Unknown

Dataset Information

0

Expression of Hybrid Peptide EF-1 in Pichia pastoris, Its Purification, and Antimicrobial Characterization.


ABSTRACT: EF-1 is a novel peptide derived from two bacteriocins, plantaricin E and plantaricin F. It has a strong antibacterial activity against Escherichia coli and with negligible hemolytic effect on red blood cells. However, the chemical synthesis of EF-1 is limited by its high cost. In this study, we established a heterologous expression of EF-1 in Pichia pastoris. The transgenic strain successfully expressed hybrid EF-1 peptide, which had a molecular weight of ~5 kDa as expected. The recombinant EF-1 was purified by Ni2+ affinity chromatography and reversed-phase high performance liquid chromatography (RP-HPLC), which achieved a yield of 32.65 mg/L with a purity of 94.9%. The purified EF-1 exhibited strong antimicrobial and bactericidal activities against both Gram-positive and -negative bacteria. Furthermore, propidium iodide staining and scanning electron microscopy revealed that EF-1 can directly induce cell membrane permeabilization of E. coli. Therefore, the hybrid EF-1 not only preserves the individual properties of the parent peptides, but also acquires the ability to disrupt Gram-negative bacterial membrane. Meanwhile, such an expression system can reduce both the time and cost for large-scale peptide production, which ensures its potential application at the industrial level.

SUBMITTER: Li Z 

PROVIDER: S-EPMC7728367 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Expression of Hybrid Peptide EF-1 in <i>Pichia pastoris</i>, Its Purification, and Antimicrobial Characterization.

Li Zhongxuan Z   Cheng Qiang Q   Guo Henan H   Zhang Rijun R   Si Dayong D  

Molecules (Basel, Switzerland) 20201126 23


EF-1 is a novel peptide derived from two bacteriocins, plantaricin E and plantaricin F. It has a strong antibacterial activity against <i>Escherichia coli</i> and with negligible hemolytic effect on red blood cells. However, the chemical synthesis of EF-1 is limited by its high cost. In this study, we established a heterologous expression of EF-1 in <i>Pichia pastoris</i>. The transgenic strain successfully expressed hybrid EF-1 peptide, which had a molecular weight of ~5 kDa as expected. The re  ...[more]

Similar Datasets

| S-EPMC3838785 | biostudies-literature
| S-EPMC3319225 | biostudies-literature
| S-EPMC4093532 | biostudies-literature
| S-EPMC3907806 | biostudies-literature
| S-EPMC4460660 | biostudies-literature
| S-EPMC3317727 | biostudies-literature
| S-EPMC3288236 | biostudies-literature
| S-EPMC4724736 | biostudies-literature
| S-EPMC3989067 | biostudies-literature
| S-EPMC4926436 | biostudies-literature