Evidence map›Paper›PMID 26800369›Full record

ArticlePloS one2016

Novel α-L-Fucosidases from a Soil Metagenome for Production of Fucosylated Human Milk Oligosaccharides.

Mateusz Lezyk, Carsten Jers, Louise Kjaerulff, Charlotte H Gotfredsen, Maria D Mikkelsen, Jørn D Mikkelsen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Frontiers in insect science · 2025
    Article
  4. A Robust α-l-Fucosidase fromACS chemical biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Identification and Characterization of a Novel α-L-Fucosidase fromInternational journal of molecular sciences · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Architecture Insight of Bifidobacterial α-L-Fucosidases.International journal of molecular sciences · 2021
    Article
  14. Article
  15. Article
  16. Fucosidases from the human gut symbiont Ruminococcus gnavus.Cellular and molecular life sciences : CMLS · 2021
    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

6 authors at 2 institutions in 1 country.

Mateusz LezykCenter for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, Kgs. Lyngby, Denmark.
Carsten JersCenter for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, Kgs. Lyngby, Denmark.
Louise KjaerulffDepartment of Chemistry, Technical University of Denmark, Kgs. Lyngby, Denmark.
Charlotte H GotfredsenDepartment of Chemistry, Technical University of Denmark, Kgs. Lyngby, Denmark.
Maria D MikkelsenDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark.
Jørn D MikkelsenCenter for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, Kgs. Lyngby, Denmark.
Technical University of Denmark · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This paper describes the discovery of novel α-L-fucosidases and evaluation of their potential to catalyse the transglycosylation reaction leading to production of fucosylated human milk oligosaccharides. Seven novel α-L-fucosidase-encoding genes were identified by functional screening of a soil-derived metagenome library and expressed in E. coli as recombinant 6xHis-tagged proteins. All seven fucosidases belong to glycosyl hydrolase family 29 (GH 29). Six of the seven α-L-fucosidases were substrate-inhibited, moderately thermostable and most hydrolytically active in the pH range 6-7, when tested with para-nitrophenyl-α-L-fucopyranoside (pNP-Fuc) as the substrate. In contrast, one fucosidase (Mfuc6) exhibited a high pH optimum and an unusual sigmoidal kinetics towards pNP-Fuc substrate. When tested for trans-fucosylation activity using pNP-Fuc as donor, most of the enzymes were able to transfer fucose to pNP-Fuc (self-condensation) or to lactose. With the α-L-fucosidase from Thermotoga maritima and the metagenome-derived Mfuc5, different fucosyllactose variants including the principal fucosylated HMO 2'-fucosyllactose were synthesised in yields of up to ~6.4%. Mfuc5 was able to release fucose from xyloglucan and could also use it as a fucosyl-donor for synthesis of fucosyllactose. This is the first study describing the use of glycosyl hydrolases for the synthesis of genuine fucosylated human milk oligosaccharides.

Indexed as

alpha-L-FucosidaseEscherichia coliFucoseHumansMetagenomeMilk, HumanOligosaccharidesalpha-L-FucosidaseFucoseOligosaccharides

Identifiers

PMID26800369
PMCPMC4723247
OpenAlexW2407716000

What OpenQuestion holds

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LicenceCC BY
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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.