Production and purification of a novel antibiotic peptide,adenoregulin, from a recombinant <Emphasis Type="Italic">Escherichia coli</Emphasis> |
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Authors: | Yu-Xun?Zhou Wei?Cao Qing-Ping?Luo Yu-Shu?Ma Jin-Zhi?Wang Email author" target="_blank">Dong-Zhi?WeiEmail author |
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Institution: | (1) State Key Laboratory of Bioreactor Engineering New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200237, P.R. China |
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Abstract: | 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. |
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Keywords: | adenoregulin Escherichia coli fed-batch culture purification recombinant protein expression |
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