ReviewMicroorganisms2025
Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.
Review in Microorganisms, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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
5 citing papers in PubMed.
- Bacterial Laccase: Recent Advances in Production, Engineering Strategies, and Diagnostic Applications.Biotechnology and bioengineering · 2026Review
- Laccase-Mediated Fabrication of Food Packaging Films: A Critical Review of Functional Performance, Safety, and Industrial Viability.Biomolecules · 2026Review
- Genome analysis of Acrophialophora yunnanensis and its lignocellulolytic enzyme system.World journal of microbiology & biotechnology · 2026Article
- The multifaceted physiological roles of fungal laccases.Communications biology · 2026Review
- Fungal Frontiers in (Bio)sensing.Biosensors · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
Laccase, a member of the blue multicopper oxidase family, is widely distributed across diverse taxonomic groups, including fungi, bacteria, plants, and insects. This enzyme drives biocatalytic processes through the oxidation of phenolic compounds, aromatic amines, and lignin derivatives, underpinning its significant potential in the food industry, cosmetics, and environmental remediation. However, wild-type laccases face critical limitations, such as low catalytic efficiency, insufficient expression yields, and poor stability. To address these bottlenecks, this review systematically examines optimization strategies for heterologous laccase expression by fungal and bacterial systems. Additionally, we discuss protein engineering for laccase modification, with a focus on the structural basis and active-site redesign. The comprehensive analysis presented herein provides strategic suggestions for advancing laccase engineering, ultimately establishing a theoretical framework for developing high-efficiency, low-cost engineered variants for large-scale biomanufacturing and green chemistry applications.
Indexed as
Identifiers
What Socratic 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 Socratic graph.