| Title |
Expression and Purification of Lacticin Q by Small Ubiquitin-Related Modifier Fusion in Escherichia coli |
| Author |
Qingshan Ma, Zhanqiao Yu, Bing Han, Qing Wang, and Rijun Zhang* |
| Address |
Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science & Technology, China Agricultural University, Beijing 100193, P. R. China |
| Bibliography |
Journal of Microbiology, 50(2),326-331, 2012,
|
| DOI |
|
| Key Words |
bacteriocin, Escherichia coli, recombinant expression, lacticin Q, small ubiquitin-related modifier |
| Abstract |
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. |
