Evidence map›Paper›PMID 28761064›Full record

ArticleScientific reports2017

The enzymatic epimerization of deoxynivalenol by Devosia mutans proceeds through the formation of 3-keto-DON intermediate.

Yousef I Hassan, Jian Wei He, Norma Perilla, KaiJie Tang, Petr Karlovsky, Ting Zhou

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
12.7field-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

35 citing papers in PubMed, 65 citations in OpenAlex.

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  16. Review
  17. 3-keto-DON, but Not 3-International journal of molecular sciences · 2022
    Article
  18. Review
  19. Microbial detoxification of mycotoxins in food.Frontiers in microbiology · 2022
    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 3 countries.

Yousef I HassanGuelph Research and Development Centre, Agriculture and Agri-Food Canada, Guelph, Ontario, Canada.
Jian Wei HeGuelph Research and Development Centre, Agriculture and Agri-Food Canada, Guelph, Ontario, Canada.
Norma PerillaGuelph Research and Development Centre, Agriculture and Agri-Food Canada, Guelph, Ontario, Canada.
KaiJie TangGuelph Research and Development Centre, Agriculture and Agri-Food Canada, Guelph, Ontario, Canada.
Petr KarlovskyMolecular Phytopathology and Mycotoxin Research, Georg-August-University Göttingen, Göttingen, Germany.ORCID 0000-0002-6532-5856
Ting ZhouGuelph Research and Development Centre, Agriculture and Agri-Food Canada, Guelph, Ontario, Canada. Ting.Zhou@agr.gc.ca.
Agriculture and Agri-Food Canada · CAUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzymatic detoxification of deoxynivalenol (DON) is a promising mitigation strategy for addressing this mycotoxin contamination of cereal grains. A recently described bacterium, Devosia mutans 17-2-E-8, capable of transforming DON into its non-toxic stereoisomer 3-epi-DON, holds promise for the development of such applications. Earlier observations suggested that DON epimerization proceeds via a two-step catalysis with 3-keto-DON as an intermediate. The results of this study indicate that NADPH is required for DON epimerization by cell-free protein extracts of D. mutans, while high concentrations of glucose and sucrose have a suppressive effect. Chemically synthesized 3-keto-DON incubated with D. mutans protein fractions enriched by ammonium sulfate precipitation at 35-55% saturation selectively reduced 3-keto-DON to 3-epi-DON, but fell short of supporting the complete epimerization of DON. In addition, seven Devosia species investigated for DON epimerization were all able to reduce 3-keto-DON to 3-epi-DON, but only a few were capable of epimerizing DON. The above observations collectively confirm that the enzymes responsible for the oxidation of DON to 3-keto-DON are physically separate from those involved in 3-keto-DON reduction to 3-epi-DON. The enzymatic nature of DON epimerization suggests that the process could be used to develop genetically engineered crops or microorganisms, ultimately reducing foodborne exposure of consumers and farm animals to DON.

Indexed as

Edible GrainFood ContaminationHyphomicrobiaceaeInactivation, MetabolicNADPRacemases and EpimerasesTrichothecenes3-keto-deoxynivalenoldeoxynivalenolNADPRacemases and EpimerasesTrichothecenes

Identifiers

PMID28761064
PMCPMC5537285
OpenAlexW2736838717

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.