Evidence map›Paper›PMID 37569374›Full record

ArticleInternational journal of molecular sciences2023

Expression and Characterization of Two α-l-Arabinofuranosidases from

Juan A Méndez-Líter, Laura I de Eugenio, Manuel Nieto-Domínguez, Alicia Prieto, María Jesús Martínez

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

0 citing papers in PubMed, 5 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 2 institutions in 2 countries.

Juan A Méndez-LíterDepartment of Microbial & Plant Biotechnology, Centro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council (CSIC), C/Ramiro de Maeztu 9, 28040 Madrid, Spain.
Laura I de EugenioDepartment of Microbial & Plant Biotechnology, Centro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council (CSIC), C/Ramiro de Maeztu 9, 28040 Madrid, Spain.
Manuel Nieto-DomínguezThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, 2800 Kongens Lyngby, Denmark.ORCID 0000-0001-8192-5176
Alicia PrietoDepartment of Microbial & Plant Biotechnology, Centro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council (CSIC), C/Ramiro de Maeztu 9, 28040 Madrid, Spain.ORCID 0000-0002-5075-4025
María Jesús MartínezDepartment of Microbial & Plant Biotechnology, Centro de Investigaciones Biológicas Margarita Salas, Spanish National Research Council (CSIC), C/Ramiro de Maeztu 9, 28040 Madrid, Spain.ORCID 0000-0003-2166-1097
Consejo Superior de Investigaciones Científicas · ESNovo Nordisk Foundation · DK

Funding

Comunidad de Madrid RETOPROSOST-2-CM P2018/EMT-4459MICIU/AEI/FEDER RTI2018-093683-B-I00TransEner Platform, Recovery and Resilience Facility of the European Union H2V2021, Unit 3
6 · The paper itself

Abstract

α-l-arabinofuranosidases are glycosyl hydrolases that catalyze the break between α-l-arabinofuranosyl substituents or between α-l-arabinofuranosides and xylose from xylan or xylooligosaccharide backbones. While they belong to several glycosyl hydrolase (GH) families, there are only 24 characterized GH62 arabinofuranosidases, making them a small and underrepresented group, with many of their features remaining unknown. Aside from their applications in the food industry, arabinofuranosidases can also aid in the processing of complex lignocellulosic materials, where cellulose, hemicelluloses, and lignin are closely linked. These materials can be fully converted into sugar monomers to produce secondary products like second-generation bioethanol. Alternatively, they can be partially hydrolyzed to release xylooligosaccharides, which have prebiotic properties. While endoxylanases and β-xylosidases are also necessary to fully break down the xylose backbone from xylan, these enzymes are limited when it comes to branched polysaccharides. In this article, two new GH62 α-l-arabinofuranosidases from

Indexed as

Endo-1,4-beta XylanasesXylansBiomassGlucuronatesGlycoside HydrolasesHumansHydrolysisOligosaccharidesSubstrate SpecificityTalaromycesXylosealpha-N-arabinofuranosidaseEndo-1,4-beta XylanasesGlucuronatesGlycoside HydrolasesOligosaccharidesXylansxylooligosaccharideXylosebiodegradationGH62glycoside hydrolaseshemicellulose

Identifiers

PMID37569374
PMCPMC10418624
OpenAlexW4385362154

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.