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Expression of Antimicrobial Peptide Dybowskin-2CAMa in Pichia pastoris and Characterization of its Antibacterial Activity

Author(s): Lili Jin | Dezheng Yuan | Yu Wang | Chao Jiang | Zheng Wang | Qian Zhao | Qiuyu Wang

Journal: Advance Journal of Food Science and Technology
ISSN 2042-4868

Volume: 5;
Issue: 8;
Start page: 1005;
Date: 2013;
Original page

Keywords: Antimicrobial peptide | antibacterial activity | dybowskin-2CAMa | expression

In this study we used a yeast expression system to express a new antimicrobial peptide dybowskin-2CAMa from the skin cDNA library of Rana amurenisis. The entire coding region of the dybowskin-2CAMa was cloned into the plasmid pPICZ&alpha-A and then transformed into competent P. pastoris X33. The expressed dybowskin-2CAMa was purified from the culture supernatant by Sephadex G-25 and YMC*GEL ODS-A chromatography followed by C18 reverse phased HPLC. The purified peptide exhibited a single band of about 2 kDa when resolved by Tricine-SDS-PAGE. Its exact molecular weight was 2456.46 Da which was consistent with the value predicted from its deduced amino acid sequence. Antimicrobial activity assay showed that the recombinant dybowskin-2CAMa could inhibit the growth of a broad spectrum of bacteria, while displaying very low level of hemolytic activity (&le4% relative to Triton X-100), even at concentration of up to 500 &mug/mL.
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