Evidence map›Paper›PMID 34530892›Full record

ArticleBiotechnology for biofuels2021

Engineering the substrate binding site of the hyperthermostable archaeal endo-β-1,4-galactanase from Ignisphaera aggregans.

Sebastian J Muderspach, Folmer Fredslund, Verena Volf, Jens-Christian Navarro Poulsen, Thomas H Blicher, Mads Hartvig Clausen, Kim Krighaar Rasmussen, Kristian B R M Krogh, Kenneth Jensen, Leila Lo Leggio

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biotechnology for biofuels, 2021. 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
1.0field-weighted citation impact, top 26% 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, 10 citations in OpenAlex.

  1. 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

10 authors at 3 institutions in 2 countries.

Sebastian J MuderspachDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark.
Folmer FredslundDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark.
Verena VolfNovozymes A/S, Biologiens vej 2, 2800, Kongens Lyngby, Denmark.
Jens-Christian Navarro PoulsenDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark.
Thomas H BlicherNovozymes A/S, Biologiens vej 2, 2800, Kongens Lyngby, Denmark.
Mads Hartvig ClausenCenter for Nanomedicine and Theranostics, Department of Chemistry, Technical University of Denmark, Kemitorvet 207, 2800, Kgs. Lyngby, Denmark.
Kim Krighaar RasmussenDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark.
Kristian B R M KroghNovozymes A/S, Biologiens vej 2, 2800, Kongens Lyngby, Denmark.
Kenneth JensenNovozymes A/S, Biologiens vej 2, 2800, Kongens Lyngby, Denmark. khjn@novozymes.com.
Leila Lo LeggioDepartment of Chemistry, University of Copenhagen, Universitetsparken 5, 2100, Copenhagen, Denmark. leila@chem.ku.dk.ORCID http://orcid.org/0000-0002-5135-0882
University of Copenhagen · DKNovozymes (Denmark) · DKTechnical University of Denmark · DK

Funding

fp7 ideas: european research council 265933uddannelses- og forskningsministeriet DANSCATT
6 · The paper itself

Abstract

backgroundEndo-β-1,4-galactanases are glycoside hydrolases (GH) from the GH53 family belonging to the largest clan of GHs, clan GH-A. GHs are ubiquitous and involved in a myriad of biological functions as well as being widely used industrially. Endo-β-1,4-galactanases, in particular hydrolyse galactan and arabinogalactan in pectin, a major component of the primary plant cell wall, with important functions in plant defence and application in the food and other industries. Here, we explore the family's biological diversity by characterizing the first archaeal and hyperthermophilic GH53 galactanase, and utilize it as a scaffold for engineering enzymes with different product lengths.

resultsA galactanase gene was identified in the genome of the anaerobic hyperthermophilic archaeon Ignisphaera aggregans, and the isolated catalytic domain expressed and characterized (IaGal). IaGal presents the typical (βα)

conclusionsWe have characterized in detail the most thermophilic endo-β-1,4-galactanase known to date and successfully engineered it to modify the degradation profile, while maintaining much of its desirable thermostability. This is an important achievement as oligosaccharide products length is an important property for industrial and natural GHs alike.

Indexed as

ArchaeaBiomass degradationCrystal structureDegradation profilesExtreme thermophileGalactanGlycoside hydrolaseHigh-performance anion-exchange chromatographyIgnisphaera aggregansRational design

Identifiers

PMID34530892
PMCPMC8447715
OpenAlexW3199386619

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.