Evidence map›Paper›PMID 31792892›Full record

ArticleGlycoconjugate journal2020

Production and characterization of Aspergillus niger GH29 family α-fucosidase and production of a novel non-reducing 1-fucosyllactose.

Anne Usvalampi, Marcela Ruvalcaba Medrano, Hannu Maaheimo, Heidi Salminen, Olli Tossavainen, Alexander D Frey

Open access · hybridAbstract read
In one paragraph

Article in Glycoconjugate journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 30% 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, 13 citations in OpenAlex.

  1. Article
  2. Recombinant Production and Characterization of a Novel α-L-Fucosidase fromInternational journal of molecular sciences · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. 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 3 institutions in 1 country.

Anne UsvalampiDepartment of Bioproducts and Biosystems, Aalto University School of Chemical Engineering, P.O. Box 16100, Espoo, Finland. anne.usvalampi@aalto.fi.ORCID 0000-0002-6176-6945
Marcela Ruvalcaba MedranoDepartment of Bioproducts and Biosystems, Aalto University School of Chemical Engineering, P.O. Box 16100, Espoo, Finland.
Hannu MaaheimoVTT Technical Research Centre of Finland Ltd., P.O. Box 1000, Espoo, Finland.ORCID 0000-0001-6563-3421
Heidi SalminenDepartment of Bioproducts and Biosystems, Aalto University School of Chemical Engineering, P.O. Box 16100, Espoo, Finland.
Olli TossavainenValio Ltd., P.O.Box 10, Helsinki, Finland.
Alexander D FreyDepartment of Bioproducts and Biosystems, Aalto University School of Chemical Engineering, P.O. Box 16100, Espoo, Finland.ORCID 0000-0002-4371-0227
Aalto University · FIValio (Finland) · FIVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fucosylated oligosaccharides are interesting molecules due to their bioactive properties. In particular, their application as active ingredient in milk powders is attractive for dairy industries. The objective of this study was to characterize the glycosyl hydrolase family 29 α-fucosidase produced by Aspergillus niger and test its ability to transfucosylate lactose with a view towards potential industrial applications such as the valorization of the lactose side stream produced by dairy industry. In order to reduce costs and toxicity the use of free fucose instead of environmentally questionable fucose derivatives was studied. In contrast to earlier studies, a recombinantly produced A. niger α-fucosidase was utilized. Using pNP-fucose as substrate, the optimal pH for hydrolytic activity was determined to be 3.8. The optimal temperature for a 30-min reaction was 60 °C, and considering temperature stability, the optimal temperature for a 24-h reaction was defined as 45 °C For the same hydrolysis reaction, the kinetic values were calculated to be 0.385 mM for the K

Indexed as

alpha-L-FucosidaseAspergillus nigerEnzyme StabilityFucoseFungal ProteinsLactoseSubstrate Specificityalpha-L-FucosidaseFucoseFungal ProteinsLactose1-FucosyllactoseAspergillus nigerFucosyllactoseNon-reducing sugarTransfucosylationα-Fucosidase

Identifiers

PMID31792892
PMCPMC7083800
OpenAlexW2991596465

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.