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KMID : 0880220120500020326
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Journal of Microbiology
2012 Volume.50 No. 2 p.326 ~ p.331
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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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Abstract
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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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KEYWORD
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bacteriocin, Escherichia coli, recombinant expression, lacticin Q, small ubiquitin-related modifier
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