Evidence map›Paper›PMID 28511724›Full record

ArticleMicrobial cell factories2017

Production of a recombinant swollenin from Trichoderma harzianum in Escherichia coli and its potential synergistic role in biomass degradation.

Clelton A Santos, Jaire A Ferreira-Filho, Anthonia O'Donovan, Vijai K Gupta, Maria G Tuohy, Anete P Souza

Abstract read
In one paragraph

Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. A Swollenin FromFrontiers in microbiology · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. 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

6 authors.

Clelton A SantosMolecular Glycobiotechnology Group, Department of Biochemistry, National University of Ireland Galway, Galway, Ireland.
Jaire A Ferreira-FilhoCenter for Molecular Biology and Genetic Engineering, University of Campinas, Campinas, SP, Brazil.
Anthonia O'DonovanMolecular Glycobiotechnology Group, Department of Biochemistry, National University of Ireland Galway, Galway, Ireland.
Vijai K GuptaMolecular Glycobiotechnology Group, Department of Biochemistry, National University of Ireland Galway, Galway, Ireland.
Maria G TuohyMolecular Glycobiotechnology Group, Department of Biochemistry, National University of Ireland Galway, Galway, Ireland.
Anete P SouzaCenter for Molecular Biology and Genetic Engineering, University of Campinas, Campinas, SP, Brazil. anete@unicamp.br.ORCID http://orcid.org/0000-0003-3831-9829

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFungal swollenins (SWOs) constitute a class of accessory proteins that are homologous to canonical plant expansins. Expansins and expansin-related proteins are well known for acting in the deagglomeration of cellulose structure by loosening macrofibrils. Consequently, SWOs can increase the accessibility and efficiency of the other enzymes involved in the saccharification of cellulosic substrates. Thus, SWOs are promising targets for improving the hydrolysis of plant biomass and for use as an additive to enhance the efficiency of an enzyme cocktail designed for the production of biofuels.

resultsHere, we report the initial characterization of an SWO from Trichoderma harzianum (ThSwo) that was successfully produced using Escherichia coli as a host. Initially, transcriptome and secretome data were used to compare swo gene expression and the amount of secreted ThSwo. The results from structural modeling and phylogenetic analysis of the ThSwo protein showed that ThSwo does preserve some structural features of the plant expansins and family-45 glycosyl hydrolase enzymes, but it evolutionarily diverges from both of these protein classes. Recombinant ThSwo was purified at a high yield and with high purity and showed secondary folding similar to that of a native fungal SWO. Bioactivity assays revealed that the purified recombinant ThSwo created a rough and amorphous surface on Avicel and displayed a high synergistic effect with a commercial xylanase from T. viride, enhancing its hydrolytic performance up to 147 ± 7%.

conclusionsMany aspects of the structure and mechanism of action of fungal SWOs remain unknown. In the present study, we produced a recombinant, active SWO from T. harzianum using a prokaryotic host and confirmed its potential synergistic role in biomass degradation. Our work paves the way for further studies evaluating the structure and function of this protein, especially regarding its use in biotechnology.

Indexed as

BiofuelsBiomassBiotechnologyCelluloseEscherichia coliFungal ProteinsHydrolysisPhylogenyTrichodermaBiofuelsCelluloseFungal ProteinsBiomass degradationExpansinOverexpressionSwolleninTrichoderma harzianum

Identifiers

PMID28511724
PMCPMC5432999

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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.