ArticleMolecular biology reports2013
Purification and characterization of a novel laccase from Coprinus cinereus and decolorization of different chemically dyes.
Article in Molecular biology reports, 2013. 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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9 citing papers in PubMed, 32 citations in OpenAlex.
- Purification, characterization and three-dimensional structure prediction of multicopper oxidase Laccases from Trichoderma lixii FLU1 and Talaromyces pinophilus FLU12.Scientific reports · 2024Article
- Comparative genomic analysis of five coprinoid mushrooms species.Functional & integrative genomics · 2023Article
- Genome-based engineering of ligninolytic enzymes in fungi.Microbial cell factories · 2021Review
- Production, characterization and Congo red dye decolourizing efficiency of a laccase fromJournal, genetic engineering & biotechnology · 2016Article
- The trade-off of availability and growth inhibition through copper for the production of copper-dependent enzymes by Pichia pastoris.BMC biotechnology · 2016Article
- Yeast Hosts for the Production of Recombinant Laccases: A Review.Molecular biotechnology · 2016Review
- Isolation, Purification and Characterization of Two Laccases from Carrot (Daucus carota L.) and Their Response to Abiotic and Metal Ions Stresses.The protein journal · 2015Article
- Purification and characterization of a laccase from Coprinopsis cinerea in Pichia pastoris.World journal of microbiology & biotechnology · 2014Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccase is a blue copper oxidase with multiple copper ions and widely distributed in higher plant and fungi. To date, numerous fungal laccases have been reported by many researchers. In present work, a new laccase gene, named CcLCC5I, from Coprinus cinereus was synthesized chemically according to the yeast bias codon and integrated into Pichia pastoris GS115 genome by electroporation. SDS-PAGE analysis showed that the recombinant laccase has a molecular mass of approximately 56.8 kDa. Its biochemical properties was carried out using substrate 2-2(')-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS). It was showed that the optimum pH and temperature of the laccase is 3.0 and 55 °C, respectively. Except for copper ions, most metal ions inhibited the laccase activity at a high concentration about 10 mM. Sodium sulfite can also highly inhibit laccase activity whereas EDTA had no inhibitory effect on the laccase activity. The CcLCC5I have high ability to decolor not only azo but also aryl methane dyes. The recombinant laccase decolored 44.6 % orange G, 54.8 % Crystal Violet, and 87.2 % Malachite green at about 2.6 h. The novel laccase may be a good candidate for breeding engineering strains used in the treatment of industrial effluent containing azo and aryl methane dyes.
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