ArticlePloS one2015
Computational analysis and low-scale constitutive expression of laccases synthetic genes GlLCC1 from Ganoderma lucidum and POXA 1B from Pleurotus ostreatus in Pichia pastoris.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 52 citations in OpenAlex.
- Decoding the distribution, structure-function-redox potential relationship and recent advances in fungal laccases: a systematic approach.Bioprocess and biosystems engineering · 2026Review
- Artificial Intelligence in Edible Mushroom Cultivation, Breeding, and Classification: A Comprehensive Review.Journal of fungi (Basel, Switzerland) · 2025Review
- Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression.Microbial cell factories · 2024Article
- Statistical Improvement of rGILCC 1 and rPOXA 1B Laccases Activity Assay Conditions Supported by Molecular Dynamics.Molecules (Basel, Switzerland) · 2023Article
- Molecular Docking of Lac_CB10: Highlighting the Great Potential for Bioremediation of Recalcitrant Chemical Compounds by One Predicted Bacteroidetes CopA-Laccase.International journal of molecular sciences · 2023Article
- Impact of Antibiotics as Waste, Physical, Chemical, and Enzymatical Degradation: Use of Laccases.Molecules (Basel, Switzerland) · 2022Review
- A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases.Molecules (Basel, Switzerland) · 2021Review
- Recombinant laccase rPOXA 1B real-time, accelerated and molecular dynamics stability study.BMC biotechnology · 2021Article
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- Tertiary treatment (3 Biotech · 2020Article
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- Detoxification of pulping black liquor with Pleurotus ostreatus or recombinant Pichia pastoris followed by CuO/TiOScientific reports · 2018Article
- Conditions and Regulation of Mixed Culture to Promote Shiraia bambusicola and Phoma sp. BZJ6 for Laccase Production.Scientific reports · 2017Article
- Advanced Materials From Fungal Mycelium: Fabrication and Tuning of Physical Properties.Scientific reports · 2017Article
- Diversity of Ligninolytic Enzymes and Their Genes in Strains of the GenusFrontiers in microbiology · 2017Article
- Plackett-Burman Design for rGILCC1 Laccase Activity Enhancement inEnzyme research · 2017Article
- Diverse Metabolic Capacities of Fungi for Bioremediation.Indian journal of microbiology · 2016Review
- Yeast Hosts for the Production of Recombinant Laccases: A Review.Molecular biotechnology · 2016Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lacasses are multicopper oxidases that can catalyze aromatic and non-aromatic compounds concomitantly with reduction of molecular oxygen to water. Fungal laccases have generated a growing interest due to their biotechnological potential applications, such as lignocellulosic material delignification, biopulping and biobleaching, wastewater treatment, and transformation of toxic organic pollutants. In this work we selected fungal genes encoding for laccase enzymes GlLCC1 in Ganoderma lucidum and POXA 1B in Pleurotus ostreatus. These genes were optimized for codon use, GC content, and regions generating secondary structures. Laccase proposed computational models, and their interaction with ABTS [2, 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid)] substrate was evaluated by molecular docking. Synthetic genes were cloned under the control of Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase (GAP) constitutive promoter. P. pastoris X-33 was transformed with pGAPZαA-LaccGluc-Stop and pGAPZαA-LaccPost-Stop constructs. Optimization reduced GC content by 47 and 49% for LaccGluc-Stop and LaccPost-Stop genes, respectively. A codon adaptation index of 0.84 was obtained for both genes. 3D structure analysis using SuperPose revealed LaccGluc-Stop is similar to the laccase crystallographic structure 1GYC of Trametes versicolor. Interaction analysis of the 3D models validated through ABTS, demonstrated higher substrate affinity for LaccPost-Stop, in agreement with our experimental results with enzymatic activities of 451.08 ± 6.46 UL-1 compared to activities of 0.13 ± 0.028 UL-1 for LaccGluc-Stop. This study demonstrated that G. lucidum GlLCC1 and P. ostreatus POXA 1B gene optimization resulted in constitutive gene expression under GAP promoter and α-factor leader in P. pastoris. These are important findings in light of recombinant enzyme expression system utility for environmentally friendly designed expression systems, because of the wide range of substrates that laccases can transform. This contributes to a great gamut of products in diverse settings: industry, clinical and chemical use, and environmental applications.
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