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, Yu-Xun[1]; Cao, Wei[1]; Luo, Qing-Ping[1]; Ma, Yu-Shu[1]; Wang, Jin-Zhi[1]; Wei, Dong-Zhi[1]

机构：[1] State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200237, China

年份：2005

卷号：27

期号：10

起止页码：725

外文期刊名：Biotechnology Letters

收录：EI(收录号：2005339305778)

语种：英文

外文关键词：Bacteria - Cultivation - Escherichia coli - Fungi - Proteins - Protozoa

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 Ni 2+-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. ? Springer 2005.