Evidence map›Paper›PMID 22204630›Full record

ArticleMicrobial cell factories2011

Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes.

Mathieu Bey, Jean-Guy Berrin, Laetitia Poidevin, Jean-Claude Sigoillot

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2011. 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
6.7field-weighted citation impact, top 3% 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, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Discovery of a Novel Cellobiose Dehydrogenase fromJournal of microbiology and biotechnology · 2024
    Article
  4. Expression of cellobiose dehydrogenase gene inFrontiers in microbiology · 2024
    Article
  5. TargetingBiology · 2020
    Article
  6. Review
  7. Article
  8. Article
  9. Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Plant-polysaccharide-degrading enzymes from Basidiomycetes.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  18. Article
  19. Article
  20. Article
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

4 authors at 1 institution in 1 country.

Mathieu BeyINRA, UMR1163 BCF, 163 avenue de Luminy, Marseille, France. mathieu.bey@esil.univmed.fr
Jean-Guy Berrin
Laetitia Poidevin
Jean-Claude Sigoillot
Centre d’Immunologie de Marseille-Luminy · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by lignocellulose-degrading fungi including Pycnoporus cinnabarinus. We investigated the cellulolytic system of P. cinnabarinus, focusing on the involvement of CDH in the deconstruction of lignocellulosic biomass.

resultsFirst, P. cinnabarinus growth conditions were optimized for CDH production. Following growth under cellulolytic conditions, the main components secreted were cellulases, xylanases and CDH. To investigate the contribution of P. cinnabarinus secretome in saccharification processes, the Trichoderma reesei enzymatic cocktail was supplemented with the P. cinnabarinus secretome. A significant enhancement of the degradation of wheat straw was observed with (i) the production of a large amount of gluconic acid, (ii) increased hemicellulose degradation, and (iii) increased overall degradation of the lignocellulosic material. P. cinnabarinus CDH was heterologously expressed in Pichia pastoris to obtain large amounts of pure enzyme. In a bioreactor, the recombinant CDH (rCDH) expression level reached 7800 U/L. rCDH exhibited values of biochemical parameters similar to those of the natural enzyme, and was able to bind cellulose despite the absence of a carbohydrate-binding module (CBM). Following supplementation of purified rCDH to T. reesei enzymatic cocktail, formation of gluconic acid and increased hemicellulose degradation were observed, thus confirming the previous results observed with P. cinnabarinus secretome.

conclusionsWe demonstrate that CDH offers an attractive tool for saccharification process enhancement due to gluconic acid production from raw lignocellulosic material.

Indexed as

Carbohydrate DehydrogenasesElectrophoresis, Polyacrylamide GelFungal ProteinsLigninPichiaPycnoporusRecombinant ProteinsCarbohydrate Dehydrogenasescellobiose-quinone oxidoreductaseFungal ProteinsLigninlignocelluloseRecombinant Proteins

Identifiers

PMID22204630
PMCPMC3268779
OpenAlexW2152062896

What OpenQuestion holds

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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.