Evidence map›Paper›PMID 28074318›Full record

ArticleJournal of industrial microbiology & biotechnology2017

Boosted large-scale production and purification of a thermostable archaeal phosphotriesterase-like lactonase for organophosphate decontamination.

Odile Francesca Restaino, Maria Giovanna Borzacchiello, Ilaria Scognamiglio, Elena Porzio, Giuseppe Manco, Luigi Fedele, Cinzia Donatiello, Mario De Rosa, Chiara Schiraldi

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Article in Journal of industrial microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

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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

9 authors at 4 institutions in 1 country.

Odile Francesca RestainoDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy. odilefrancesca.restaino@unina2.it.
Maria Giovanna BorzacchielloDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy.
Ilaria ScognamiglioDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy.
Elena PorzioInstitute of Protein Biochemistry, National Research Council of Italy, Naples, Italy.
Giuseppe MancoInstitute of Protein Biochemistry, National Research Council of Italy, Naples, Italy.
Luigi FedeleDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy.
Cinzia DonatielloDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy.
Mario De RosaDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy.
Chiara SchiraldiDepartment of Experimental Medicine, Section of Biotechnology and Molecular Biology, Second University of Naples, Naples, Italy. chiara.schiraldi@unina2.it.
University of Naples Federico II · ITUniversity of Campania "Luigi Vanvitelli" · ITInstitute of Protein Biochemistry · ITNational Research Council · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermostable phosphotriesterase-like lactonases (PLLs) from extremophile archaea, like SsoPox from Sulfolobus solfataricus, are attractive biotechnological tools with industrial applications as organophosphate decontaminants, but their manufacturing still remains an unresolved issue because of the high costs and the low production yields. In this paper, for the first time, an efficient biotechnological process for the production and purification of a recombinant, engineered PLL, SsoPox W263F, expressed in E. coli, has been set up by studying new induction strategies, by designing high cell density cultivations and a new membrane-based downstream process. In fed batches, the enzyme production was boosted of 69-fold up to 4660.0 U L

Indexed as

Genes, ArchaealBatch Cell Culture TechniquesCarboxylic Ester HydrolasesCulture MediaDecontaminationEscherichia coliFermentationIndustrial MicrobiologyMicroorganisms, Genetically-ModifiedOrganophosphatesPhosphoric Triester HydrolasesProtein EngineeringSulfolobus solfataricusCarboxylic Ester HydrolasesCulture MediagluconolactonaseOrganophosphatesPhosphoric Triester HydrolasesHigh cell density cultivationOrganophosphatesSulfolobus solfataricusThermostable phosphotriesterase-like lactonaseUltrafiltration

Identifiers

PMID28074318
OpenAlexW2569344827

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.