Open AccessProduction of Bacteriocin E50-52 by Small Ubiquitin-Related Modifier Fusion in Escherichia coli
Author(s) -
Qing Wang,
Wen-Juan Fu,
Qingshan Ma,
Yu Zhen,
Rijun Zhang
Publication year - 2013
Publication title -
polish journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.312
H-Index - 34
eISSN - 2544-4646
pISSN - 1733-1331
DOI - 10.33073/pjm-2013-047
Subject(s) - bacteriocin , escherichia coli , fusion protein , sepharose , recombinant dna , fermentation , protease , chemistry , biochemistry , biology , microbiology and biotechnology , antimicrobial , gene , enzyme
Bacteriocin E50-52, a class IIa bacteriocin with a wide antibacterial spectrum, and has a huge potential to be a substitute for convention. antibiotics. In this research, the bacteriocin E50-52 gene was cloned into the expression vector pET SUMO (small ubiquitin-related modifier) and introduced into Escherichia coli BL21 (DE3). The recombinant fusion protein SUMO-bacteriocin E50-52 expressed in a soluble form was purified to a purity of more than 90% by Ni-NTA sepharose column and 117 mg fusion protein was obtained per liter of fermentation culture. The fusion protein was cleaved with SUMO protease and re-applied to a Ni-NTA Sepharose column. Finally, about 16 mg recombinant bacteriocin E50-52 (rbE50-52) was obtained from a 1-liter fermentation culture with no less than 95% purity. The rbE50-52 had similar antimicrobial properties and molecular weight as the native bacteriocin E50-52 and showed very low hemolytic activity.