Evidence map›Paper›PMID 24141566›Full record

ArticleThe protein journal2013

Characterization of a cold-active β-glucosidase from Paenibacillus xylanilyticus KJ-03 capable of hydrolyzing isoflavones daidzin and genistin.

Dong-Ju Park, Yong-Suk Lee, Yong-Lark Choi

Abstract read
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Article in The protein journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

9 citing papers in PubMed, 18 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

3 authors at 1 institution in 1 country.

Dong-Ju ParkDepartment of Biotechnology, College of Natural Resources and Life Science, Dong-A University, Busan, 604-714, South Korea.
Yong-Suk Lee
Yong-Lark Choi
Dong-A University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Paenibacillus xylanilyticus KJ-03 isolated from konjac field, showed β-glucosidase activity on tryptic soy agar plate supplemented with 0.1 % esculin and 0.25 % ferric ammonium citrate. A genome library was constructed to obtain the β-glucosidase gene and a recombinant clone, pGlc2-3 was selected. The 2,247 bp gene encoding KJ-03 β-glucosidase consisted of 749 amino acids. The deduced amino acids of BglA were 61 % homologous with that of the β-glucosidase from Bacillus cereus AH1272, which belongs to the glycoside hydrolase family 3. His-tagged β-glucosidase was purified by using His-Trap column and characterized. KJ-03 β-glucosidase was showed as a single band with about 82 kDa on SDS-PAGE. The purified enzyme has optimal activity at 20 °C and pH 7.0 using p-NPβG and 72 % of the maximal activity was still remaining at 10 °C. The β-glucosidase has optimal activity at low temperatures indicating that it is a cold-active enzyme. The substrate specificity showed that the purified enzyme hydrolyzed aryl β-glucoside substrates and isoflavones such as daidzin and genistin.

Indexed as

Amino Acid SequenceBacterial Proteinsbeta-GlucosidaseEnzyme StabilityIsoflavonesKineticsMolecular Sequence DataPaenibacillusRecombinant ProteinsSequence AlignmentSubstrate SpecificityBacterial Proteinsbeta-GlucosidasedaidzingenistinIsoflavonesRecombinant Proteins

Identifiers

PMID24141566
OpenAlexW2074857733

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.