Evidence map›Paper›PMID 32356197›Full record

ReviewApplied microbiology and biotechnology2020

α-L-Fucosidases and their applications for the production of fucosylated human milk oligosaccharides.

Li Wan, Yingying Zhu, Wenli Zhang, Wanmeng Mu

Abstract readReview
PubMed Publisher
In one paragraph

Review in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
4.8field-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

10 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. L-Fucose is involved in human-gut microbiome interactions.Applied microbiology and biotechnology · 2023
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. 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

4 authors at 2 institutions in 1 country.

Li WanState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, Jiangsu, China.
Yingying ZhuState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, Jiangsu, China.
Wenli ZhangState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, Jiangsu, China.
Wanmeng MuState Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, Jiangsu, China. wmmu@jiangnan.edu.cn.
State Key Laboratory of Food Science and Technology · CNJiangnan University · CN

Funding

National First-Class Discipline Program of Food Science and Technology of China JUFSTR20180203National Natural Science Foundation of China No. 31922073Zhangjiagang international cooperation project No. ZKH1905
6 · The paper itself

Abstract

α-L-Fucosidases (EC 3.2.1.51), catalyzing the hydrolysis of fucosides and/or the transfer of fucosyl residue, have been characterized and modified into a trans-fucosylation mode or, further, engineered to function as "fucosynthase", which can be employed for the enzymatic synthesis of bioactive glycans, including fucosylated human milk oligosaccharides (HMOs). More than half of HMOs are fucosylated and have attracted ever-increasing interest because of their excellent physiological functions on breast-fed infants. To date, the characterization of novel fucosidases and molecular modification of these enzymes have been extensively studied to efficiently synthesize valuable fucosylated compounds. Herein, we discuss the advantages and challenges of different strategies for the production of HMOs and compare various donor/acceptor substrates used for the synthesis of fucosylated HMOs and their biomimetics. The implementation of trans-fucosylation patterns investigated in this paper via well-designed fucosidase mutants and proper reaction conditions may lead to development of an excellent platform, serving both fundamental studies and industrial-scale processes, for valuable carbohydrates synthesis.Key Points• Highlights different approaches for the production of human milk oligosaccharides.• Summarizes α-l-fucosidases and their mutants in enzymatic synthesis of fucosylated human milk oligosaccharides and the biomimetics.• Concludes future perspectives on methods for improving fucosylated compounds synthesis.• Highlights different approaches for the production of human milk oligosaccharides.• Summarizes α-l-fucosidases and their mutants in enzymatic synthesis of fucosylated human milk oligosaccharides and the biomimetics.• Concludes future perspectives on methods for improving fucosylated compounds synthesis.

Indexed as

alpha-L-FucosidaseBacteriaBioengineeringFucoseGlycosylationHumansMilk, HumanMutationOligosaccharidesSubstrate Specificityalpha-L-FucosidaseFucoseOligosaccharidesEnzymatic synthesisFucosylated human milk oligosaccharidesTrans-fucosylationα-L-Fucosidase

Identifiers

PMID32356197
OpenAlexW3021770203

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.