1. Academic Validation
  2. Eukaryotic expression and antimicrobial spectrum determination of the peptide tachyplesin II

Eukaryotic expression and antimicrobial spectrum determination of the peptide tachyplesin II

  • Protein Expr Purif. 2008 Apr;58(2):175-83. doi: 10.1016/j.pep.2007.12.007.
Feng Xu 1 Kun Meng Ya-Ru Wang Hui-Ying Luo Pei-Long Yang Ning-Feng Wu Yun-Liu Fan Bin Yao
Affiliations

Affiliation

  • 1 Microbial Engineering Department, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12, Zhongguancun South Street, Haidan District, Beijing 100081, China; College of Life Science, Yangtze University, Jingsha, Hubei 434100, China.
Abstract

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 150mg/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 microg/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.

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