Abstract: Antibacterial peptides are expected to replace antibiotics and become a safe, green and efficient ideal antibacterial agent. Bovine lactoferricin(LFcinB) is a kind of short peptide with broad spectrum antibacterial activity produced via hydrolysis of lactoferrin by digestive enzymes. Based on LFcinB, the derivative peptide LFcinB-W was obtained by optimizing the structure of LFcinB according to the relationship between structure and function of antibacterial peptide. The recombinant expression vector was constructed by combining LFcinB-W gene fragment with pPIC9K plasmid, and transformed into Pichia pastoris GS115 cells to induce expression. The fermentation supernatants were separated, purified and tested for antibacterial activity, and the results showed that the peptide had stronger antibacterial activity against Staphylococcus aureus, Escherichia coli and Bacillus subtilis. The model organism Drosophila gut was infected by the pathogen Erwinia carotovora carotovora 15(Ecc15) to investigate the protective effect of LFcinB-W on the infection model, and the results indicated that LFcinB-W could effectively alleviate the damage caused by pathogen infection in Drosophila and showed better anti-infection effect than LFcinB, providing reference for the further study of the biological activity and production and application of LFcinB-W.
Keywords: bovine lactoferricin(LFcinB); structure design; Drosophila; anti-infection effect
合肥工业大学学报自科版