ArticleMicrobial cell factories2024
Secretion of the cytoplasmic and high molecular weight β-galactosidase of Paenibacillus wynnii with Bacillus subtilis.
Article in Microbial cell factories, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Recombinant production of acidophilic L-arabinose isomerase from Lentilactobacillus parakefiri in Bacillus subtilis.Microbial cell factories · 2025Article
- Toward food-grade production of the Glutamicibacter halophytocola diamine oxidase using Komagataella phaffii.AMB Express · 2025Article
- Recombinant Forms of α-Amylase AmyBL159 from a Thermophilic BacteriumMicroorganisms · 2025Article
- From Biocontrol to Synthesis: Innovative Progress ofInternational journal of molecular sciences · 2025Review
- Importance of the 5' untranslated region for recombinant enzyme production in isolated Bacillus subtilis 007.AMB Express · 2025Article
- Recombinant production of Paenibacillus wynnii β-galactosidase with Komagataella phaffii.Microbial cell factories · 2024Article
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4 authors.
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Abstract
backgroundThe gram-positive bacterium Bacillus subtilis is widely used for industrial enzyme production. Its ability to secrete a wide range of enzymes into the extracellular medium especially facilitates downstream processing since cell disruption is avoided. Although various heterologous enzymes have been successfully secreted with B. subtilis, the secretion of cytoplasmic enzymes with high molecular weight is challenging. Only a few studies report on the secretion of cytoplasmic enzymes with a molecular weight > 100 kDa.
resultsIn this study, the cytoplasmic and 120 kDa β-galactosidase of Paenibacillus wynnii (β-gal-Pw) was expressed and secreted with B. subtilis SCK6. Different strategies were focused on to identify the best secretion conditions. Tailormade codon-optimization of the β-gal-Pw gene led to an increase in extracellular β-gal-Pw production. Consequently, the optimized gene was used to test four signal peptides and two promoters in different combinations. Differences in extracellular β-gal-Pw activity between the recombinant B. subtilis strains were observed with the successful secretion being highly dependent on the specific combination of promoter and signal peptide used. Interestingly, signal peptides of both the general secretory- and the twin-arginine translocation pathway mediated secretion. The highest extracellular activity of 55.2 ± 6 µkat/L
conclusionFor the first time, the β-gal-Pw was efficiently secreted with B. subtilis SCK6, demonstrating the potential of this strain for secretory production of cytoplasmic, high molecular weight enzymes.
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