ArticleApplied microbiology and biotechnology2022
Accelerated strain construction and characterization of C. glutamicum protein secretion by laboratory automation.
Article in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Rapid Identification of Superior Endogenous Signal Peptides for Heterologous Protein Secretion by Corynebacterium glutamicum Through Modular Cloning and Automation.Microbial biotechnology · 2026Article
- Best Practices for Protein Expression in Pichia pastoris Combining Design of Experiments with an Automated Platform for Parallelized Cultivation in Small-Scale Stirred Tank Bioreactors.Methods in molecular biology (Clifton, N.J.) · 2026Article
- 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
- Expanding the genetic programmability of Lactiplantibacillus plantarum.Microbial biotechnology · 2024Review
- 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
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Secretion of bacterial proteins into the culture medium simplifies downstream processing by avoiding cell disruption for target protein purification. However, a suitable signal peptide for efficient secretion needs to be identified, and currently, there are no tools available to predict optimal combinations of signal peptides and target proteins. The selection of such a combination is influenced by several factors, including protein biosynthesis efficiency and cultivation conditions, which both can have a significant impact on secretion performance. As a result, a large number of combinations must be tested. Therefore, we have developed automated workflows allowing for targeted strain construction and secretion screening using two platforms. Key advantages of this experimental setup include lowered hands-on time and increased throughput. In this study, the automated workflows were established for the heterologous production of Fusarium solani f. sp. pisi cutinase in Corynebacterium glutamicum. The target protein was monitored in culture supernatants via enzymatic activity and split GFP assay. Varying spacer lengths between the Shine-Dalgarno sequence and the start codon of Bacillus subtilis signal peptides were tested. Consistent with previous work on the secretory cutinase production in B. subtilis, a ribosome binding site with extended spacer length to up to 12 nt, which likely slows down translation initiation, does not necessarily lead to poorer cutinase secretion by C. glutamicum. The best performing signal peptides for cutinase secretion with a standard spacer length were identified in a signal peptide screening. Additional insights into the secretion process were gained by monitoring secretion stress using the C. glutamicum K9 biosensor strain. KEY POINTS: • Automated workflows for strain construction and screening of protein secretion • Comparison of spacer, signal peptide, and host combinations for cutinase secretion • Signal peptide screening for secretion by C. glutamicum using the split GFP assay.
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