Evidence map›Paper›PMID 32671051›Full record

ArticleFrontiers in bioengineering and biotechnology2020

Functional Validation of Two Fungal Subfamilies in Carbohydrate Esterase Family 1 by Biochemical Characterization of Esterases From Uncharacterized Branches.

Xinxin Li, Kelli Griffin, Sandra Langeveld, Matthias Frommhagen, Emilie N Underlin, Mirjam A Kabel, Ronald P de Vries, Adiphol Dilokpimol

Open access · goldAbstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 25 citations in OpenAlex.

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  11. Fungal Treatment for the Valorization of Technical Soda Lignin.Journal of fungi (Basel, Switzerland) · 2021
    Article
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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

8 authors at 3 institutions in 2 countries.

Xinxin LiFungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Utrecht, Netherlands.
Kelli GriffinFungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Utrecht, Netherlands.
Sandra LangeveldFungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Utrecht, Netherlands.
Matthias FrommhagenLaboratory of Food Chemistry, Wageningen University & Research, Wageningen, Netherlands.
Emilie N UnderlinLaboratory of Food Chemistry, Wageningen University & Research, Wageningen, Netherlands.
Mirjam A KabelLaboratory of Food Chemistry, Wageningen University & Research, Wageningen, Netherlands.
Ronald P de VriesFungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Utrecht, Netherlands.
Adiphol DilokpimolFungal Physiology, Westerdijk Fungal Biodiversity Institute, Fungal Molecular Physiology, Utrecht University, Utrecht, Netherlands.
Wageningen University & Research · NLWesterdijk Fungal Biodiversity Institute · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fungal members of Carbohydrate Esterase family 1 (CE1) from the CAZy database include both acetyl xylan esterases (AXEs) and feruloyl esterases (FAEs). AXEs and FAEs are essential auxiliary enzymes to unlock the full potential of feedstock. They are being used in many biotechnology applications including food and feed, pulp and paper, and biomass valorization. AXEs catalyze the hydrolysis of acetyl group from xylan, while FAEs release ferulic and other hydroxycinnamic acids from xylan and pectin. Previously, we reported a phylogenetic analysis for the fungal members of CE1, establishing five subfamilies (CE1_SF1-SF5). Currently, the characterized AXEs are in the subfamily CE1_SF1, whereas CE1_SF2 contains mainly characterized FAEs. These two subfamilies are more related to each other than to the other subfamilies and are predicted to have evolved from a common ancestor, but target substrates with a different molecular structure. In this study, four ascomycete enzymes from CE1_SF1 and SF2 were heterologously produced in

Indexed as

acetyl xylan esterasecarbohydrate esteraseCAZy subfamiliesferulic acidferuloyl esterasefungiplant biomass degradation

Identifiers

PMID32671051
PMCPMC7332973
OpenAlexW3037082139

What OpenQuestion holds

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LicenceCC BY
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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.