ArticleMicrobial cell factories2016
Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum.
Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 74 citations in OpenAlex.
- Multi-parameter optimization of recombinant protein secretion in Bacillus subtilis: a review.Microbial cell factories · 2026Review
- Exploration of Length and Hydrophobicity Requirements for Optimal α-Amylase Secretion in Bacillus subtilis Based on Rational Design.Microbial biotechnology · 2026Article
- Rapid Identification of Superior Endogenous Signal Peptides for Heterologous Protein Secretion by Corynebacterium glutamicum Through Modular Cloning and Automation.Microbial biotechnology · 2026Article
- Development and Immunogenicity Assessment of a Multi-Epitope Antigen Against Zika Virus: An In Silico and In Vivo Approach.Vaccines · 2025Article
- 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
- Comparative evaluation of the extracellular production of a polyethylene terephthalate degrading cutinase by Corynebacterium glutamicum and leaky Escherichia coli in batch and fed-batch processes.Microbial cell factories · 2024Article
- Design of fully synthetic signal peptide library and its use for enhanced secretory production of recombinant proteins in Corynebacterium glutamicum.Microbial cell factories · 2024Article
- Development of a split-luciferase assay to establish optimal protein secretion conditions for protein production byMicrobiology (Reading, England) · 2024Article
- Genetic identification and expression optimization of a novel protease HapR fromFrontiers in bioengineering and biotechnology · 2024Article
- From frozen cell bank to product assay: high-throughput strain characterisation for autonomous Design-Build-Test-Learn cycles.Microbial cell factories · 2023Article
- Optimized recombinant production of the bacteriocin garvicin Q byFrontiers in microbiology · 2023Article
- High-level recombinant protein production with Corynebacterium glutamicum using acetate as carbon source.Microbial biotechnology · 2022Article
- 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
- Scaling production of GFP1-10 detector protein in E. coli for secretion screening by split GFP assay.Microbial cell factories · 2021Article
- An overview and future prospects of recombinant protein production in Bacillus subtilis.Applied microbiology and biotechnology · 2021Review
- Random and combinatorial mutagenesis for improved total production of secretory target protein in Escherichia coli.Scientific reports · 2021Article
- SPSED: A Signal Peptide Secretion Efficiency Database.Frontiers in bioengineering and biotechnology · 2021Article
- Biosensor-Based Optimization of Cutinase Secretion byFrontiers in microbiology · 2021Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTechnical bulk enzymes represent a huge market, and the extracellular production of such enzymes is favorable due to lowered cost for product recovery. Protein secretion can be achieved via general secretion (Sec) pathway. Specific sequences, signal peptides (SPs), are necessary to direct the target protein into the translocation machinery. For example, >150 Sec-specific SPs have been identified for Bacillus subtilis alone. As the best SP for a target protein of choice cannot be predicted a priori, screening of homologous SPs has been shown to be a powerful tool for different expression organisms. While SP libraries between closely related species were successfully applied to optimize recombinant protein secretion, this was not investigated for distantly related species. Therefore, in this study a Sec SP library from low-GC firmicutes B. subtilis is investigated to optimize protein secretion in high-GC actinobacterium Corynebacterium glutamicum using cutinase from Fusarium solani pisi as model protein.
resultsA homologous SP library (~150 SP) for recombinant cutinase secretion in B. subtilis was successfully transferred to C. glutamicum as alternative secretion host. Cutinase secretion in C. glutamicum was quantified using an automated micro scale cultivation system for online growth monitoring, cell separation and cutinase activity determination. Secretion phenotyping results were correlated to those from a previous study, in which the same SP library was used to optimize secretion of the same cutinase but using B. subtilis as host. Strikingly, behavior of specific SP-cutinase combinations was changed dramatically between B. subtilis and C. glutamicum. Some SPs showed comparable cutinase secretion performances in both hosts, whereas other SPs caused diametrical extracellular cutinase activities.
conclusionThe optimal production strain for a specific target protein of choice still cannot be designed in silico. Not only the best SP for a target protein has to be evaluated each time from scratch, the expression host also affects which SP is best. Thus, (heterologous) SP library screening using high-throughput methods is considered to be crucial to construct an optimal production strain for a target protein.
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