Evidence map›Paper›PMID 27696775›Full record

ReviewMicrobial biotechnology2017

Laccase: a multi-purpose biocatalyst at the forefront of biotechnology.

Diana M Mate, Miguel Alcalde

Abstract readReview
In one paragraph

Review in Microbial biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
–field-weighted citation impact
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

125 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Chemo-Enzymatic Route for Covalent Cellulose Fiber Dyeing.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  7. Enhanced Inhibition ofInternational journal of molecular sciences · 2026
    Article
  8. Transcriptome Analysis of PostharvestFoods (Basel, Switzerland) · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Polymers · 2025
    Article
  15. Review
  16. 3 Biotech · 2025
    Article
  17. Article
  18. Review
  19. The research progress of LACC1.Frontiers in immunology · 2025
    Review
  20. Article

65 more citing papers are in PubMed but not listed here.

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.

Diana M MateDepartment of Biocatalysis, Institute of Catalysis, CSIC, Cantoblanco, 28049, Madrid, Spain.
Miguel AlcaldeDepartment of Biocatalysis, Institute of Catalysis, CSIC, Cantoblanco, 28049, Madrid, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laccases are multicopper containing enzymes capable of performing one electron oxidation of a broad range of substrates. Using molecular oxygen as the final electron acceptor, they release only water as a by-product, and as such, laccases are eco-friendly, versatile biocatalysts that have generated an enormous biotechnological interest. Indeed, this group of enzymes has been used in different industrial fields for very diverse purposes, from food additive and beverage processing to biomedical diagnosis, and as cross-linking agents for furniture construction or in the production of biofuels. Laccases have also been studied intensely in nanobiotechnology for the development of implantable biosensors and biofuel cells. Moreover, their capacity to transform complex xenobiotics makes them useful biocatalysts in enzymatic bioremediation. This review summarizes the most significant recent advances in the use of laccases and their future perspectives in biotechnology.

Indexed as

BacteriaBacterial ProteinsBiocatalysisBiotechnologyLaccaseNanotechnologyBacterial ProteinsLaccase

Identifiers

PMID27696775
PMCPMC5658592

What OpenQuestion holds

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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.