A Novel Bacteriocin Against From Isolated From Tilapia Intestine: Purification, Antibacterial Properties and Antibiofilm Activity.

Few bacteriocins with antibacterial activity against have been reported. Here, a novel bacteriocin () produced by strain LF-8 from the intestine of tilapia was purified and extensively characterized. possesses a molecular weight of 1049.56 Da and an amino acid sequence of I-T-G-G-P-A-V-V-H-Q-A. significantly inhibited strain 14 (_14) growth. Moreover, it exhibited excellent stability under heat and acid-base stress, and presented sensitivity to a variety of proteases, such as proteinase K, pepsin, and trypsin. The minimum inhibitory concentration (MIC) of against _14 was 12.65 μg/mL, which was smaller than that of most of the previously found bacteriocins. Furthermore, significantly inhibited ( < 0.05) _14 cells and decreased their cell viability. In addition, could significantly ( < 0.05) inhibit biofilm formation of _14. Scanning electron microscopy analysis presented that the cell membrane permeability of _14 was demolished by , leading to cytoplasmic contents leakage and cell rupture death. In summary, a novel bacteriocin of lactic acid bacteria (LAB) was found, which could effectively control in both planktonic and biofilm states.