Dataset Information

High-efficiency production of the antimicrobial peptide pediocin PA-1 in metabolically engineered Corynebacterium glutamicum using a microaerobic process at acidic pH and elevated levels of bivalent calcium ions.

ABSTRACT:

Background

Pediocin PA-1 is a bacteriocin of recognized value with applications in food bio-preservation and the medical sector for the prevention of infection. To date, industrial manufacturing of pediocin PA-1 is limited by high cost and low-performance. The recent establishment of the biotechnological workhorse Corynebacterium glutamicum as recombinant host for pediocin PA-1 synthesis displays a promising starting point towards more efficient production.

Results

Here, we optimized the fermentative production process. Following successful simplification of the production medium, we carefully investigated the impact of dissolved oxygen, pH value, and the presence of bivalent calcium ions on pediocin production. It turned out that the formation of the peptide was strongly supported by an acidic pH of 5.7 and microaerobic conditions at a dissolved oxygen level of 2.5%. Furthermore, elevated levels of CaCl₂ boosted production. The IPTG-inducible producer C. glutamicum CR099 pXMJ19 P_tac pedACD^Cg provided 66 mg L^-1 of pediocin PA-1 in a two-phase batch process using the optimized set-up. In addition, the novel constitutive strain P_tuf pedACD^Cg allowed successful production without the need for IPTG.

Conclusions

The achieved pediocin titer surpasses previous efforts in various microbes up to almost seven-fold, providing a valuable step to further explore and develop this important bacteriocin. In addition to its high biosynthetic performance C. glutamicum proved to be highly robust under the demanding producing conditions, suggesting its further use as host for bacteriocin production.

SUBMITTER: Christmann J

PROVIDER: S-EPMC9969654 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature

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Publications

High-efficiency production of the antimicrobial peptide pediocin PA-1 in metabolically engineered Corynebacterium glutamicum using a microaerobic process at acidic pH and elevated levels of bivalent calcium ions.

Christmann Jens J Cao Peng P Becker Judith J Desiderato Christian K CK Goldbeck Oliver O Riedel Christian U CU Kohlstedt Michael M Wittmann Christoph C

Microbial cell factories 20230227 1

<h4>Background</h4>Pediocin PA-1 is a bacteriocin of recognized value with applications in food bio-preservation and the medical sector for the prevention of infection. To date, industrial manufacturing of pediocin PA-1 is limited by high cost and low-performance. The recent establishment of the biotechnological workhorse Corynebacterium glutamicum as recombinant host for pediocin PA-1 synthesis displays a promising starting point towards more efficient production.<h4>Results</h4>Here, we optimi ...[more]

PMID: 36849884

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Dataset Information

High-efficiency production of the antimicrobial peptide pediocin PA-1 in metabolically engineered Corynebacterium glutamicum using a microaerobic process at acidic pH and elevated levels of bivalent calcium ions.

Background

Results

Conclusions

Publications

High-efficiency production of the antimicrobial peptide pediocin PA-1 in metabolically engineered Corynebacterium glutamicum using a microaerobic process at acidic pH and elevated levels of bivalent calcium ions.

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