Evidence map›Paper›PMID 17006740›Full record

ArticleExtremophiles : life under extreme conditions2007

Fusion of carbohydrate binding modules from Thermotoga neapolitana with a family 10 xylanase from Bacillus halodurans S7.

Gashaw Mamo, Rajni Hatti-Kaul, Bo Mattiasson

Abstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2007. 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
1.4field-weighted citation impact, top 19% 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, 54 citations in OpenAlex.

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  3. Molecular Basis of Broad SpectrumACS central science · 2019
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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

3 authors at 1 institution in 1 country.

Gashaw MamoDepartment of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, 22100, Lund, Sweden. gashaw.mamo@biotek.lu.se
Rajni Hatti-Kaul
Bo Mattiasson
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xylanase A of Thermotoga neapolitana contains binding domains both at the N- and C-terminal ends of the catalytic domain. In the N-terminal position it contains two carbohydrate-binding modules (CBM) which belong to family 22. These CBMs bind xylan but not to cellulose. The gene encoding the mature peptide of these CBMs was fused with an alkaline active GH10 xylanase from Bacillus halodurans S7 and expressed in Escherichia coli. The (His)(6) tagged hybrid protein was purified by immobilized metal affinity chromatography and characterized. Xylan binding by the chimeric protein was influenced by NaCl concentration and pH of the binding medium. Binding increased with increasing salt concentration up to 200 mM. Higher extent of binding was observed under acidic conditions. The fusion of the CBM structures enhanced the hydrolytic efficiency of the xylanase against insoluble xylan, but decreased the stability of the enzyme. The optimum temperature and pH for the activity of the xylanase did not change.

Indexed as

Amino Acid SequenceBacillusBacterial ProteinsBinding SitesCatalytic DomainChromatography, AffinityCloning, MolecularEndo-1,4-beta XylanasesEnzyme StabilityHydrogen-Ion ConcentrationHydrolysisKineticsMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsSodium ChlorideBacterial ProteinsEndo-1,4-beta XylanasesRecombinant Fusion ProteinsSodium ChlorideXylans

Identifiers

PMID17006740
OpenAlexW1996249514

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.