Evidence map›Paper›PMID 28220903›Full record

ArticleScientific reports2017

Application of carbohydrate arrays coupled with mass spectrometry to detect activity of plant-polysaccharide degradative enzymes from the fungus Aspergillus niger.

Jolanda M van Munster, Baptiste Thomas, Michel Riese, Adrienne L Davis, Christopher J Gray, David B Archer, Sabine L Flitsch

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

4 citing papers in PubMed, 14 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Jolanda M van MunsterFungal Biology and Genetics, School of Life Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Baptiste ThomasChemical Biology, Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Michel RieseChemical Biology, Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Adrienne L DavisSchool of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Christopher J GrayChemical Biology, Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
David B ArcherFungal Biology and Genetics, School of Life Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
Sabine L FlitschChemical Biology, Manchester Institute for Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
University of Manchester · GBUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G01616X/1Biotechnology and Biological Sciences Research Council BB/K01434X/1
6 · The paper itself

Abstract

Renewables-based biotechnology depends on enzymes to degrade plant lignocellulose to simple sugars that are converted to fuels or high-value products. Identification and characterization of such lignocellulose degradative enzymes could be fast-tracked by availability of an enzyme activity measurement method that is fast, label-free, uses minimal resources and allows direct identification of generated products. We developed such a method by applying carbohydrate arrays coupled with MALDI-ToF mass spectrometry to identify reaction products of carbohydrate active enzymes (CAZymes) of the filamentous fungus Aspergillus niger. We describe the production and characterization of plant polysaccharide-derived oligosaccharides and their attachment to hydrophobic self-assembling monolayers on a gold target. We verify effectiveness of this array for detecting exo- and endo-acting glycoside hydrolase activity using commercial enzymes, and demonstrate how this platform is suitable for detection of enzyme activity in relevant biological samples, the culture filtrate of A. niger grown on wheat straw. In conclusion, this versatile method is broadly applicable in screening and characterisation of activity of CAZymes, such as fungal enzymes for plant lignocellulose degradation with relevance to biotechnological applications as biofuel production, the food and animal feed industry.

Indexed as

Aspergillus nigerBiotechnologyFungal ProteinsGlycoside HydrolasesLigninSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationFungal ProteinsGlycoside HydrolasesLigninlignocellulose

Identifiers

PMID28220903
PMCPMC5318901
OpenAlexW2591511879

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.