Evidence map›Paper›PMID 20549295›Full record

ArticleJournal of industrial microbiology & biotechnology2010

Purification and characterization studies of a thermostable β-xylanase from Aspergillus awamori.

Ricardo Sposina Sobral Teixeira, Félix Gonçalves Siqueira, Marcelo Valle de Souza, Edivaldo Ximenes Ferreira Filho, Elba Pinto da Silva Bon

Open access · bronzeAbstract read
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In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

14 citing papers in PubMed, 53 citations in OpenAlex.

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  5. Frontiers in microbiology · 2020
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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

5 authors at 2 institutions in 1 country.

Ricardo Sposina Sobral TeixeiraLaboratory of Enzyme Technology, Biochemistry Department, Chemistry Institute, Federal University of Rio de Janeiro, Av. Athos da Silveira Ramos 149, Bloco A, Ilha do Fundão, CEP 21941-909, Rio de Janeiro, RJ, Brazil.
Félix Gonçalves Siqueira
Marcelo Valle de Souza
Edivaldo Ximenes Ferreira Filho
Elba Pinto da Silva Bon
Universidade de Brasília · BRUniversidade Federal do Rio de Janeiro · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study presents data on the production, purification, and properties of a thermostable β-xylanase produced by an Aspergillus awamori 2B.361 U2/1 submerged culture using wheat bran as carbon source. Fractionation of the culture filtrate by membrane ultrafiltration followed by Sephacryl S-200 and Q-Sepharose chromatography allowed for the isolation of a homogeneous xylanase (PXII-1), which was 32.87 kDa according to MS analysis. The enzyme-specific activity towards soluble oat spelt xylan, which was found to be 490 IU/mg under optimum reaction conditions (50°C and pH 5.0-5.5), was 17-fold higher than that measured in the culture supernatant. Xylan reaction products were identified as xylobiose, xylotriose, and xylotetraose. K (m) values (mg ml(-1)) for soluble oat spelt and birchwood xylan were 11.8 and 9.45, respectively. Although PXII-1 showed 85% activity retention upon incubation at 50 °C and pH 5.0 for 20 days, incubation at pH 7.0 resulted in 50% activity loss within 3 days. PXII-1 stability at pH 7.0 was improved in the presence of 20 mM cysteine, which allowed for 85% activity retention for 25 days. This study on the production in high yields of a remarkably thermostable xylanase is of significance due to the central role that this class of biocatalyst shares, along with cellulases, for the much needed enzymatic hydrolysis of biomass. Furthermore, stable xylanases are important for the manufacture of paper, animal feed, and xylooligosaccharides.

Indexed as

AnimalsAspergillusChromatography, GelChromatography, Ion ExchangeCysteineDietary FiberEndo-1,4-beta XylanasesEnzyme ActivatorsEnzyme StabilityHot TemperatureHydrogen-Ion ConcentrationMass SpectrometryMolecular WeightSubstrate SpecificityTime FactorsUltrafiltrationCysteineDietary FiberEndo-1,4-beta XylanasesEnzyme ActivatorsXylans

Identifiers

PMID20549295
OpenAlexW2064118575

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.