Evidence map›Paper›PMID 38354215›Full record

ArticleJournal of agricultural and food chemistry2024

Thermostability Enhancement of GH 62 α-l-Arabinofuranosidase by Directed Evolution and Rational Design.

Manoela Martins, Alberto M Dos Santos, Clauber H S da Costa, Samuel W Canner, Michael Chungyoun, Jeffrey J Gray, Munir S Skaf, Marc Ostermeier, Rosana Goldbeck

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of agricultural and food chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

1 citing paper in PubMed, 10 citations in OpenAlex.

  1. 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 2 institutions in 2 countries.

Manoela MartinsDepartment of Chemical & Biomolecular Engineering, Johns Hopkins University, 3400 N Charles Street, Baltimore, Maryland 21218, United States.ORCID 0000-0002-2679-4721
Alberto M Dos SantosDepartment of Chemistry, State University of Campinas, 336, R. Josué de Castro, 126-Cidade Universitária, Campinas, São Paulo 13083-861, Brazil.
Clauber H S da CostaDepartment of Chemistry, State University of Campinas, 336, R. Josué de Castro, 126-Cidade Universitária, Campinas, São Paulo 13083-861, Brazil.
Samuel W CannerDepartment of Chemical & Biomolecular Engineering, Johns Hopkins University, 3400 N Charles Street, Baltimore, Maryland 21218, United States.ORCID 0000-0002-8678-0639
Michael ChungyounDepartment of Chemical & Biomolecular Engineering, Johns Hopkins University, 3400 N Charles Street, Baltimore, Maryland 21218, United States.
Jeffrey J GrayDepartment of Chemical & Biomolecular Engineering, Johns Hopkins University, 3400 N Charles Street, Baltimore, Maryland 21218, United States.ORCID 0000-0001-6380-2324
Munir S SkafDepartment of Chemistry, State University of Campinas, 336, R. Josué de Castro, 126-Cidade Universitária, Campinas, São Paulo 13083-861, Brazil.ORCID 0000-0001-7485-1228
Marc OstermeierDepartment of Chemical & Biomolecular Engineering, Johns Hopkins University, 3400 N Charles Street, Baltimore, Maryland 21218, United States.ORCID 0000-0003-0900-3665
Rosana GoldbeckDepartment of Food Engineering, State University of Campinas, Monteiro Lobato, 80, Cidade Universitária, Campinas, São Paulo 13083-862, Brazil.ORCID 0000-0003-2953-8050
Johns Hopkins University · USUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

Prediction of the Structures of Protein ComplexesR35GM141881 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JEFFREY J GRAY · 2021 to 2026
$7.6M
Program of Molecular BiophysicsT32GM135131 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Karen G. Fleming · 2020 to 2026
$5.4M
NIGMS NIH HHS R35 GM141881NIGMS NIH HHS T32 GM135131
6 · The paper itself

Abstract

GH 62 arabinofuranosidases are known for their excellent specificity for arabinoxylan of agroindustrial residues and their synergism with endoxylanases and other hemicellulases. However, the low thermostability of some GH enzymes hampers potential industrial applications. Protein engineering research highly desires mutations that can enhance thermostability. Therefore, we employed directed evolution using one round of error-prone PCR and site-saturation mutagenesis for thermostability enhancement of GH 62 arabinofuranosidase from

Indexed as

Glycoside HydrolasesProtein EngineeringEnzyme StabilityMutagenesisTemperaturealpha-N-arabinofuranosidaseGlycoside Hydrolasesarabinoxylanerror-prone PCRprotein evolutionsite-directed mutagenesis

Identifiers

PMID38354215
PMCPMC11995439
OpenAlexW4391806995

What OpenQuestion holds

Textmetadata
LicenceTDM
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.