Evidence map›Paper›PMID 33997930›Full record

ReviewApplied microbiology and biotechnology2021

Pecularities and applications of aryl-alcohol oxidases from fungi.

Vlada B Urlacher, Katja Koschorreck

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

20 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Oestrogen Detoxification Ability of White Rot FungusJournal of fungi (Basel, Switzerland) · 2024
    Article
  8. Article
  9. Substrate specificity mapping of fungal CAZy AA3_2 oxidoreductases.Biotechnology for biofuels and bioproducts · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Vlada B UrlacherInstitute of Biochemistry, Heinrich-Heine-University Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany.
Katja KoschorreckInstitute of Biochemistry, Heinrich-Heine-University Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany. Katja.Koschorreck@hhu.de.ORCID http://orcid.org/0000-0001-9689-9863
Heinrich Heine University Düsseldorf · DE

Funding

Ministry of Innovation, Science and Research within the framework of the NRW-Strategieprojekt BioSC 313/323-400-002 13
6 · The paper itself

Abstract

Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate spectrum accompanied by the only need for molecular oxygen as cosubstrate and production of hydrogen peroxide as sole by-product makes these enzymes very promising biocatalysts. AAOs were used in the synthesis of flavors, fragrances, and other high-value-added compounds and building blocks as well as in dye decolorization and pulp biobleaching. Furthermore, AAOs offer a huge potential as efficient suppliers of hydrogen peroxide for peroxidase- and peroxygenase-catalyzed reactions. A prerequisite for application as biocatalysts at larger scale is the production of AAOs in sufficient amounts. Heterologous expression of these predominantly fungal enzymes is, however, quite challenging. This review summarizes different approaches aiming at enhancing heterologous expression of AAOs and gives an update on substrates accepted by these promising enzymes as well as potential fields of their application. KEY POINTS: • Aryl-alcohol oxidases (AAOs) supply ligninolytic peroxidases with H

Indexed as

Alcohol OxidoreductasesHydrogen PeroxideAlcoholsFungiLigninPeroxidasePeroxidasesAlcohol OxidoreductasesAlcoholsHydrogen PeroxideLigninPeroxidasePeroxidasesAliphatic allylic alcoholsAryl-alcohol oxidaseAryl alcoholsBio-based precursorsBiocatalysisFlavorsGMC familyLignin degradation

Identifiers

PMID33997930
PMCPMC8140971
OpenAlexW3163383841

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.