Evidence map›Paper›PMID 26698313›Full record

ReviewMolecular biotechnology2016

Yeast Hosts for the Production of Recombinant Laccases: A Review.

Zuzana Antošová, Hana Sychrová

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
7.2field-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

22 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Characterization of a New Laccase fromMolecules (Basel, Switzerland) · 2023
    Article
  12. Characterization of a Recombinant Laccase B fromMolecules (Basel, Switzerland) · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  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

2 authors at 1 institution in 1 country.

Zuzana AntošováDepartment of Membrane Transport, Institute of Physiology, Czech Academy of Sciences (CAS), Vídeňská 1083, 142 20, Prague 4, Czech Republic. antosova@biomed.cas.cz.
Hana SychrováDepartment of Membrane Transport, Institute of Physiology, Czech Academy of Sciences (CAS), Vídeňská 1083, 142 20, Prague 4, Czech Republic. hana.sychrova@fgu.cas.cz.
Czech Academy of Sciences · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laccases are multi-copper oxidoreductases which catalyze the oxidation of a wide range of substrates during the simultaneous reduction of oxygen to water. These enzymes, originally found in fungi, plants, and other natural sources, have many industrial and biotechnological applications. They are used in the food, textile, pulp, and paper industries, as well as for bioremediation purposes. Although natural hosts can provide relatively high levels of active laccases after production optimization, heterologous expression can bring, moreover, engineered enzymes with desired properties, such as different substrate specificity or improved stability. Hence, diverse hosts suitable for laccase production are reviewed here, while the greatest emphasis is placed on yeasts which are commonly used for industrial production of various proteins. Different approaches to optimize the laccase expression and activity are also discussed in detail here.

Indexed as

AnimalsBacteriaFungiInsectaLaccaseProtein EngineeringRecombinant ProteinsSubstrate SpecificityYeastsLaccaseRecombinant ProteinsExpression optimizationHeterologous expressionLaccaseRecombinantYeasts

Identifiers

PMID26698313
OpenAlexW2212838866

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.