ArticleMicrobial cell factories2020
Constructing a novel expression system by specific activation of amylase expression pathway in Penicillium.
Article in Microbial cell factories, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Engineering genetic elements for microbial protein expression systems: Advances, challenges, applications, and prospects.Synthetic and systems biotechnology · 2026Review
- Analyzing the Challenges and Opportunities Associated With Harnessing New Antibiotics From the Fungal Microbiome.MicrobiologyOpen · 2025Review
- Modification of essential factors mediating post-translational processing for high-quality protein expression inEngineering microbiology · 2025Article
- Heterochromatin Protein Activates the Amylase Expression Pathway and Its Application to Recombinant Protein Expression in Penicillium oxalicum.Current microbiology · 2025Article
- An impact of N-glycosylation on biochemical properties of a recombinant α-amylase fromHeliyon · 2024Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
backgroundFilamentous fungi have long been used as hosts for the production of proteins, enzymes and valuable products in various biotechnological applications. However, recombinant proteins are expressed with highly secreted host proteins when stronger promoters are used under inducing conditions. In addition, the efficiency of target protein expression can be limited by the application of constitutive promoters in recently developed filamentous fungal expression systems.
resultsIn this study, a novel expression system was constructed by using a Penicillium oxalium strain that has powerful protein secretion capability. The secretory background of the host was reduced by knocking out the Amy13A protein and utilizing the starch as a carbon source. The strong promoter amy15A(p) was further improved by overexpressing the transcription activator AmyR and deleting of putative repressor CreA. By using the native amylase Amy15A as a reporter, the efficiency of expression from the amy15A promoter was dramatically and specifically enhanced after redesigning the regulatory network of amylase expression.
conclusionsOur researches clearly indicated that the triple-gene recombinant strain Δ13A-OamyR-ΔCreA, with the amy15A(p) promoter could be used as a suitable expression system especially for high-level and high-purity protein production.
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