Evidence map›Paper›PMID 25361767›Full record

ArticleThe Journal of biological chemistry2014

Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency.

Manuel Eibinger, Thomas Ganner, Patricia Bubner, Stephanie Rošker, Daniel Kracher, Dietmar Haltrich, Roland Ludwig, Harald Plank, Bernd Nidetzky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

105 citing papers in PubMed, 284 citations in OpenAlex.

  1. Article
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  12. Discovery of a Novel Cellobiose Dehydrogenase fromJournal of microbiology and biotechnology · 2024
    Article
  13. TheApplied and environmental microbiology · 2023
    Article
  14. Article
  15. Efficient Secretory Production of Lytic Polysaccharide MonooxygenaseInternational journal of molecular sciences · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

45 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Manuel EibingerFrom the Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, A-8010 Graz, Austria.
Thomas GannerInstitute of Electron Microscopy and Nanoanalysis and.
Patricia BubnerFrom the Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, A-8010 Graz, Austria.
Stephanie RoškerInstitute of Electron Microscopy and Nanoanalysis and.
Daniel KracherDepartment of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria, and.
Dietmar HaltrichDepartment of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria, and.
Roland LudwigDepartment of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria, and.
Harald PlankInstitute of Electron Microscopy and Nanoanalysis and Graz Centre for Electron Microscopy, Steyrergasse 17, A-8010 Graz, Austria, harald.plank@felmi-zfe.at.
Bernd NidetzkyFrom the Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, A-8010 Graz, Austria, Austrian Centre of Industrial Biotechnology, Petersgasse 14, A-8010 Graz, Austria bernd.nidetzky@tugraz.at.
Austrian Centre for Electron Microscopy and Nanoanalysis · ATBOKU University · ATGraz University of Technology · AT

Funding

Austrian Science Fund FWF P 24156Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Lytic polysaccharide monooxygenase (LPMO) represents a unique principle of oxidative degradation of recalcitrant insoluble polysaccharides. Used in combination with hydrolytic enzymes, LPMO appears to constitute a significant factor of the efficiency of enzymatic biomass depolymerization. LPMO activity on different cellulose substrates has been shown from the slow release of oxidized oligosaccharides into solution, but an immediate and direct demonstration of the enzyme action on the cellulose surface is lacking. Specificity of LPMO for degrading ordered crystalline and unordered amorphous cellulose material of the substrate surface is also unknown. We show by fluorescence dye adsorption analyzed with confocal laser scanning microscopy that a LPMO (from Neurospora crassa) introduces carboxyl groups primarily in surface-exposed crystalline areas of the cellulosic substrate. Using time-resolved in situ atomic force microscopy we further demonstrate that cellulose nano-fibrils exposed on the surface are degraded into shorter and thinner insoluble fragments. Also using atomic force microscopy, we show that prior action of LPMO enables cellulases to attack otherwise highly resistant crystalline substrate areas and that it promotes an overall faster and more complete surface degradation. Overall, this study reveals key characteristics of LPMO action on the cellulose surface and suggests the effects of substrate morphology on the synergy between LPMO and hydrolytic enzymes in cellulose depolymerization.

Indexed as

CellulaseCelluloseFungal ProteinsHydrolysisMixed Function OxygenasesNeurospora crassaOxidation-ReductionSurface PropertiesCellulaseCelluloseFungal ProteinsMixed Function OxygenasesAtomic Force Microscopy (AFM)BiofuelCellulaseCelluloseCopper MonooxygenaseGH61-AA9Lytic Polysaccharide Monooxygenase (LPMO)Oxidative Cellulose Surface DegradationSynergy

Identifiers

PMID25361767
PMCPMC4276861
OpenAlexW2103990390

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.