Evidence map›Paper›PMID 32332833›Full record

ArticleScientific reports2020

A Highly Glucose Tolerant ß-Glucosidase from Malbranchea pulchella (MpBg3) Enables Cellulose Saccharification.

Lummy Maria Oliveira Monteiro, Ana Claudia Vici, Matheus Pinto Pinheiro, Paulo Ricardo Heinen, Arthur Henrique Cavalcante de Oliveira, Richard John Ward, Rolf Alexander Prade, Marcos S Buckeridge, Maria de Lourdes Teixeira de Moraes Polizeli

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Biochemical andHeliyon · 2024
    Article
  7. Article
  8. Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023
    Article
  9. Controlling the Adsorption of β-Glucosidase onto Wrinkled SiOLangmuir : the ACS journal of surfaces and colloids · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. TheFrontiers in microbiology · 2022
    Article
  15. IncreasedBiotechnology reports (Amsterdam, Netherlands) · 2021
    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

9 authors at 4 institutions in 2 countries.

Lummy Maria Oliveira MonteiroFaculdade de Medicina de Ribeirão Preto. Universidade de São Paulo. Bandeirantes Av., 3.900, 14049-900, Ribeirão Preto, SP, Brazil.
Ana Claudia ViciFaculdade de Filosofia, Ciências e Letras de Ribeirão Preto. Universidade de São Paulo. Bandeirantes Av., 3.900, 14040-901, Ribeirão Preto, SP, Brazil.
Matheus Pinto PinheiroLaboratório Nacional de Biociência (LNBio), Centro Nacional de Pesquisa em Energia e Materiais (CNPEM), Campinas, SP, Brazil.
Paulo Ricardo HeinenFaculdade de Medicina de Ribeirão Preto. Universidade de São Paulo. Bandeirantes Av., 3.900, 14049-900, Ribeirão Preto, SP, Brazil.
Arthur Henrique Cavalcante de OliveiraFaculdade de Filosofia, Ciências e Letras de Ribeirão Preto. Universidade de São Paulo. Bandeirantes Av., 3.900, 14040-901, Ribeirão Preto, SP, Brazil.
Richard John WardFaculdade de Filosofia, Ciências e Letras de Ribeirão Preto. Universidade de São Paulo. Bandeirantes Av., 3.900, 14040-901, Ribeirão Preto, SP, Brazil.
Rolf Alexander PradeDepartment of Microbiology and Molecular Genetics. Oklahoma State University, Stillwater, USA.
Marcos S BuckeridgeInstituto de Biociências, Universidade de São Paulo. Matão Street, 277, 05508-090, São Paulo, SP, Brazil.
Maria de Lourdes Teixeira de Moraes PolizeliFaculdade de Medicina de Ribeirão Preto. Universidade de São Paulo. Bandeirantes Av., 3.900, 14049-900, Ribeirão Preto, SP, Brazil. polizeli@ffclrp.usp.br.ORCID http://orcid.org/0000-0002-5026-6363
Universidade de Ribeirão Preto · BRLaboratório Nacional de Ciência e Tecnologia do Bioetanol · BROklahoma State University · USUniversidade de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-glucosidases catalyze the hydrolysis β-1,4, β-1,3 and β-1,6 glucosidic linkages from non-reducing end of short chain oligosaccharides, alkyl and aryl β-D-glucosides and disaccharides. They catalyze the rate-limiting reaction in the conversion of cellobiose to glucose in the saccharification of cellulose for second-generation ethanol production, and due to this important role the search for glucose tolerant enzymes is of biochemical and biotechnological importance. In this study we characterize a family 3 glycosyl hydrolase (GH3) β-glucosidase (Bgl) produced by Malbranchea pulchella (MpBgl3) grown on cellobiose as the sole carbon source. Kinetic characterization revealed that the MpBgl3 was highly tolerant to glucose, which is in contrast to many Bgls that are completely inhibited by glucose. A 3D model of MpBgl3 was generated by molecular modeling and used for the evaluation of structural differences with a Bgl3 that is inhibited by glucose. Taken together, our results provide new clues to understand the glucose tolerance in GH3 β-glucosidases.

Indexed as

beta-GlucosidaseCarbonCellobioseCelluloseGlucoseHydrolysisOnygenalesbeta-GlucosidaseCarbonCellobioseCelluloseGlucose

Identifiers

PMID32332833
PMCPMC7181827
OpenAlexW3019214208

What OpenQuestion holds

Textmetadata
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.