ReviewBiotechnology and bioengineering2026
Bacterial Laccase: Recent Advances in Production, Engineering Strategies, and Diagnostic Applications.
Review in Biotechnology and bioengineering, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Bacterial laccases are multicopper oxidase enzymes that are able to catalyze the oxidation reaction of phenolic and non-phenolic substrates followed by the reduction reaction of molecular oxygen to water as the only byproduct. It exhibits high stability under harsh conditions and can be produced recombinantly in various microbial hosts. Herein, we review recent advances in bacterial laccase research over the past decade, which focus on production technologies, protein engineering strategies, and diagnostic applications. We also discuss how synthetic biology has overcome historical limitations in heterologous expression and enabled industrial-scale production in hosts such as Escherichia coli and Bacillus subtilis. In addition, we analyzed how directed evolution, rational design, post-translational modifications, and computational modeling have enhanced the catalytic properties of laccases. In the final chapter, we evaluate the use of bacterial laccases as peroxidase alternatives for detecting clinical analytes like dopamine, uric acid, and glucose biosensing and point-of-care diagnostics. This review integrated more than 120 peer-reviewed papers and provides a comprehensive assessment of how bacterial laccases are transitioning from laboratory curiosities to practical biocatalysts in environmental monitoring, industrial processing, and medical diagnostics. We conclude the review by identifying remaining challenges and future research directions for realizing the full potential of these versatile enzymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.