文献类型：期刊文献

英文题名：Production and purification of a novel antibiotic peptide, adenoregulin, from a recombinant Escherichia coli

作者：Zhou, YX; Cao, W; Luo, QP; Ma, YS; Wang, JZ; Wei, DZ

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn New World Inst Biot, Shanghai 200237, Peoples R China

年份：2005

卷号：27

期号：10

起止页码：725

外文期刊名：BIOTECHNOLOGY LETTERS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000230844500010)】；

语种：英文

外文关键词：adenoregulin; Escherichia coli; fed-batch culture; purification; recombinant protein expression

摘要：Adenoregulin is a member of dermaseptin family which are vertebrate antibiotic peptides having lethal effects against a broad spectrum of bacteria, fungi and protozoa. The 99 bp adenoregulin gene was cloned in the expression vector pET32a and transformed into Escherichia coli BL21(DE3). In fed-batch cultivation of BL21(DE3)/pET32a-adr, an exponential feeding strategy was applied to gain 60 g dry cells l(-1). The recombinant fusion protein Trx-ADR was expressed in a soluble form. The fusion protein was isolated by Ni2+-chelating chromatography, cleaved with CNBr and purified to homogeneity through reverse phase-HPLC and size exclusion-HPLC. The purified recombinant adenoregulin had antibacterial activity against Escherichia coli K12D31 with apparent Mr of 3.4 kDa, identical to the anticipated value.