Evidence map›Paper›PMID 34350478›Full record

ReviewApplied microbiology and biotechnology2021

Novel oleate hydratases and potential biotechnological applications.

Peter Leon Hagedoorn, Frank Hollmann, Ulf Hanefeld

Open access · hybridAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 29 citations in OpenAlex.

  1. A Comparative Biochemical Study of Oleate Hydratases.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Chiral Alcohols from Alkenes and Water: Directed Evolution of a Styrene Hydratase.Angewandte Chemie (International ed. in English) · 2023
    Article
  12. Article
  13. Selective Supercritical COMolecules (Basel, Switzerland) · 2022
    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

3 authors at 1 institution in 1 country.

Peter Leon HagedoornDepartment of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629, HZ, Delft, The Netherlands. P.L.Hagedoorn@tudelft.nl.ORCID http://orcid.org/0000-0001-6342-2022
Frank HollmannDepartment of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629, HZ, Delft, The Netherlands.ORCID https://orcid.org/0000-0003-4821-756X
Ulf HanefeldDepartment of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629, HZ, Delft, The Netherlands.ORCID https://orcid.org/0000-0002-4102-6165
Delft University of Technology · NL

Funding

Netherlands Organisation for Scientific Research (NWO) domain Applied and Engineering Sciences 14170
6 · The paper itself

Abstract

Oleate hydratase catalyses the addition of water to the CC double bond of oleic acid to produce (R)-10-hydroxystearic acid. The enzyme requires an FAD cofactor that functions to optimise the active site structure. A wide range of unsaturated fatty acids can be hydrated at the C10 and in some cases the C13 position. The substrate scope can be expanded using 'decoy' small carboxylic acids to convert small chain alkenes to secondary alcohols, albeit at low conversion rates. Systematic protein engineering and directed evolution to widen the substrate scope and increase the conversion rate is possible, supported by new high throughput screening assays that have been developed. Multi-enzyme cascades allow the formation of a wide range of products including keto-fatty acids, secondary alcohols, secondary amines and α,ω-dicarboxylic acids. KEY POINTS: • Phylogenetically distinct oleate hydratases may exhibit mechanistic differences. • Protein engineering to improve productivity and substrate scope is possible. • Multi-enzymatic cascades greatly widen the product portfolio.

Indexed as

Hydro-LyasesOleic AcidCatalysisCatalytic DomainFatty Acids, UnsaturatedFatty Acids, UnsaturatedHydro-LyasesOleic Acid10-hydroxystearic acidBiocatalysisOleate hydrataseProtein engineering

Identifiers

PMID34350478
PMCPMC8403116
OpenAlexW3189327053

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.