Evidence map›Paper›PMID 29738566›Full record

ArticlePloS one2018

A novel α-galactosidase from the thermophilic probiotic Bacillus coagulans with remarkable protease-resistance and high hydrolytic activity.

Ruili Zhao, Rui Zhao, Yishuai Tu, Xiaoming Zhang, Liping Deng, Xiangdong Chen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. 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
4.2field-weighted citation impact, top 6% 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, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Molecular advances in microbial α-galactosidases: challenges and prospects.World journal of microbiology & biotechnology · 2022
    Review
  8. Review
  9. Review
  10. Article
  11. Application ofAnimals : an open access journal from MDPI · 2020
    Review
  12. Article
  13. Article
  14. Review
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

6 authors at 2 institutions in 1 country.

Ruili ZhaoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, P. R. China.
Rui ZhaoState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, P. R. China.
Yishuai TuState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, P. R. China.
Xiaoming ZhangState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, P. R. China.
Liping DengState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, P. R. China.
Xiangdong ChenState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, P. R. China.ORCID 0000-0002-3475-3436
Wuhan University · CNChina Tourism Academy · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel α-galactosidase of glycoside hydrolase family 36 was cloned from Bacillus coagulans, overexpressed in Escherichia coli, and characterized. The purified enzyme Aga-BC7050 was 85 kDa according to SDS-PAGE and 168 kDa according to gel filtration, indicating that its native structure is a dimer. With p-nitrophenyl-α-d- galactopyranoside (pNPGal) as the substrate, optimal temperature and pH were 55 °C and 6.0, respectively. At 60 °C for 30 min, it retained > 50% of its activity. It was stable at pH 5.0-10.0, and showed remarkable resistance to proteinase K, subtilisin A, α-chymotrypsin, and trypsin. Its activity was not inhibited by glucose, sucrose, xylose, or fructose, but was slightly inhibited at galactose concentrations up to 100 mM. Aga-BC7050 was highly active toward pNPGal, melibiose, raffinose, and stachyose. It completely hydrolyzed melibiose, raffinose, and stachyose in < 30 min. These characteristics suggest that Aga-BC7050 could be used in feed and food industries and sugar processing.

Indexed as

alpha-GalactosidaseBacillus coagulansEnzyme StabilityHydrolysisNitrophenylgalactosidesPeptide HydrolasesProbioticsSubstrate Specificity4-nitrophenylgalactosidealpha-GalactosidaseNitrophenylgalactosidesPeptide Hydrolases

Identifiers

PMID29738566
PMCPMC5940202
OpenAlexW2800204380

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.