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Abstract
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Article Information:
Expression of Antimicrobial Peptide Dybowskin-2CAMa in Pichia pastoris and Characterization of its Antibacterial Activity
Lili Jin, Dezheng Yuan, Yu Wang, Chao Jiang, Zheng Wang, Qian Zhao and Qiuyu Wang
Corresponding Author: Qiuyu Wang
Submitted: March 26, 2013
Accepted: April 15, 2013
Published: August 05, 2013 |
Abstract:
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n 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.
Key words: Antimicrobial peptide, antibacterial activity, dybowskin-2CAMa, expression, , ,
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Cite this Reference:
Lili Jin, Dezheng Yuan, Yu Wang, Chao Jiang, Zheng Wang, Qian Zhao and Qiuyu Wang, . Expression of Antimicrobial Peptide Dybowskin-2CAMa in Pichia pastoris and Characterization of its Antibacterial Activity. Advance Journal of Food Science and Technology, (08): 1005-1010.
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ISSN (Online): 2042-4876
ISSN (Print): 2042-4868 |
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