Evidence map›Paper›PMID 27621442›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome.

Lital Davidi, Sarah Moraïs, Lior Artzi, Doriv Knop, Yitzhak Hadar, Yonathan Arfi, Edward A Bayer

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
19.9field-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

33 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. 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. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Carbohydrate Depolymerization by Intricate Cellulosomal Systems.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Evaluating Enzymatic Productivity-The Missing Link to Enzyme Utility.International journal of molecular sciences · 2022
    Review
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  15. Article
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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

7 authors at 2 institutions in 1 country.

Lital DavidiDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel;
Sarah MoraïsDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel;
Lior ArtziDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel;
Doriv KnopFaculty of Agricultural, Food, and Environmental Quality Sciences, The Hebrew University of Jerusalem, Rehovot 76100, Israel.
Yitzhak HadarFaculty of Agricultural, Food, and Environmental Quality Sciences, The Hebrew University of Jerusalem, Rehovot 76100, Israel.
Yonathan ArfiDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel;
Edward A BayerDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel; ed.bayer@weizmann.ac.il.
Weizmann Institute of Science · ILHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficient breakdown of lignocellulose polymers into simple molecules is a key technological bottleneck limiting the production of plant-derived biofuels and chemicals. In nature, plant biomass degradation is achieved by the action of a wide range of microbial enzymes. In aerobic microorganisms, these enzymes are secreted as discrete elements in contrast to certain anaerobic bacteria, where they are assembled into large multienzyme complexes termed cellulosomes. These complexes allow for very efficient hydrolysis of cellulose and hemicellulose due to the spatial proximity of synergistically acting enzymes and to the limited diffusion of the enzymes and their products. Recently, designer cellulosomes have been developed to incorporate foreign enzymatic activities in cellulosomes so as to enhance lignocellulose hydrolysis further. In this study, we complemented a cellulosome active on cellulose and hemicellulose by addition of an enzyme active on lignin. To do so, we designed a dockerin-fused variant of a recently characterized laccase from the aerobic bacterium Thermobifida fusca The resultant chimera exhibited activity levels similar to the wild-type enzyme and properly integrated into the designer cellulosome. The resulting complex yielded a twofold increase in the amount of reducing sugars released from wheat straw compared with the same system lacking the laccase. The unorthodox use of aerobic enzymes in designer cellulosome machinery effects simultaneous degradation of the three major components of the plant cell wall (cellulose, hemicellulose, and lignin), paving the way for more efficient lignocellulose conversion into soluble sugars en route to alternative fuels production.

Indexed as

Carbohydrate MetabolismCell Cycle ProteinsCelluloseCellulosomesChromosomal Proteins, Non-HistoneCohesinsHydrolysisKineticsLaccaseLigninProtein BindingRecombinant ProteinsSubstrate SpecificityTriticumCell Cycle ProteinsCelluloseChromosomal Proteins, Non-HistoneCohesinsLaccaseLigninRecombinant Proteinsbiomass conversioncatalysislignocellulosemultienzyme complex

Identifiers

PMID27621442
PMCPMC5047212
OpenAlexW2519286380

What OpenQuestion holds

Textmetadata
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.