Evidence map›Paper›PMID 31532909›Full record

ArticleThe FEBS journal2020

Polysaccharide oxidation by lytic polysaccharide monooxygenase is enhanced by engineered cellobiose dehydrogenase.

Daniel Kracher, Zarah Forsberg, Bastien Bissaro, Sonja Gangl, Marita Preims, Christoph Sygmund, Vincent G H Eijsink, Roland Ludwig

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 71 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

8 authors at 3 institutions in 3 countries.

Daniel KracherDepartment of Food Science and Technology, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0002-3856-3170
Zarah ForsbergFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.ORCID 0000-0002-8236-7986
Bastien BissaroFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.ORCID 0000-0001-8354-3892
Sonja GanglDepartment of Food Science and Technology, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
Marita PreimsDepartment of Food Science and Technology, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
Christoph SygmundDepartment of Food Science and Technology, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.
Vincent G H EijsinkFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences (NMBU), Ås, Norway.ORCID 0000-0002-9220-8743
Roland LudwigDepartment of Food Science and Technology, BOKU - University of Natural Resources and Life Sciences, Vienna, Austria.ORCID 0000-0002-5058-5874
BOKU University · ATNorwegian University of Life Sciences · NOUniversity of Manchester · GB

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

The catalytic function of lytic polysaccharide monooxygenases (LPMOs) to cleave and decrystallize recalcitrant polysaccharides put these enzymes in the spotlight of fundamental and applied research. Here we demonstrate that the demand of LPMO for an electron donor and an oxygen species as cosubstrate can be fulfilled by a single auxiliary enzyme: an engineered fungal cellobiose dehydrogenase (CDH) with increased oxidase activity. The engineered CDH was about 30 times more efficient in driving the LPMO reaction due to its 27 time increased production of H

Indexed as

Carbohydrate DehydrogenasesCelluloseHydrogen PeroxideMixed Function OxygenasesPolysaccharidesCarbohydrate Dehydrogenasescellobiose-quinone oxidoreductaseCelluloseHydrogen PeroxideMixed Function OxygenasesPolysaccharidescellobiose dehydrogenasecellulose degradationcopper monooxygenasehydrogen peroxidelytic polysaccharide monooxygenase

Identifiers

PMID31532909
PMCPMC7078924
OpenAlexW2973759826

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.