Serine and threonine activate Ser/Thr kinase gene to increase the density of Lactobacillus bulgaricus sp1.1 under salt stress
Salt stress significantly impedes high cell-density culture by suppressing the reproductive capacity of lactic acid bacteria. This study examined the effects of salt stress conditions (2% w/v NaCl) on Lactobacillus bulgaricus sp1.1. Although DNA replication and division ring localization remained unaffected, the down-regulation of the ftsZ and dnaA genes inhibited division ring assembly. Consequently, bacteria exhibited filamentation, increased cell length, and accumulated chromosomes and division rings, which obstructed cell division. Under salt stress, sp1.1 experienced several transcriptional changes. The serine/threonine kinase gene was identified as a significant regulator of bacterial division under salt stress. Exogenous addition of serine and threonine could stimulate the expression of Ser/Thr kinase gene, promote the assembly of division ring, and enhance the dividing ability of the bacterium, which led to a density of 7.93 log CFU/mL under the salt stress, which was 6.92 times higher than that of the untreated group. This study provides a new perspective for high-density cultivation of lactic acid bacteria. • The division ring of strain sp1.1 is incomplete under salt stress. • Gene Ser/Thr kinase is a key gene affecting bacterial division under salt stress. • Ser and Thr promote cell division by increasing the expression of Ser/Thr kinase gene.
Authors
- Jialei Sun
- Yuanqiang Tu
- Yihan Wang (ORCID: https://orcid.org/0000-0002-8219-2901)
- Xue Han (ORCID: https://orcid.org/0000-0002-5276-8631)
- Yu Wang (ORCID: https://orcid.org/0000-0002-8009-9076)
- Huaxi Yi (ORCID: https://orcid.org/0000-0002-6071-7113)
- Peng Yu (ORCID: https://orcid.org/0000-0001-9572-7939)
Institutions
- Harbin Institute of Technology (CN)
- Anhui University of Traditional Chinese Medicine (CN)
- Dairy Management (US)
- Ocean University of China (CN)
Publication Details
- Journal
- LWT
- Published
- 2024-09-12
- DOI
- https://doi.org/10.1016/j.lwt.2024.116755
- Citations
- 1
- Primary Topic
- Protein Hydrolysis and Bioactive Peptides
- Type
- article
- Field-Weighted Citation Impact
- 0.23