Evidence map›Paper›PMID 18568289›Full record

ArticleExtremophiles : life under extreme conditions2008

Evidence that the xylanase activity from Sulfolobus solfataricus Oalpha is encoded by the endoglucanase precursor gene (sso1354) and characterization of the associated cellulase activity.

Luisa Maurelli, Alfonso Giovane, Alessandra Esposito, Marco Moracci, Immacolata Fiume, Mosè Rossi, Alessandra Morana

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Article in Extremophiles : life under extreme conditions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  5. Engineering ofJournal of microbiology and biotechnology · 2022
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  10. Multifunctional enzymes in archaea: promiscuity and moonlight.Extremophiles : life under extreme conditions · 2013
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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

7 authors at 3 institutions in 1 country.

Luisa MaurelliIstituto di Biochimica delle Proteine, Consiglio Nazionale delle Ricerche, via Pietro Castellino 111, 80131 Naples, Italy.
Alfonso Giovane
Alessandra Esposito
Marco Moracci
Immacolata Fiume
Mosè Rossi
Alessandra Morana
National Research Council · ITInstitute of Protein Biochemistry · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sulfolobus solfataricus strain Oalpha was previously isolated for its ability to grow on minimal medium supplemented with xylan as a carbon source. The strain exhibited thermostable xylanase activity but several attempts to identify the gene encoding for the activity failed. Further studies showed that the xylanase displayed activity on carboxymethylcellulose (CMC) and the new activity was characterized. It exhibited an optimal temperature and pH of 95 degrees C and 3.5, respectively, and a half-life of 53 min at 95 degrees C. The enzyme, which was demonstrated to be glycosylated, hydrolyzed CMC in an endo-manner releasing cellobiose and other cello-oligomers. Analysis of the tryptic fragments by tandem mass spectrometry led to identification of the endoglucanase precursor, encoded by the sso1354 gene, as the protein possessing dual activity. The efficiency of the SSO1354 protein in degrading cellulosic and hemicellulosic fractions contained in agronomic residues was tested at low pH and high temperature. Cellulose and xylan were degraded to glucose and xylose at 90 degrees C, pH 4 by an enzyme mix consisting of SSO1354 and additional glycosyl hydrolases from S. solfataricus Oalpha. Given its role in saccharification processes requiring high temperatures and acidic environments, SSO1354 represents an interesting candidate for the utilization of agro-industrial waste for fuel production.

Indexed as

Amino Acid SequenceArchaeal ProteinsCarboxymethylcellulose SodiumCellulaseChromatography, GelConserved SequenceEndo-1,4-beta XylanasesKineticsMass SpectrometryMembrane ProteinsMolecular Sequence DataPeptide FragmentsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificitySulfolobus solfataricusArchaeal ProteinsCarboxymethylcellulose SodiumCellulaseEndo-1,4-beta XylanasesMembrane ProteinsPeptide Fragments

Identifiers

PMID18568289
OpenAlexW2044535803

What OpenQuestion holds

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Registered trials

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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.