ArticleMicrobial biotechnology2021
Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.
Article in Microbial biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 47 citations in OpenAlex.
- Understanding Lignin Oxidation by a Two-Domain Multicopper Oxidase fromBiochemistry · 2026Article
- Bacterial laccases for green remediation of contaminants of emerging concern: from molecular cloning to metagenomic and computational insights.Biodegradation · 2026Review
- Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions.Protein science : a publication of the Protein Society · 2026Article
- Screening of Lactic Acid Bacteria Strains for Potential Sourdough and Bread Applications: Enzyme Expression and Exopolysaccharide Production.Probiotics and antimicrobial proteins · 2025Article
- Regional and National Shared Research Resources: Challenges and Opportunities§.Journal of biomolecular techniques : JBT · 2025Article
- Leveraging bacterial laccases to facilitate the decomposition of xenobiotic compounds: a review.3 Biotech · 2024Review
- Biochemical and Structural Characterization of a Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered fromInternational journal of molecular sciences · 2024Article
- Structural Insight into the Amino Acid Environment of the Two-Domain Laccase's Trinuclear Copper Cluster.International journal of molecular sciences · 2023Article
- Heterologous expression, purification, and characterization of thermo- and alkali-tolerant laccase-like multicopper oxidase from Bacillus mojavensis TH309 and determination of its antibiotic removal potential.Archives of microbiology · 2023Article
- Structure-function studies of a novel laccase-like multicopper oxidase from Thermothelomyces thermophila provide insights into its biological role.Acta crystallographica. Section D, Structural biology · 2023Article
- The Biomodified Lignin Platform: A Review.Polymers · 2023Review
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- The potential of lactic acid bacteria isolated fromVeterinary world · 2023Article
- Heterologous Expression of theFoods (Basel, Switzerland) · 2022Article
- Involvement ofInsects · 2022Article
- New liquid supports in the development of integrated platforms for the reuse of oxidative enzymes and polydopamine production.Frontiers in bioengineering and biotechnology · 2022Article
- Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.Microbial biotechnology · 2021Article
- Enzymatic Oxidation of Ca-Lignosulfonate and Kraft Lignin in Different Lignin-Laccase-Mediator-Systems and MDF Production.Frontiers in bioengineering and biotechnology · 2021Article
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 at 3 institutions in 2 countries.
Funding
Abstract
Prokaryotic laccases are emergent biocatalysts. However, they have not been broadly found and characterized in bacterial organisms, especially in lactic acid bacteria. Recently, a prokaryotic laccase from the lactic acid bacterium Pediococcus acidilactici 5930, which can degrade biogenic amines, was discovered. Thus, our study aimed to shed light on laccases from lactic acid bacteria focusing on two Pediococcus laccases, P. acidilactici 5930 and Pediococcus pentosaceus 4816, which have provided valuable information on their biochemical activities on redox mediators and biogenic amines. Both laccases are able to oxidize canonical substrates as ABTS, ferrocyanide and 2,6-DMP, and non-conventional substrates as biogenic amines. With ABTS as a substrate, they prefer an acidic environment and show sigmoidal kinetic activity, and are rather thermostable. Moreover, this study has provided the first structural view of two lactic acid bacteria laccases, revealing new structural features not seen before in other well-studied laccases, but which seem characteristic for this group of bacteria. We believe that understanding the role of laccases in lactic acid bacteria will have an impact on their biotechnological applications and provide a framework for the development of engineered lactic acid bacteria with enhanced properties.
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.