ArticleMicrobial cell factories2023
Development of an efficient protein expression system in the thermophilic fungus Myceliophthora thermophila.
Article in Microbial cell factories, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 8 citations in OpenAlex.
- Semi-automated strain engineering and screening in the thermophilic fungusApplied and environmental microbiology · 2026Article
- Boosting the cellulolytic oxidative and hydrolytic enzyme systems in Myceliophthora thermophila for the efficient enzymatic saccharification of lignocellulosic biomass.Bioresources and bioprocessing · 2025Article
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
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11 authors at 2 institutions in 1 country.
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Abstract
backgroundThermophilic fungus Myceliophthora thermophila has been widely used in industrial applications due to its ability to produce various enzymes. However, the lack of an efficient protein expression system has limited its biotechnological applications.
resultsIn this study, using a laccase gene reporting system, we developed an efficient protein expression system in M. thermophila through the selection of strong constitutive promoters, 5'UTRs and signal peptides. The expression of the laccase was confirmed by enzyme activity assays. The results showed that the Mtpdc promoter (Ppdc) was able to drive high-level expression of the target protein in M. thermophila. Manipulation of the 5'UTR also has significant effects on protein expression and secretion. The best 5'UTR (NCA-7d) was identified. The transformant containing the laccase gene under the Mtpdc promoter, NCA-7d 5'UTR and its own signal peptide with the highest laccase activity (1708 U/L) was obtained. In addition, the expression system was stable and could be used for the production of various proteins, including homologous proteins like MtCbh-1, MtGh5-1, MtLPMO9B, and MtEpl1, as well as a glucoamylase from Trichoderma reesei.
conclusionsAn efficient protein expression system was established in M. thermophila for the production of various proteins. This study provides a valuable tool for protein production in M. thermophila and expands its potential for biotechnological applications.
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