Evidence map›Paper›PMID 27714589›Full record

ArticleMolecular biotechnology2016

Expression of Two Novel β-Glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and Characterization of the Heterologous Protein Products.

Ana C Colabardini, Mari Valkonen, Anne Huuskonen, Matti Siika-Aho, Anu Koivula, Gustavo H Goldman, Markku Saloheimo

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. MIST: a Multilocus Identification System forApplied and environmental microbiology · 2020
    Article
  6. Article
  7. Article
  8. Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  9. Review
  10. Review
  11. Article
  12. 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 2 institutions in 2 countries.

Ana C ColabardiniVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044, Espoo, Finland. annnacrrristina@gmail.com.
Mari ValkonenVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044, Espoo, Finland.
Anne HuuskonenVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044, Espoo, Finland.
Matti Siika-AhoVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044, Espoo, Finland.
Anu KoivulaVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044, Espoo, Finland.
Gustavo H GoldmanDepartamento de Ciências Farmacêuticas, Faculdade de Ciências Farmacêuticas de Ribeirão Prêto, Universidade de São Paulo, Ribeirão Prêto, São Paulo, Brazil.
Markku SaloheimoVTT Technical Research Centre of Finland Ltd, P.O. Box 1000, 02044, Espoo, Finland.
VTT Technical Research Centre of Finland · FIUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two novel GH3 family thermostable β-glucosidases from the filamentous fungus Chaetomium atrobrunneum (CEL3a and CEL3b) were expressed in Trichoderma reesei, purified by two-step ion exchange chromatography, and characterized. Both enzymes were active over a wide range of pH as compared to Neurospora crassa β-glucosidase GH3-3, which was also expressed in T. reesei and purified. The optimum temperature of both C. atrobrunneum enzymes was around 60 °C at pH 5, and both enzymes had better thermal and pH stability and higher resistance to metallic compounds and to glucose inhibition than GH3-3. They also showed higher activity against oligosaccharides composed of glucose units and linked with β-1,4-glycosidic bonds and moreover, had higher affinity for cellotriose over cellobiose. In hydrolysis tests against Avicel cellulose and steam-exploded sugarcane bagasse, performed at 45 °C, particularly the CEL3a enzyme performed similarly to N. crassa GH3-3 β-glucosidase. Taking into account the thermal stability of the C. atrobrunneum β-glucosidases, they both represent promising alternatives as enzyme mixture components for improved cellulose saccharification at elevated temperatures.

Indexed as

beta-GlucosidaseChaetomiumCloning, MolecularEnzyme StabilityFungal ProteinsHydrogen-Ion ConcentrationHydrolysisLigninTemperatureTrichodermabeta-GlucosidaseFungal ProteinsLigninlignocelluloseBioethanolChaetomium atrobrunneumHydrolysisThermostabilityβ-glucosidase

Identifiers

PMID27714589
OpenAlexW2527925983

What OpenQuestion holds

Textmetadata
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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.