Abstract: In order to explore the technical route for prokaryotic expression and purification of bovine neutrophilβ-defensin 11 (BNBD11), BNBD11 gene was synthesized using preferred condons of E. coli, according to the reported amino acid sequence of BNBD11. The recombinant expression plasmid pET32a-BNBD11 was constructed and then transformed into E. coli BL21. The expression of BNBD11 in E. coli BL21 was induced by isopropylβ-D-1-thiogalactopyranoside (IPTG). SDS-PAGE showed that most expressed products were soluble. The fusion protein was purified by Ni Sepharose column chromatography. After the cleavage of the fusion protein by formic acid, Ni Sepharose column was used again to remove proteins with His-Tag and the purified recombinant BNBD11 was achieved. Therefore, BNBD11 was successfully expressed in E. coli, and the recombinant BNBD11 was obtained.

Key words: β-defensin, BNBD1, fusion expression, Escherichia coli