ArticleBMC biotechnology2017
Expression and characteristics of manganese peroxidase from Ganoderma lucidum in Pichia pastoris and its application in the degradation of four dyes and phenol.
Article in BMC biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 126 citations in OpenAlex.
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- Tramates trogii biomass in carboxymethylcellulose-lignin composite beads for adsorption and biodegradation of bisphenol A.Biodegradation · 2023Article
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- Endophytes in Lignin Valorization: A Novel Approach.Frontiers in bioengineering and biotechnology · 2022Review
- Current advances ofFrontiers in microbiology · 2022Review
- Design and Engineering of an Efficient Peroxidase Using Myoglobin for Dye Decolorization and Lignin Bioconversion.International journal of molecular sciences · 2021Article
- Challenges and Recent Advances in Enzyme-Mediated Wastewater Remediation-A Review.Nanomaterials (Basel, Switzerland) · 2021Review
- The mechanism of degradation of alizarin red by a white-rot fungus Trametes gibbosa.BMC biotechnology · 2021Article
- Biodegradation of aromatic pollutants meets synthetic biology.Synthetic and systems biotechnology · 2021Article
- Trends and Applications of Omics Technologies to Functional Characterisation of Enzymes and Protein Metabolites Produced by Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- Textile Dye Biodecolorization by Manganese Peroxidase: A Review.Molecules (Basel, Switzerland) · 2021Review
- Genetic and functional analysis of the Zn(II)Applied microbiology and biotechnology · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundManganese peroxidase (MnP) of white rot basidiomycetes, an extracellular heme enzyme, is part of a peroxidase superfamily that is capable of degrading the different phenolic compounds. Ganoderma, a white rot basidiomycete widely distributed worldwide, could secrete lignin-modifying enzymes (LME), including laccase (Lac), lignin peroxidases (LiP) and MnP.
resultsAfter the selection of a G. lucidum strain from five Ganoderma strains, the 1092 bp full-length cDNA of the MnP gene, designated as G. lucidum MnP (GluMnP1), was cloned from the selected strain. We subsequently constructed an eukaryotic expression vector, pAO815:: GlMnP, and transferred it into Pichia pastoris SMD116. Recombinant GluMnP1 (rGluMnP1) was with a yield of 126 mg/L and a molecular weight of approximately 37.72 kDa and a specific enzyme activity of 524.61 U/L. The rGluMnP1 could be capable of the decolorization of four types of dyes and the degradation of phenol. Phenol and its principal degradation products including hydroquinone, pyrocatechol, resorcinol, benzoquinone, were detected successfully in the experiments.
conclusionsThe rGluMnP1 could be effectively expressed in Pichia pastoris and with a higher oxidation activity. We infer that, in the initial stages of the reaction, the catechol-mediated cycle should be the principal route of enzymatic degradation of phenol and its oxidation products. This study highlights the potential industrial applications associated with the production of MnP by genetic engineering methods, and the application of industrial wastewater treatment.
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