Evidence map›Paper›PMID 32683479›Full record

ArticleEuropean biophysics journal : EBJ2020

Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis.

Ana Elisa T Leite, Lorenzo Briganti, Evandro Ares de Araújo, Vanessa de Oliveira Arnoldi Pellegrini, Cesar Moyses Camilo, Igor Polikarpov

Open access · greenAbstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
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

6 authors at 1 institution in 2 countries.

Ana Elisa T LeiteSão Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil.
Lorenzo BrigantiSão Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil.
Evandro Ares de AraújoSão Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil.
Vanessa de Oliveira Arnoldi PellegriniSão Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil.
Cesar Moyses CamiloSão Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil.
Igor PolikarpovSão Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil. ipolikarpov@ifsc.usp.br.ORCID http://orcid.org/0000-0001-9496-4174
Universidade de São Paulo · BR

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 303988/2016-9Conselho Nacional de Desenvolvimento Científico e Tecnológico 440977/2016-9Fundação de Amparo à Pesquisa do Estado de São Paulo 2015/13684-0
6 · The paper itself

Abstract

Bacterial esterases are highly versatile enzymes, currently widely used in detergents, biosurfactants, bioemulsifiers and as biocatalysts in paper and food industries. Present work describes heterologous expression, purification, and biophysical and biochemical characterization of a halotolerant esterase from Bacillus licheniformis (BlEstA). BlEstA preferentially cleaves pNP-octanoate and both activity and stability of the enzyme increased in the presence of 2 M NaCl, and also with several organic solvents (ethanol, methanol and DMSO). Furthermore, BlEstA has considerable emulsifying properties, particularly with olive oil as substrate. Our studies also show that the enzyme is monomeric in solution and its small-angle X-ray scattering low-resolution molecular envelope fits well its high-resolution homology model.

Indexed as

Bacillus licheniformisBiocatalysisEmulsifying AgentsEsterasesHydrogen-Ion ConcentrationModels, MolecularPhylogenyProtein ConformationSodium ChlorideSubstrate SpecificityTemperatureEmulsifying AgentsEsterasesSodium ChlorideBacillus licheniformisBiochemical characterizationEsterasesSmall-angle X-ray scattering

Identifiers

PMID32683479
OpenAlexW3043525708

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.