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Biotechnol Lett. 2005 May;27(10):725-30.

Production and purification of a novel antibiotic peptide, adenoregulin, from a recombinant Escherichia coli.

Author information

1
State Key Laboratory of Bioreactor Engineering New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200237, P.R. China.

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.

PMID:
16049742
DOI:
10.1007/s10529-005-5361-2
[Indexed for MEDLINE]

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