ArticleMicrobial cell factories2017
Cell surface engineering of Bacillus subtilis improves production yields of heterologously expressed α-amylases.
Article in Microbial cell factories, 2017. 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, 36 citations in OpenAlex.
- System reconstruction ofSynthetic and systems biotechnology · 2027Article
- α-Amylase: Its Structure, Molecular Modification, and Application in the Food Field.Foods (Basel, Switzerland) · 2026Review
- Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis.Microbial cell factories · 2024Article
- The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024Article
- Review
- Membrane composition and organization of Bacillus subtilis 168 and its genome-reduced derivative miniBacillus PG10.Microbial biotechnology · 2022Article
- Enhanced production of heterologous proteins via engineering the cell surface of Bacillus licheniformis.Journal of industrial microbiology & biotechnology · 2019Article
- Article
- Enhanced production of heterologous proteins by Bacillus licheniformis with defective D-alanylation of lipoteichoic acid.World journal of microbiology & biotechnology · 2018Article
- Genetic Tools and Techniques for Recombinant Expression in Thermophilic Bacillaceae.Microorganisms · 2018Review
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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
backgroundBacillus subtilis is widely used as a cell factory for numerous heterologous proteins of commercial value and medical interest. To explore the possibility of further enhancing the secretion potential of this model bacterium, a library of engineered strains with modified cell surface components was constructed, and the corresponding influences on protein secretion were investigated by analyzing the secretion of α-amylase variants with either low-, neutral- or high- isoelectric points (pI).
resultsRelative to the wild-type strain, the presence of overall anionic membrane phospholipids (phosphatidylglycerol and cardiolipin) increased dramatically in the PssA-, ClsA- and double KO mutants, which resulted in an up to 47% higher secretion of α-amylase. Additionally, we demonstrated that the appropriate net charge of secreted targets (AmyTS-23, AmyBs and AmyBm) was beneficial for secretion efficiency as well.
conclusionsIn B. subtilis, the characteristics of cell membrane phospholipid bilayer and the pIs of heterologous α-amylases appear to be important for their secretion efficiency. These two factors can be engineered to reduce the electrostatic interaction between each other during the secretion process, which finally leads to a better secretion yield of α-amylases.
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