ArticleWorld journal of microbiology & biotechnology2019
Heterologous expression and purification of BtCspB, a novel cold-shock protein-like bacteriocin from Bacillus thuringiensis BRC-ZYR2.
Article in World journal of microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 14 citations in OpenAlex.
- Different Detection Strategies of Pediocin-Like Produced by Pediococcus pentosaceus.Probiotics and antimicrobial proteins · 2025Article
- Striving for sustainable biosynthesis: discovery, diversification, and production of antimicrobial drugs in Escherichia coli.Biochemical Society transactions · 2022Review
- Identification of Cyt2Ba from a New Strain of Bacillus thuringiensis and Its Toxicity in Bradysia difformis.Current microbiology · 2020Article
- Molecular Characterization and Heterologous Production of the Bacteriocin Peocin, a DNA Starvation/Stationary Phase Protection Protein, fromMolecules (Basel, Switzerland) · 2019Article
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10 authors at 3 institutions in 2 countries.
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Abstract
A novel Bacillus thuringiensis (Bt) bacteriocin BtCspB, active against a food-borne pathogen Bacillus cereus, was identified and purified by a traditional four-step chromatographic process with low yield (44.5 µg/L) in our lab previously. The aim of this study was to dramatically increase its yield by heterologous expression of BtCspB. The BtCspB gene from Bt BRC-ZYR2 was successfully heterologously expressed in Escherichia coli BL21 (DE3). Affinity chromatography was used to obtain the pure BtCspB up to 20 mg/L. The purified BtCspB showed a MIC value of 12.5 µg/mL and a MBC value of 50.0 µg/mL against Bacillus cereus ATCC 10987. The bacteriocin activity of BtCspB against B. cereus ATCC 10987 was further directly detected in a gel-overlay assay. The anti-B. cereus activity, however, was lower than the bacteriocin purified by the traditional four-step chromatographic process probably because of structural modifications. Compared with the traditional method, the yield of the bacteriocin by heterologous expression increased by 449 times, and the purification step was dramatically simplified, which laying a foundation for the industrial production of this novel cold-shock protein-like bacteriocin BtCspB active against B. cereus.
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