Evidence map›Paper›PMID 24037406›Full record

ArticleApplied microbiology and biotechnology2014

Recombinant Aspergillus β-galactosidases as a robust glycomic and biotechnological tool.

Martin Dragosits, Stefan Pflügl, Simone Kurz, Ebrahim Razzazi-Fazeli, Iain B H Wilson, Dubravko Rendic

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2014. 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
4.2field-weighted citation impact, top 7% 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, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Analysis of Caenorhabditis Protein Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Article
  6. Article
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  9. Review
  10. Article
  11. Sulfated and sialylatedThe Journal of biological chemistry · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Systematic assessment ofSynthetic and systems biotechnology · 2017
    Article
  16. Article
  17. Article
  18. Analysis of Invertebrate and Protist N-Glycans.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  19. Review
  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

6 authors at 2 institutions in 1 country.

Martin DragositsDepartment of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, Vienna, 1190, Austria.
Stefan Pflügl
Simone Kurz
Ebrahim Razzazi-Fazeli
Iain B H Wilson
Dubravko Rendic
BOKU University · ATUniversity of Veterinary Medicine Vienna · AT

Funding

Austrian Science Fund FWF TRP 127Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Galactosidases are widespread enzymes that are used for manifold applications, including production of prebiotics, biosynthesis of different transgalactosylated products, improving lactose tolerance and in various analytical approaches. The nature of these applications often require galactosidases to be present in a purified form with clearly defined properties, including precisely determined substrate specificities, low sensitivity to inhibitors, and high efficiency and stability under distinct conditions. In this study, we present the recombinant expression and purification of two previously uncharacterized β-galactosidases from Aspergillus nidulans as well as one β-galactosidase from Aspergillus niger. All enzymes were active toward p-nitrophenyl-β-D-galactopyranoside as substrate and displayed similar temperature and pH optima. The purified recombinant galactosidases digested various complex substrates containing terminal galactose β-1,4 linked to either N-acetylglucosamine or fucose, such as N-glycans derived from bovine fibrin and Caenorhabditis elegans. In our comparative study of the recombinant galactosidases with the commercially available galactosidase from Aspergillus oryzae, all enzymes also displayed various degrees of activity toward complex oligosaccharides containing β-1,3-linked terminal galactose residues. All recombinant enzymes were found to be robust in the presence of various organic solvents, temperature variations, and freeze/thaw cycles and were also tested for their ability to synthesize galactooligosaccharides. Furthermore, the use of fermentors considerably increased the yield of recombinant galactosidases. Taken together, we demonstrate that purified recombinant galactosidases from A. niger and from A. nidulans are suitable for various glycobiological and biotechnological applications.

Indexed as

Aspergillus nidulansAspergillus nigerbeta-GalactosidaseBiotechnologyGlycomicsHydrogen-Ion ConcentrationKineticsRecombinant ProteinsSubstrate SpecificityTemperaturebeta-GalactosidaseRecombinant Proteins

Identifiers

PMID24037406
PMCPMC3973953
OpenAlexW2110122344

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.