ArticleMolecular biology reports2020
Purification, characterization, and gene cloning of two laccase isoenzymes (Lac1 and Lac2) from Trametes hirsuta MX2 and their potential in dye decolorization.
Article in Molecular biology reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Characterization and application potential of a robust recombinant laccase rTpLcc3 from Trametes polyzona for textile dye decolorization.Scientific reports · 2026Article
- Cloning and Heterologous Expression of Laccase from Beauveria pseudobassiana PHF4 in E. coli and its Application in the Degradation of Catechol.Current microbiology · 2026Article
- Recent Advances in Laccase Production: Challenges and Future Perspectives.Journal of microbiology and biotechnology · 2025Review
- Optimization, purification and characterization of laccase from a new endophytic Trichoderma harzianum AUMC14897 isolated from Opuntia ficus-indica and its applications in dye decolorization and wastewater treatment.Microbial cell factories · 2024Article
- Review
- Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5.Folia microbiologica · 2023Article
- Improvement of Laccase Production byJournal of fungi (Basel, Switzerland) · 2023Article
- Characterization of a Recombinant Laccase B fromMolecules (Basel, Switzerland) · 2022Article
- Multicopper oxidase (MCO) laccase from3 Biotech · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In this study, two laccase isoenzymes (Lac1 and Lac2) from the culture supernatant of Trametes hirsuta MX2 were purified, and the genes (Lac1 and Lac2) coding the isoenzymes were cloned. Both Lac1 and Lac2 contained an open reading frame of 1563 bp with an identity of 79%. The two isoenzymes showed significant biochemical differences. The maximal activities of Lac1 and Lac2 were at pH 2.5 with 2-2'-azino-di-(3-ethylbenzthiazoline sulfonic acid) (ABTS), and the optimal temperatures for the activities of Lac1 and Lac2 were 60 and 50 °C, respectively. Lac1 exhibited excellent resistance to acidic conditions and retained 62.17% of its initial activity at pH 2.5 after a 72-h incubation. Lac2 was more thermostable than Lac1 with half-lives (t
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Registered trials
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