Review3 Biotech2016
Bioprospecting and biotechnological applications of fungal laccase.
Review in 3 Biotech, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 234 citations in OpenAlex.
- Efficient Chitosan-Ferulic Acid Hydrogel Formation at Neutral pH by a Two-Domain Bacterial Laccase: Mechanistic and Functional Study.Polymers · 2026Article
- Trametes versicolor laccase induces apoptosis and DNA damage in colorectal cancer via reactive oxygen species-mediated signaling disruption.Molecular biology reports · 2026Article
- Development of SpyTag/SpyCatcher-driven thermostable cyclic laccase and its application in lignin and dye degradation and polymerization of phenolic compounds.Science China. Life sciences · 2026Article
- Genome-wide identification, classification and expression analysis of laccase family members in Solanum lycopersicum.BMC plant biology · 2026Article
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- Anticancer potential of purified laccase enzyme from Trametes versicolor: specific cytotoxicity against thyroid and endometrial cancer cells.Molecular biology reports · 2025Article
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- Article
- Advancements in enzyme immobilization on magnetic nanomaterials: toward sustainable industrial applications.RSC advances · 2024Review
- An Enzymatic and Proteomic Analysis ofJournal of fungi (Basel, Switzerland) · 2024Article
- Recent Progress and Future Prospects of Laccase Immobilization on MOF Supports for Industrial Applications.Applied biochemistry and biotechnology · 2024Review
- Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the ExtremophileMolecules (Basel, Switzerland) · 2024Article
- A low-cost and eco-friendly recombinant protein expression system using copper-containing industrial wastewater.Frontiers in microbiology · 2024Article
- Fungal Laccases: Fundamentals, Engineering and Classification Update.Biomolecules · 2023Review
- Application of Immobilized Enzymes in Juice Clarification.Foods (Basel, Switzerland) · 2023Review
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- Identification and Characterization of a NewFrontiers in microbiology · 2022Article
- Trends and Applications of Omics Technologies to Functional Characterisation of Enzymes and Protein Metabolites Produced by Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases.Molecules (Basel, Switzerland) · 2021Review
- Port Sediments: Problem or Resource? A Review Concerning the Treatment and Decontamination of Port Sediments by Fungi and Bacteria.Microorganisms · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccase belongs to a small group of enzymes called the blue multicopper oxidases, having the potential ability of oxidation. It belongs to enzymes, which have innate properties of reactive radical production, but its utilization in many fields has been ignored because of its unavailability in the commercial field. There are diverse sources of laccase producing organisms like bacteria, fungi and plants. In fungi, laccase is present in Ascomycetes, Deuteromycetes, Basidiomycetes and is particularly abundant in many white-rot fungi that degrade lignin. Laccases can degrade both phenolic and non-phenolic compounds. They also have the ability to detoxify a range of environmental pollutants. Due to their property to detoxify a range of pollutants, they have been used for several purposes in many industries including paper, pulp, textile and petrochemical industries. Some other application of laccase includes in food processing industry, medical and health care. Recently, laccase has found applications in other fields such as in the design of biosensors and nanotechnology. The present review provides an overview of biological functions of laccase, its mechanism of action, laccase mediator system, and various biotechnological applications of laccase obtained from endophytic fungi.
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.