Evidence map›Paper›PMID 27876889›Full record

ArticleScientific reports2016

Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications.

Benjamin Rémy, Laure Plener, Laetitia Poirier, Mikael Elias, David Daudé, Eric Chabrière

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  5. Engineering quorum quenching acylases with improved kinetic and biochemical properties.Protein science : a publication of the Protein Society · 2024
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  6. Review
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  19. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
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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

6 authors at 3 institutions in 1 country.

Benjamin RémyAix Marseille Univ, INSERM, CNRS, IRD, URMITE, Marseille, France.
Laure PlenerGene&GreenTK, Faculté de Médecine, 27 boulevard Jean Moulin, 13385 Marseille Cedex 5, France.
Laetitia PoirierAix Marseille Univ, INSERM, CNRS, IRD, URMITE, Marseille, France.
Mikael EliasUniversity of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics &Biotechnology Institute, St. Paul, MN 55108, USA.
David DaudéGene&GreenTK, Faculté de Médecine, 27 boulevard Jean Moulin, 13385 Marseille Cedex 5, France.
Eric ChabrièreAix Marseille Univ, INSERM, CNRS, IRD, URMITE, Marseille, France.
Inserm · FRMéditerranée Infection Foundation · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extremozymes have gained considerable interest as they could meet industrial requirements. Among these, SsoPox is a hyperthermostable enzyme isolated from the archaeon Sulfolobus solfataricus. This enzyme is a lactonase catalyzing the hydrolysis of acyl-homoserine lactones; these molecules are involved in Gram-negative bacterial communication referred to as quorum sensing. SsoPox exhibits promiscuous phosphotriesterase activity for the degradation of organophosphorous chemicals including insecticides and chemical warfare agents. Owing to its bi-functional catalytic abilities as well as its intrinsic stability, SsoPox is appealing for many applications, having potential uses in the agriculture, defense, food and health industries. Here we investigate the biotechnological properties of the mutant SsoPox-W263I, a variant with increased lactonase and phosphotriesterase activities. We tested enzyme resistance against diverse process-like and operating conditions such as heat resistance, contact with organic solvents, sterilization, storage and immobilization. Bacterial secreted materials from both Gram-negative and positive bacteria were harmless on SsoPox-W263I activity and could reactivate heat-inactivated enzyme. SsoPox showed resistance to harsh conditions demonstrating that it is an extremely attractive enzyme for many applications. Finally, the potential of SsoPox-W263I to be active at subzero temperature is highlighted and discussed in regards to the common idea that hyperthermophile enzymes are nearly inactive at low temperatures.

Indexed as

AlginatesBiocatalysisBiotechnologyCarboxylic Ester HydrolasesCross-Linking ReagentsEnzyme StabilityGlucuronic AcidHeat-Shock ResponseHexuronic AcidsImmobilized ProteinsParaoxonSolventsSterilizationStress, PhysiologicalSulfolobus solfataricusTemperatureAlginatesCarboxylic Ester HydrolasesCross-Linking ReagentsgluconolactonaseGlucuronic AcidHexuronic AcidsImmobilized ProteinsParaoxonSolvents

Identifiers

PMID27876889
PMCPMC5120315
OpenAlexW2550137417

What OpenQuestion holds

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LicenceCC BY
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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.