Evidence map›Paper›PMID 22283494›Full record

ArticleJournal of agricultural and food chemistry2012

Homodimeric β-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus DSM 20081: expression in Lactobacillus plantarum and biochemical characterization.

Tien-Thanh Nguyen, Hoang Anh Nguyen, Sheryl Lozel Arreola, Georg Mlynek, Kristina Djinović-Carugo, Geir Mathiesen, Thu-Ha Nguyen, Dietmar Haltrich

Open access · greenAbstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

27 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Characterization of a β-Galactosidase fromMolecules (Basel, Switzerland) · 2025
    Article
  3. Review
  4. Article
  5. Galacto-oligosaccharide production byJDS communications · 2024
    Article
  6. Article
  7. Article
  8. β-galactosidase GALA fromBioengineered · 2021
    Article
  9. Article
  10. Review
  11. Immobilization of β-Galactosidases on theCatalysts (Basel, Switzerland) · 2019
    Article
  12. β-Galactosidase fromInternational journal of molecular sciences · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

8 authors at 6 institutions in 5 countries.

Tien-Thanh NguyenSchool of Biotechnology and Food Technology, Hanoi University of Science and Technology, Hanoi, Vietnam.
Hoang Anh Nguyen
Sheryl Lozel Arreola
Georg Mlynek
Kristina Djinović-Carugo
Geir Mathiesen
Thu-Ha Nguyen
Dietmar Haltrich
BOKU University · ATHanoi University of Science and Technology · VNMax Perutz Labs · ATNorwegian University of Life Sciences · NOUniversity of Ljubljana · SIUniversity of the Philippines Los Baños · PH

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

The lacZ gene from Lactobacillus delbrueckii subsp. bulgaricus DSM 20081, encoding a β-galactosidase of the glycoside hydrolase family GH2, was cloned into different inducible lactobacillal expression vectors for overexpression in the host strain Lactobacillus plantarum WCFS1. High expression levels were obtained in laboratory cultivations with yields of approximately 53000 U of β-galactosidase activity per liter of medium, which corresponds to ~170 mg of recombinant protein per liter and β-galactosidase levels amounting to 63% of the total intracellular protein of the host organism. The wild-type (nontagged) and histidine-tagged recombinant enzymes were purified to electrophoretic homogeneity and further characterized. β-Galactosidase from L. bulgaricus was used for lactose conversion and showed very high transgalactosylation activity. The maximum yield of galacto-oligosaccharides (GalOS) was approximately 50% when using an initial concentration of 600 mM lactose, indicating that the enzyme can be of interest for the production of GalOS.

Indexed as

Gene Expressionbeta-GalactosidaseCloning, MolecularDNA, BacterialGalactoseGenetic VectorsLactiplantibacillus plantarumLactobacillus delbrueckiiLactoseProtein MultimerizationRecombinant Proteinsbeta-GalactosidaseDNA, BacterialGalactoseLactoseRecombinant Proteins

Identifiers

PMID22283494
PMCPMC3284191
OpenAlexW2093280917

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.