Expression and Purification of Lacticin Q by Small Ubiquitin-Related Modifier Fusion in Escherichia coli
2012
Ma, Qingshan, China Agricultural University, Beijing, P. R. China | Yu, Zhanqiao, China Agricultural University, Beijing, P. R. China | Han, Bing, China Agricultural University, Beijing, P. R. China | Wang, Qing, China Agricultural University, Beijing, P. R. China | Zhang, Rijun, China Agricultural University, Beijing, P. R. China
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 (greater-than or equal to 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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