Evidence map›Paper›PMID 31371784›Full record

ArticleScientific reports2019

Microbial diversity analysis and screening for novel xylanase enzymes from the sediment of the Lobios Hot Spring in Spain.

Kamila Knapik, Manuel Becerra, María-Isabel González-Siso

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.2field-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

26 citing papers in PubMed, 55 citations in OpenAlex.

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  11. Metabolic versatility ofFrontiers in microbiology · 2023
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  18. Breeding of a thermostable xylanase-producing strain ofFrontiers in bioengineering and biotechnology · 2022
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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

3 authors at 1 institution in 1 country.

Kamila KnapikUniversidade da Coruña, Grupo EXPRELA, Facultade de Ciencias, Centro de Investigacións Científicas Avanzadas (CICA), A Coruña, Spain.
Manuel BecerraUniversidade da Coruña, Grupo EXPRELA, Facultade de Ciencias, Centro de Investigacións Científicas Avanzadas (CICA), A Coruña, Spain.
María-Isabel González-SisoUniversidade da Coruña, Grupo EXPRELA, Facultade de Ciencias, Centro de Investigacións Científicas Avanzadas (CICA), A Coruña, Spain. isabel.gsiso@udc.es.ORCID http://orcid.org/0000-0001-9538-4841
Universidade da Coruña · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we describe the metagenome composition of a microbial community in a hot spring sediment as well as a sequence-based and function-based screening of the metagenome for identification of novel xylanases. The sediment was collected from the Lobios Hot Spring located in the province of Ourense (Spain). Environmental DNA was extracted and sequenced using Illumina technology, and a total of 3.6 Gbp of clean paired reads was produced. A taxonomic classification that was obtained by comparison to the NCBI protein nr database revealed a dominance of Bacteria (93%), followed by Archaea (6%). The most abundant bacterial phylum was Acidobacteria (25%), while Thaumarchaeota (5%) was the main archaeal phylum. Reads were assembled into contigs. Open reading frames (ORFs) predicted on these contigs were searched by BLAST against the CAZy database to retrieve xylanase encoding ORFs. A metagenomic fosmid library of approximately 150,000 clones was constructed to identify functional genes encoding thermostable xylanase enzymes. Function-based screening revealed a novel xylanase-encoding gene (XynA3), which was successfully expressed in E. coli BL21. The resulting protein (41 kDa), a member of glycoside hydrolase family 11 was purified and biochemically characterized. The highest activity was measured at 80 °C and pH 6.5. The protein was extremely thermostable and showed 94% remaining activity after incubation at 60 °C for 24 h and over 70% remaining activity after incubation at 70 °C for 24 h. Xylanolytic activity of the XynA3 enzyme was stimulated in the presence of β-mercaptoethanol, dithiothreitol and Fe

Indexed as

ArchaeaArchaeal ProteinsBacteriaBacterial ProteinsDisaccharidesDNA, EnvironmentalEndo-1,4-beta XylanasesEnzyme AssaysEnzyme StabilityExtremophilesGeologic SedimentsHot SpringsIndustrial MicrobiologyMetagenomeMicrobiotaOpen Reading FramesArchaeal ProteinsBacterial ProteinsDisaccharidesDNA, EnvironmentalEndo-1,4-beta Xylanasesxylobiose

Identifiers

PMID31371784
PMCPMC6671963
OpenAlexW2966731664

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.