Evidence map›Paper›PMID 29177717›Full record

ArticleExtremophiles : life under extreme conditions2018

Biochemical characterization of a thermostable endomannanase/endoglucanase from Dictyoglomus turgidum.

Francesca Anna Fusco, Raffaele Ronca, Gabriella Fiorentino, Emilia Pedone, Patrizia Contursi, Simonetta Bartolucci, Danila Limauro

Abstract 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  7. Lignocellulolytic extremozymes and their biotechnological applications.Extremophiles : life under extreme conditions · 2023
    Review
  8. Insight into CAZymes ofInternational journal of molecular sciences · 2022
    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

7 authors at 2 institutions in 1 country.

Francesca Anna FuscoDipartimento di Biologia, University of Naples Federico II, Complesso universitario di Monte S. Angelo, Via Cinthia, Naples, Italy.
Raffaele RoncaDipartimento di Biologia, University of Naples Federico II, Complesso universitario di Monte S. Angelo, Via Cinthia, Naples, Italy.
Gabriella FiorentinoDipartimento di Biologia, University of Naples Federico II, Complesso universitario di Monte S. Angelo, Via Cinthia, Naples, Italy.
Emilia PedoneIstituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, Naples, Italy.
Patrizia ContursiDipartimento di Biologia, University of Naples Federico II, Complesso universitario di Monte S. Angelo, Via Cinthia, Naples, Italy.
Simonetta BartolucciDipartimento di Biologia, University of Naples Federico II, Complesso universitario di Monte S. Angelo, Via Cinthia, Naples, Italy.
Danila LimauroDipartimento di Biologia, University of Naples Federico II, Complesso universitario di Monte S. Angelo, Via Cinthia, Naples, Italy. limauro@unina.it.
University of Naples Federico II · ITInstitute of Biostructure and Bioimaging · IT

Funding

BIOPOLIS: PON03PE_00107_1 E48C14000030005
6 · The paper itself

Abstract

Dictyoglomus turgidum is a hyperthermophilic, anaerobic, gram-negative bacterium that shows an array of putative glycoside hydrolases (GHs) encoded by its genome, a feature that makes this microorganism very interesting for biotechnological applications. The aim of this work is the characterization of a hyperthermophilic GH5, Dtur_0671, of D. turgidum, annotated as endoglucanase and herein named DturCelB in agreement to DturCelA, which was previously characterized. The synthetic gene was expressed in Escherichia coli. The purified recombinant enzyme is active as a monomer (40 kDa) and CD structural studies showed a conserved α/β structure at different temperatures (25 and 70 °C) and high thermoresistance (Tm of 88 °C). Interestingly, the enzyme showed high endo-β-1,4-mannanase activity vs various mannans, but low endo-β-1,4 glucanase activity towards carboxymethylcellulose. The K

Indexed as

ThermotoleranceBacterial ProteinsCarboxymethylcellulose SodiumCellulaseEnzyme StabilityExtreme HeatGram-Negative BacteriaMannansMannosidasesSubstrate SpecificityBacterial ProteinsCarboxymethylcellulose SodiumCellulaseendo-1,4-beta-D-mannanaseMannansMannosidasesDictyoglomus turgidumEndoglucanaseEndomannanaseThermophilic enzyme

Identifiers

PMID29177717
OpenAlexW2769802623

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.