Evidence map›Paper›PMID 27142164›Full record

ArticleMicrobial cell factories2016

Cloning, expression and characterization of a β-D-xylosidase from Lactobacillus rossiae DSM 15814(T).

Erica Pontonio, Jennifer Mahony, Raffaella Di Cagno, Mary O'Connell Motherway, Gabriele Andrea Lugli, Amy O'Callaghan, Maria De Angelis, Marco Ventura, Marco Gobbetti, Douwe van Sinderen

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Draft Genome Sequence ofGenome announcements · 2017
    Article
  11. Review
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

10 authors at 3 institutions in 2 countries.

Erica PontonioDepartment of Soil, Plant and Food Science, University of Bari Aldo Moro, Via G. Amendola 165/A, 70126, Bari, Italy.
Jennifer MahonySchool of Microbiology, University College Cork, Cork, Ireland.
Raffaella Di CagnoDepartment of Soil, Plant and Food Science, University of Bari Aldo Moro, Via G. Amendola 165/A, 70126, Bari, Italy. raffaella.dicagno@uniba.it.
Mary O'Connell MotherwaySchool of Microbiology, University College Cork, Cork, Ireland.
Gabriele Andrea LugliLaboratory of Probiogenomics, Department of Life Sciences, University of Parma, Parma, Italy.
Amy O'CallaghanSchool of Microbiology, University College Cork, Cork, Ireland.
Maria De AngelisDepartment of Soil, Plant and Food Science, University of Bari Aldo Moro, Via G. Amendola 165/A, 70126, Bari, Italy.
Marco VenturaLaboratory of Probiogenomics, Department of Life Sciences, University of Parma, Parma, Italy.
Marco GobbettiDepartment of Soil, Plant and Food Science, University of Bari Aldo Moro, Via G. Amendola 165/A, 70126, Bari, Italy.
Douwe van SinderenSchool of Microbiology, University College Cork, Cork, Ireland.
University College Cork · IEUniversity of Bari Aldo Moro · ITUniversity of Parma · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAmong the oligosaccharides that may positively affect the gut microbiota, xylo-oligosaccharides (XOS) and arabinoxylan oligosaccharides (AXOS) possess promising functional properties. Ingestion of XOS has been reported to contribute to anti-oxidant, anti-bacterial, immune-modulatory and anti-diabetic activities. Because of the structural complexity and chemical heterogeneity, complete degradation of xylan-containing plant polymers requires the synergistic activity of several enzymes. Endo-xylanases and β-D-xylosidases, collectively termed xylanases, represent the two key enzymes responsible for the sequential hydrolysis of xylan. Xylanase cocktails are used on an industrial scale for biotechnological purposes. Lactobacillus rossiae DSM 15814(T) can utilize an extensive set of carbon sources, an ability that is likely to contribute to its adaptive ability. In this study, the capacity of this strain to utilize XOS, xylan, D-xylose and L-arabinose was investigated.

resultsGenomic and transcriptomic analyses revealed the presence of two gene clusters, designated xyl and ara, encoding proteins predicted to be responsible for XOS uptake and hydrolysis and D-xylose utilization, and L-arabinose metabolism, respectively. The deduced amino acid sequence of one of the genes of the xyl gene cluster, LROS_1108 (designated here as xylA), shows high similarity to (predicted) β-D-xylosidases encoded by various lactic acid bacteria, and belongs to glycosyl hydrolase family 43. Heterologously expressed XylA was shown to completely hydrolyse XOS to xylose and showed optimal activity at pH 6.0 and 40 °C. Furthermore, β-D-xylosidase activity of L. rossiae DSM 15814(T) was also measured under sourdough conditions.

conclusionsThis study highlights the ability of L. rossiae DSM 15814(T) to utilize XOS, which is a very useful trait when selecting starters with specific metabolic performances for sourdough fermentation or as probiotics.

Indexed as

Gene Expression Regulation, BacterialArabinoseCloning, MolecularHydrogen-Ion ConcentrationHydrolysisLactobacillusMultigene FamilyOligosaccharidesPhylogenyPlasmidsRecombinant ProteinsTemperatureXyloseXylosidasesArabinoseexo-1,4-beta-D-xylosidaseOligosaccharidesRecombinant ProteinsXyloseXylosidasesFunctional foodsGut microbiotaPrebioticProbioticSourdoughXylo-oligosaccharides

Identifiers

PMID27142164
PMCPMC4855831
OpenAlexW2346226236

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.