Evidence map›Paper›PMID 16086105›Full record

ArticleCurrent microbiology2005

Construction, expression, and characterization of a thermostable xylanase.

Xiao-Yan Weng, Jian-Yi Sun

Abstract read
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In one paragraph

Article in Current microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Xiao-Yan WengDepartment of Biological Science, College of Life Science, Zhejiang University, Hangzhou, 310029, PR China.
Jian-Yi Sun
Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A hybrid gene, btx, encoding a thermostable xylanase, Btx, was constructed by substituting the 31 N-terminal amino acid residues of the Thermomonospora fusca xylanase A (TfxA) for the corresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A (BsxA). The btx gene was expressed in Escherichia coli BL21. The halo size produced by xylanase Btx on a Remanzol brilliant blue R (RBB) xylan plate at 60 degrees C and pH 6.0 was larger than those of BsxA and TfxA. The molecular weight of Btx was 22 kDa. Temperature and pH optima for Btx were at 50-60 degrees C and 6.0, respectively. Btx showed activity over 80% over a pH range of 5.0-9.0, which was wider than that of BsxA, and was also more acid-resistant than TfxA. Btx exhibited significant thermostability compared with BsxA. The results show the importance of the N-terminal sequence of TfxA in thermostability.

Indexed as

ActinomycetalesAmino Acid SequenceBacillus subtilisEndo-1,4-beta XylanasesEscherichia coliGene ExpressionGenes, BacterialHybridization, GeneticHydrogen-Ion ConcentrationMolecular Sequence DataMolecular WeightRecombinant ProteinsSequence AlignmentTemperatureXylansEndo-1,4-beta XylanasesRecombinant ProteinsXylans

Identifiers

PMID16086105
OpenAlexW2074987689

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.