Expression and antimicrobial activity of the recombinant bovine lactoferricin in Pichia pastoris.

ABSTRACT: Lactoferricin, a multifunctional peptide located in the N-terminal region of lactoferrin, has a broad-spectrum bacteriostatic activity. It is a promising candidate as a food additive and immune fortification agent and does not have the risks associated with drug residues and drug resistance. First, we performed promoter and host cell screening to achieve the recombinant expression of lactoferricin in Pichia pastoris, showing an initial titer of 19.5 mg/L in P. pastoris X-33 using P_AOX1 promoter. Second, we constructed a 0030-α hybrid signal peptide by fusing the 0030 signal peptide with the pro-sequence of α-factor secretory signal peptide. This further increased the production of lactoferricin, with a titer of 28.8 mg/L in the fermentation supernatan

SUBMITTER: Lv X 

PROVIDER: S-EPMC10787256 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature