasesHot TemperatureHydrophobic and Hydrophilic InteractionsRecombinant ProteinsSalinitySolventsSubstrate SpecificityBacterial ProteinsEsterasesRecombinant ProteinsSolventsEnhanced oil recovery (EOR)EsteraseFluorescence spectroscopyProtein stabilitySynchrotron radiation circular dichroism (SRCD) spectroscopy

Identifiers

PMID30014242
OpenAlexW2884278356

What OpenQuestion holds

Textmetadata
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.