- Expression and Purification of Lacticin Q by Small Ubiquitin-Related Modifier Fusion in Escherichia coli
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Qingshan Ma , Zhanqiao Yu , Bing Han , Qing Wang , Rijun Zhang
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J. Microbiol. 2012;50(2):326-331. Published online April 27, 2012
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DOI: https://doi.org/10.1007/s12275-012-1425-x
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Lacticin Q is a broad-spectrum class II bacteriocin with potential as an alternative to conventional antibiotics. The objective of this study was to produce recombinant lacticin Q using a small ubiquitin-related modifier (SUMO) fusion protein expression system. The 168-bp lacticin Q gene was cloned into the expression vector pET SUMO and transformed into Escherichia coli BL21(DE3). The soluble fusion protein was recovered with a Ni-NTA Sepharose column (95% purity); 130 mg protein was obtained per liter of fermentation culture. The SUMO tag was then proteolytically cleaved from the protein, which was re-applied to the column. Finally, about 32 mg lacticin Q (≥96% purity) was obtained. The recombinant protein exhibited antimicrobial properties similar to that of the native protein, demonstrating that lacticin Q had been successfully expressed by the SUMO fusion system.
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