ArticleMolecular biology reports2012
Expression, characterization and 2,4,6-trichlorophenol degradation of laccase from Monilinia fructigena.
Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Degradation and Detoxification of Chlorophenols with Different Structure by LAC-4 Laccase Purified from White-Rot FungusInternational journal of environmental research and public health · 2022Article
- Genome-based engineering of ligninolytic enzymes in fungi.Microbial cell factories · 2021Review
- Characterization of a Novel Laccase LAC-Yang1 from White-Rot FungusMolecules (Basel, Switzerland) · 2021Article
- Proteomic Studies to Understand the Mechanisms of Peach Tissue Degradation byFrontiers in plant science · 2020Article
- Purification and Characterization of a White Laccase with Pronounced Dye Decolorizing Ability and HIV-1 Reverse Transcriptase Inhibitory Activity from Lepista nuda.Molecules (Basel, Switzerland) · 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 novel laccase from Coprinus cinereus and decolorization of different chemically dyes.Molecular biology reports · 2013Article
- Heterologous expression and characterization of a novel laccase isoenzyme with dyes decolorization potential from Coprinus comatus.Molecular biology reports · 2013Article
Corrections and comments
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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
A novel laccase gene from Monilinia fructigena was synthesized chemically according to the yeast bias codon and integrated into the genome of Pichia pastoris GS115 by electroporation. The expressed enzyme was recovered from the culture supernatant and purified. The result of enzyme activity assay and SDS-PAGE demonstrated that the recombinant laccase was induced and extracellularly expressed in P. pastoris. Main biochemical properties of this laccase, such as thermodependence and thermostability, optimal pH and pH stability, and the effect of metal ions and inhibitors, were characterized. With 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate (ABTS) as the substrate, MfLcc had its optimal pH at 3.5 and optimal temperature at 45°C. The Km values of the ABTS, guaiacol were 0.012 and 0.016 Mm, respectively, and the corresponding V (max) values are 243.9 and 10.55 Um min(-1) mg(-1), respectively. The recombinant laccase degraded 80% 2,4,6-trichlorophenol after 8 h under the optimal conditions. The recombinant strain and its laccase can be considered as candidate for treating waste water polluted with trichlorophenols.
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