Evidence map›Paper›PMID 31385056›Full record

ArticleAMB Express2019

Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries.

Simo Ellilä, Paul Bromann, Mari Nyyssönen, Merja Itävaara, Anu Koivula, Lars Paulin, Kristiina Kruus

Open access · goldAbstract read
In one paragraph

Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Emerging priorities for microbial metagenome research.Bioresource technology reports · 2020
    Review
  10. 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

7 authors at 2 institutions in 1 country.

Simo ElliläVTT Technical Research Centre of Finland, P.O. Box 1000, 02044, Vuorimiehentie, Espoo, Finland. simo.ellila@vtt.fi.ORCID http://orcid.org/0000-0001-7516-3363
Paul BromannVTT Technical Research Centre of Finland, P.O. Box 1000, 02044, Vuorimiehentie, Espoo, Finland.
Mari NyyssönenVTT Technical Research Centre of Finland, P.O. Box 1000, 02044, Vuorimiehentie, Espoo, Finland.
Merja ItävaaraVTT Technical Research Centre of Finland, P.O. Box 1000, 02044, Vuorimiehentie, Espoo, Finland.
Anu KoivulaVTT Technical Research Centre of Finland, P.O. Box 1000, 02044, Vuorimiehentie, Espoo, Finland.
Lars PaulinInstitute of Biotechnology, University of Helsinki, P.O.Box 56, 00014, Helsinki, Finland.
Kristiina KruusVTT Technical Research Centre of Finland, P.O. Box 1000, 02044, Vuorimiehentie, Espoo, Finland.
VTT Technical Research Centre of Finland · FIUniversity of Helsinki · FI

Funding

Seventh Framework Programme 211863Seventh Framework Programme 222699Tekes (FI) 40148/07
6 · The paper itself

Abstract

Xylanases are in important class of industrial enzymes that are essential for the complete hydrolysis of lignocellulosic biomass into fermentable sugars. In the present study, we report the cloning of novel xylanases with interesting properties from compost metagenomics libraries. Controlled composting of lignocellulosic materials was used to enrich the microbial population in lignocellulolytic organisms. DNA extracted from the compost samples was used to construct metagenomics libraries, which were screened for xylanase activity. In total, 40 clones exhibiting xylanase activity were identified and the thermostability of the discovered xylanases was assayed directly from the library clones. Five genes, including one belonging to the more rare family GH8, were selected for subcloning and the enzymes were expressed in recombinant form in E. coli. Preliminary characterization of the metagenome-derived xylanases revealed interesting properties of the novel enzymes, such as high thermostability and specific activity, and differences in hydrolysis profiles. One enzyme was found to perform better than a standard Trichoderma reesei xylanase in the hydrolysis of lignocellulose at elevated temperatures.

Indexed as

CloningCompostLignocelluloseMetagenomicsScreeningXylanase

Identifiers

PMID31385056
PMCPMC6682842
OpenAlexW2966052182

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.