کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2021644 | 1069256 | 2008 | 9 صفحه PDF | دانلود رایگان |
Ta0-a, the gene encoding the mature antimicrobial peptide tachyplesin II, was engineered to optimize the coding sequence according to codon usage bias in yeast. Ta0-a was efficiently expressed in the methylotrophic yeast Pichia pastoris strain SMD1168. The recombinant peptide Ta0 reached 150 mg/L after methanol induction for 6 d. Ta0 was rapidly purified to homogeneity by a single step of size-exclusion chromatography. The minimal lethal concentrations of Ta0 to the Escherichia coli strain K12 was 30 μg/mL. Ta0 exhibited a wide range of antimicrobial activity: the growth of 26 bacterial and fungal strains, including some typical food/feed spoilage microorganisms, was all substantially inhibited. This result indicates the potential practical application of the recombinant peptide in various industrial products.
Journal: Protein Expression and Purification - Volume 58, Issue 2, April 2008, Pages 175–183