Expression and Purification of Lacticin Q by Small Ubiquitin-Related Modifier Fusion in Escherichia coli

Qingshan Ma; Zhanqiao Yu; Bing Han; Qing Wang; Rijun Zhang

doi:10.1007/s12275-012-1425-x

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Expression and Purification of Lacticin Q by Small Ubiquitin-Related Modifier Fusion in Escherichia coli: Qingshan Ma , Zhanqiao Yu , Bing Han , Qing Wang , Rijun Zhang; Journal of Microbiology 2012;50(2):326-331.
DOI: https://doi.org/10.1007/s12275-012-1425-x
Published online: April 27, 2012

Laboratory of Feed Biotechnology, State Key Laboratory of Animal Nutrition, College of Animal Science & Technology, China Agricultural University, Beijing 100193, P. R. China

Corresponding author: Rijun Zhang , Tel: +86-010-6273-1208,

Received: 25 August 2011 • Accepted: 19 November 2011

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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.

Keywords: bacteriocin;Escherichia coli;recombinant expression;lacticin Q;small ubiquitin-related modifier

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Expression and Purification of Lacticin Q by Small Ubiquitin-Related Modifier Fusion in Escherichia coli

J. Microbiol. 2012;50(2):326-331. Published online April 27, 2012

DOI: https://doi.org/10.1007/s12275-012-1425-x

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