ArticleWorld journal of microbiology & biotechnology2014
Purification and characterization of a laccase from Coprinopsis cinerea in Pichia pastoris.
Article in World journal of microbiology & biotechnology, 2014. 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, 18 citations in OpenAlex.
- Article
- Purification and biochemical characterization of laccase from3 Biotech · 2025Article
- Role and structure of the small subunit forming heterodimers with laccase-like enzymes.Protein science : a publication of the Protein Society · 2023Article
- Multicopper oxidases with laccase-ferroxidase activity: Classification and study of ferroxidase activity determinants in a member fromComputational and structural biotechnology journal · 2023Article
- Heterologous Expression, Engineering and Characterization of a Novel Laccase ofJournal of fungi (Basel, Switzerland) · 2021Article
- Signal peptide replacement resulted in recombinant homologous expression of laccase Lcc8 in Coprinopsis cinerea.AMB Express · 2019Article
- Heterologous expression and characterisation of a laccase from Colletotrichum lagenarium and decolourisation of different synthetic dyes.World journal of microbiology & biotechnology · 2016Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A modified laccase gene, CcLCC6, from Coprinopsis cinerea was chemically synthesized according to the yeast codon bias and expressed in Pichia pastoris. The main properties of laccase, effects of ions and inhibitors, and optimal condition for decolouring malachite green (MG) were investigated in this study. The optimal pH level and temperature of laccase are 3.0 and 40 °C, respectively. The metal ions Mn²⁺, Zn²⁺, Fe³⁺ and Al³⁺ could inhibit laccase activity, as well as 1 mM of sodium dodecyl sulphate and sodium thiosulphate. 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), as a mediator, was necessary in decolorizing MG. The optimal pH and temperature for MG decolorization were 3.0 and 50 °C, respectively. Approximately 0.02 μM recombinant laccase could effectively decolour 0.05 mM of MG in 1 h. CcLCC6I could inhibit the toxicity of MG to P. pastoris. This is the first report on the successful expression in P. pastoris of CcLCC6I and its enzymatic property. Laccase can also be considered as a candidate for treating industrial effluent containing MG.
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