ReviewApplied biochemistry and biotechnology2022
Eminent Industrial and Biotechnological Applications of Laccases from Bacterial Source: a Current Overview.
Review in Applied biochemistry and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 48 citations in OpenAlex.
- 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
- Comparative performance of non-white rot fungal stirred-tank and biofilm-based bioreactors for pharmaceutical wastewater treatment: kinetic modelling and scalability potential.Biodegradation · 2026Article
- Laccase enzyme as a sustainable tool for improving environmental health.Biodegradation · 2025Review
- Laccase-Catalyzed Oligomerization of Esculin: Effect of Key Reaction Parameters and Evaluation of Oligoesculin Antioxidant and Skin Prebiotic Capacity.Applied biochemistry and biotechnology · 2025Article
- Designing Artificial Laccase Catalysts by Introducing Substrate Oxidation Metals into Oxygen-Reducing Metal-Organic Frameworks: Cu-Doped ZIF-67.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Microbial Immobilized Enzyme Biocatalysts for Multipollutant Mitigation: Harnessing Nature's Toolkit for Environmental Sustainability.International journal of molecular sciences · 2024Review
- Biochemical and Structural Characterization of a Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered fromInternational journal of molecular sciences · 2024Article
- Optimization of laccase from Stenotrophomonas maltophilia E1 by submerge fermentation using coconut husk with its detoxification and biodecolorization ability of synthetic dyes.Bioresources and bioprocessing · 2023Article
- Enhancing the production of a heterologous Trametes laccase (LacA) by replacement of the major cellulase CBH1 in Trichoderma reesei.Journal of industrial microbiology & biotechnology · 2023Article
- Low-abundance populations distinguish microbiome performance in plant cell wall deconstruction.Microbiome · 2022Article
- Genomic analysis uncovers laccase-coding genes and biosynthetic gene clusters encoding antimicrobial compounds in laccase-producing Acinetobacter baumannii.Scientific reports · 2022Article
- Identification and Characterization of a NewFrontiers in microbiology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccases are blue multicopper oxidases that oxidize a wide range of phenolic as well as non-phenolic substrates in the presence or absence of mediators. They occur in various species of bacteria, fungi, insects, and plants; bacterial laccases show high substrate specificity. Bacteria produce these enzymes either extracellularly or intracellularly and exhibit stability to a wide range of pH and temperature. Therefore, they are suitable for various industrial processes such as food, textile, and paper and pulp industry. They are also valuable for producing biofuels, pharmaceuticals, biosensors, and degradation of various environmental pollutants and xenobiotics compounds. Since bacterial laccases are more versatile in the sense of nutritional needs and ecological factors, their use can provide a promising solution to various problems related to industry and the field of biotechnology. However, there is a need for a thorough understanding of the chemistry and activity of bacterial laccases to enable their full potential use in bioremediation and biofuel production.
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.