Evidence map›Paper›PMID 26068013›Full record

ArticleScientific reports2015

Biochemical properties and yields of diverse bacterial laccase-like multicopper oxidases expressed in Escherichia coli.

Julian Ihssen, Renate Reiss, Ronny Luchsinger, Linda Thöny-Meyer, Michael Richter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
21.7field-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

38 citing papers in PubMed, 113 citations in OpenAlex.

  1. A Putative Multicopper Oxidase Encoded byInternational journal of molecular sciences · 2026
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  6. Review
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  8. Degradation of tetracycline, oxytetracycline & ampicillin by purified multiple copper oxidase like laccase from Stentrophomonas sp. YBX1.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  9. Article
  10. Bacterial transformation of lignin: key enzymes and high-value products.Biotechnology for biofuels and bioproducts · 2024
    Review
  11. Article
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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

5 authors at 1 institution in 1 country.

Julian IhssenEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biointerfaces, Lerchenfeldstr.5, 9014 St. Gallen, Switzerland.
Renate ReissEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biointerfaces, Lerchenfeldstr.5, 9014 St. Gallen, Switzerland.
Ronny LuchsingerEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biointerfaces, Lerchenfeldstr.5, 9014 St. Gallen, Switzerland.
Linda Thöny-MeyerEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biointerfaces, Lerchenfeldstr.5, 9014 St. Gallen, Switzerland.
Michael RichterEmpa, Swiss Federal Laboratories for Materials Science and Technology, Laboratory for Biointerfaces, Lerchenfeldstr.5, 9014 St. Gallen, Switzerland.
Swiss Federal Laboratories for Materials Science and Technology · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laccases are multi-copper oxidases that oxidize a broad range of substrates at the expense of molecular oxygen, without any need for co-factor regeneration. These enzymes bear high potential for the sustainable synthesis of fine chemicals and the modification of (bio)polymers. Here we describe cloning and expression of five novel bacterial laccase-like multi copper oxidases (LMCOs) of diverse origin which were identified by homology searches in online databases. Activity yields under different expression conditions and temperature stabilities were compared to three previously described enzymes from Bacillus subtilis, Bacillus pumilus and Bacillus clausii. In almost all cases, a switch to oxygen-limited growth conditions after induction increased volumetric activity considerably. For proteins with predicted signal peptides for secretion, recombinant expression with and without signal sequence was investigated. Bacillus CotA-type LMCOs outperformed enzymes from Streptomyces and Gram-negative bacteria with respect to activity yields in Escherichia coli and application relevant biochemical properties. The novel Bacillus coagulans LMCO combined high activity yields in E. coli with unprecedented activity at strong alkaline pH and high storage stability, making it a promising candidate for further development.

Indexed as

BacillusBacterial ProteinsEnzyme StabilityEscherichia coliGene ExpressionHydrogen-Ion ConcentrationLaccaseRecombinant ProteinsBacterial ProteinsLaccaseRecombinant Proteins

Identifiers

PMID26068013
PMCPMC4464401
OpenAlexW566003893

What OpenQuestion holds

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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.