ArticlePeerJ2021
Expression of thermophilic two-domain laccase from
Article in PeerJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- Strategies for recombinant laccase expression and their roles in environmental remediation.World journal of microbiology & biotechnology · 2026Review
- Metal-Resistant Mesophilic Laccase from Achromobacter Species: Identification, Physical Characterisation, and Dye Bioremediation.Applied biochemistry and biotechnology · 2026Article
- Bioelectrocatalyst for OInternational journal of molecular sciences · 2025Article
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
- Functionalization of MWCNTs for Bioelectrocatalysis by Bacterial Two-Domain Laccase fromNanomaterials (Basel, Switzerland) · 2023Article
- Recombinant expression and characterization of a new laccase, bioinformatically identified, from the Antarctic thermophilic bacterium Geobacillus sp. ID17.Extremophiles : life under extreme conditions · 2023Article
- Efficient Degradation of Aflatoxin BToxins · 2021Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTwo-domain laccases are copper-containing oxidases found in bacteria in the beginning of 2000ths. Two-domain laccases are known for their thermal stability, wide substrate specificity and, the most important of all, their resistance to so-called «strong inhibitors» of classical fungal laccases (azides, fluorides). Low redox potential was found to be specific for all the two-domain laccases, due to which these enzymes lost the researchers' interest as potentially applicable for various biotechnological purposes, such as bioremediation. Searching, obtaining and studying the properties of novel two-domain laccases will help to obtain an enzyme with high redox-potential allowing its practical application.
methodsA gene encoding two-domain laccase was identified in
resultsA novel two-domain recombinant laccase CjSL appeared to be a multimer with a subunit molecular mass of 37 kDa. It oxidized a wide range of phenolic substrates (ferulic acid, caffeic acid, hydroquinone, catechol, etc.) at alkaline pH, while oxidizing of non phenolic substrates (K
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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.