ArticleApplied and environmental microbiology2010
Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and heterologous signal peptides.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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66 citing papers in PubMed, 183 citations in OpenAlex.
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- A novel signal peptide toolbox for optimized heterologous expression of yeast pheromones in Bacillus subtilis.Journal, genetic engineering & biotechnology · 2025Article
- Screening signal peptides from Bacillus thuringiensis secretome for heterologous protein secretion.Applied microbiology and biotechnology · 2025Article
- Advances in recombinant protease production: current state and perspectives.World journal of microbiology & biotechnology · 2024Review
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- Genetic identification and expression optimization of a novel protease HapR fromFrontiers in bioengineering and biotechnology · 2024Article
- Induction of the CtsR regulon improves Xylanase production in Bacillus subtilis.Microbial cell factories · 2023Article
- Study on active capacity and detergent application potential of low-temperature alkaline serine protease produced by new strain Exiguobacterium indicum 1.2.3.Bioresources and bioprocessing · 2023Article
- Metabolic engineering of Thermoanaerobacterium aotearoense strain SCUT27 for biofuels production from sucrose and molasses.Biotechnology for biofuels and bioproducts · 2023Article
- Analysis of protein secretion in Bacillus subtilis by combining a secretion stress biosensor strain with an in vivo split GFP assay.Microbial cell factories · 2023Article
- Efficient production of α-monoglucosyl hesperidin by cyclodextrin glucanotransferase from Bacillus subtilis.Applied microbiology and biotechnology · 2023Article
- Secretory expression of recombinant small laccase genes in Gram-positive bacteria.Microbial cell factories · 2023Article
- Modular Engineering to Enhance Keratinase Production for Biotransformation of Discarded Feathers.Applied biochemistry and biotechnology · 2023Article
- Signal Peptide Efficiency: From High-Throughput Data to Prediction and Explanation.ACS synthetic biology · 2023Article
- Accelerated strain construction and characterization of C. glutamicum protein secretion by laboratory automation.Applied microbiology and biotechnology · 2022Article
- Construction and Application of a Plasmid-Based Signal Peptide Library for Improved Secretion of Recombinant Proteins withMicroorganisms · 2022Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN' from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.
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