Identification, Recombinant Expression, and Characterization of LHG2, a Novel Antimicrobial Peptide of Lactobacillus casei HZ1.

ABSTRACT: L. casei HZ1 was identified from Chinese traditional fermented milk, and angiotensin converting enzyme inhibitory peptide was separated from its culture in our previous work. Here, LGH2 was a novel AMP, identified from the genome of L. casei HZ1. Altogether, roughly 52.76% of LGH2 was α -helical, with the remainder in β -strand and random coil in 50% TFE solution tested by CD. The peptide was also an amphipathic and cationic molecule, which was composed of 20 amino acid residues. The similarity of the amino acid sequence between LGH2 and Temporin-RN3 was highest. Then, the peptide successfully expressed in E. coli Rossetta (DE3) pLysS using the SUMO fusion expression system and purified by chromatography technologies. The molecular weight of the peptide was 2448 Da determined by MALDI-TOF

SUBMITTER: He J 

PROVIDER: S-EPMC6225214 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature