Evidence map›Paper›PMID 32678825›Full record

ArticlePloS one2020

Cloning and expression of a novel α-galactosidase from Lactobacillus amylolyticus L6 with hydrolytic and transgalactosyl properties.

Yongtao Fei, WenJuan Jiao, Ying Wang, Jinglong Liang, Gongliang Liu, Li Li

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 22% 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, 1 synthesis or guideline pooled it, 13 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Adaptive mechanism ofFood science & nutrition · 2022
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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

6 authors at 3 institutions in 1 country.

Yongtao FeiCollege of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China.
WenJuan JiaoGuangdong Academy of Agricultural Sciences, Sericultural & Agri-Food Research Institute, Guangzhou, China.
Ying WangCollege of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China.
Jinglong LiangCollege of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China.
Gongliang LiuCollege of Light Industry and Food Science, Zhongkai University of Agriculture and Engineering, Guangzhou, China.
Li LiSchool of Food Science and Engineering, South China University of Technology, Guangzhou, China.
Zhongkai University of Agriculture and Engineering · CNGuangdong Academy of Agricultural Sciences · CNSouth China University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactobacillus amylolyticus L6, a gram-positive amylolytic bacterium isolated from naturally fermented tofu whey (NFTW), was able to hydrolyze raffinose and stachyose for the production of α-galactosidase. The cell-free extract of L. amylolyticus L6 was found to exhibit glycosyltransferase activity to synthesize α-galacto-oligosaccharides (GOS) with melibiose as substrate. The coding genes of α-galactosidase were identified in the genome of L. amylolyticus L6. The α-galactosidase (AglB) was placed into GH36 family by amino acid sequence alignments with other α-galactosidases from lactobacilli. The optimal reaction conditions of pH and temperature for AglB were pH 6.0 and 37°C, respectively. Besides, potassium ion was found to improve the activity of AglB while divalent mercury ion, copper ion and zinc ion displayed different degrees of inhibition effect. Under the optimum reaction condition, AglB could catalyze the synthesis of GOS with degree of polymerization (DP) ≥5 by using 300 mM melibiose concentration as substrate. The maximum yield of GOS with (DP) ≥3 could reach 31.56% (w/w). Transgalactosyl properties made AglB a potential candidate for application in the production of GOS.

Indexed as

Cloning, Molecularalpha-GalactosidaseAmino Acid SequenceBacterial ProteinsEnzyme StabilityGlycosylationHydrogen-Ion ConcentrationHydrolysisLactobacillusRecombinant ProteinsSequence AlignmentTemperaturealpha-GalactosidaseBacterial ProteinsRecombinant Proteins

Identifiers

PMID32678825
PMCPMC7367483
OpenAlexW3042942733

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.