Evidence map›Paper›PMID 27759119›Full record

ArticleScientific reports2016

Enzymatic diversity of the Clostridium thermocellum cellulosome is crucial for the degradation of crystalline cellulose and plant biomass.

Katsuaki Hirano, Masahiro Kurosaki, Satoshi Nihei, Hiroki Hasegawa, Suguru Shinoda, Mitsuru Haruki, Nobutaka Hirano

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Deconstruction byLife science alliance · 2026
    Article
  3. Creating a large designer cellulosome in yeast to boost ethanol production.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. ThermophilicFrontiers in microbiology · 2022
    Article
  11. Article
  12. Article
  13. Constructing a yeast to express the largest cellulosome complex on the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. 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

7 authors at 1 institution in 1 country.

Katsuaki HiranoDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Masahiro KurosakiDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Satoshi NiheiDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Hiroki HasegawaDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Suguru ShinodaDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Mitsuru HarukiDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Nobutaka HiranoDepartment of Chemical Biology &Applied Chemistry, College of Engineering, Nihon University, Koriyama, Fukushima 963-8642, Japan.
Nihon University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cellulosome is a supramolecular multienzyme complex comprised of a wide variety of polysaccharide-degrading enzymes and scaffold proteins. The cellulosomal enzymes that bind to the scaffold proteins synergistically degrade crystalline cellulose. Here, we report in vitro reconstitution of the Clostridium thermocellum cellulosome from 40 cellulosomal components and the full-length scaffoldin protein that binds to nine enzyme molecules. These components were each synthesized using a wheat germ cell-free protein synthesis system and purified. Cellulosome complexes were reconstituted from 3, 12, 30, and 40 components based on their contents in the native cellulosome. The activity of the enzyme-saturated complex indicated that greater enzymatic variety generated more synergy for the degradation of crystalline cellulose and delignified rice straw. Surprisingly, a less complete enzyme complex displaying fewer than nine enzyme molecules was more efficient for the degradation of delignified rice straw than the enzyme-saturated complex, despite the fact that the enzyme-saturated complex exhibited maximum synergy for the degradation of crystalline cellulose. These results suggest that greater enzymatic diversity of the cellulosome is crucial for the degradation of crystalline cellulose and plant biomass, and that efficient degradation of different substrates by the cellulosome requires not only a different enzymatic composition, but also different cellulosome structures.

Indexed as

Acetivibrio thermocellusBacterial ProteinsBiomassBiotransformationCarrier ProteinsCellulaseCellulasesCelluloseMultienzyme ComplexesOryzaPlant StemsTriticumBacterial ProteinsCarrier ProteinsCellulaseCellulasesCellulosecellulose binding protein A, Clostridium cellulovoranscellulosome, ClostridiumMultienzyme Complexes

Identifiers

PMID27759119
PMCPMC5069625
OpenAlexW2536143430

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.