Evidence map›Paper›PMID 30267127›Full record

ArticleApplied microbiology and biotechnology2018

Analysis of the substrate specificity of α-L-arabinofuranosidases by DNA sequencer-aided fluorophore-assisted carbohydrate electrophoresis.

Maria João Maurício da Fonseca, Edita Jurak, Kim Kataja, Emma R Master, Jean-Guy Berrin, Ingeborg Stals, Tom Desmet, Anita Van Landschoot, Yves Briers

Open access · greenAbstract read
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In one paragraph

Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 54% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. Article
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

9 authors at 4 institutions in 4 countries.

Maria João Maurício da FonsecaDepartment of Biotechnology, Ghent University, Ghent, Belgium.
Edita JurakDepartment of Biotechnology and Chemical Technology, Aalto University, Espoo, Finland.
Kim KatajaDepartment of Biotechnology and Chemical Technology, Aalto University, Espoo, Finland.
Emma R MasterDepartment of Biotechnology and Chemical Technology, Aalto University, Espoo, Finland.
Jean-Guy BerrinINRA, Aix Marseille Université, UMR1163 BBF, Marseille, France.
Ingeborg StalsDepartment of Materials, Textiles and Chemical Engineering, Ghent University, Ghent, Belgium.
Tom DesmetDepartment of Biotechnology, Ghent University, Ghent, Belgium.
Anita Van LandschootDepartment of Biotechnology, Ghent University, Ghent, Belgium.
Yves BriersDepartment of Biotechnology, Ghent University, Ghent, Belgium. Yves.Briers@UGent.be.ORCID http://orcid.org/0000-0001-9682-7827
Ghent University · BEAalto University · FIAix-Marseille Université · FRUniversity of Toronto · CA

Funding

Research fund of the University College Ghent and Ghent University B/13845/01
6 · The paper itself

Abstract

Carbohydrate-active enzyme discovery is often not accompanied by experimental validation, demonstrating the need for techniques to analyze substrate specificities of carbohydrate-active enzymes in an efficient manner. DNA sequencer-aided fluorophore-assisted carbohydrate electrophoresis (DSA-FACE) is utmost appropriate for the analysis of glycoside hydrolases that have complex substrate specificities. DSA-FACE is demonstrated here to be a highly convenient method for the precise identification of the specificity of different α-L-arabinofuranosidases for (arabino)xylo-oligosaccharides ((A)XOS). The method was validated with two α-L-arabinofuranosidases (EC 3.2.1.55) with well-known specificity, specifically a GH62 α-L-arabinofuranosidase from Aspergillus nidulans (AnAbf62A-m2,3) and a GH43 α-L-arabinofuranosidase from Bifidobacterium adolescentis (BaAXH-d3). Subsequently, application of DSA-FACE revealed the AXOS specificity of two α-L-arabinofuranosidases with previously unknown AXOS specificities. PaAbf62A, a GH62 α-L-arabinofuranosidase from Podospora anserina strain S mat+, was shown to target the O-2 and the O-3 arabinofuranosyl monomers as side chain from mono-substituted β-D-xylosyl residues, whereas a GH43 α-L-arabinofuranosidase from a metagenomic sample (AGphAbf43) only removes an arabinofuranosyl monomer from the smallest AXOS tested. DSA-FACE excels ionic chromatography in terms of detection limit for (A)XOS (picomolar sensitivity), hands-on and analysis time, and the analysis of the degree of polymerization and binding site of the arabinofuranosyl substituent.

Indexed as

Sequence Analysis, DNAAspergillus nidulansBifidobacterium adolescentisCarbohydratesElectrophoresisFluorescent DyesGlycoside HydrolasesLimit of DetectionMetagenomicsPodosporaSubstrate Specificityalpha-N-arabinofuranosidaseCarbohydratesFluorescent DyesGlycoside HydrolasesDSA-FACEEnzyme analysisHPAEC-PADSubstrate specificityα-L-arabinofuranosidases

Identifiers

PMID30267127
OpenAlexW2892736660

What OpenQuestion holds

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Registered trials

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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.