Lactococcal membrane-permeabilizing antimicrobial peptides.
A number of lactococcal antimicrobial peptides, bacteriocins have been discovered and characterized. Since Lactococcus spp. are generally regarded as safe bacteria, their bacteriocins are expected for various application uses. Most of lactococcal bacteriocins exert antimicrobial activity via membrane permeabilization. The most studied and prominent bacteriocin, nisin A is characterized in the high activity and has been utilized as food preservatives for more than half a century. Recently, other lactococcal bacteriocins such as lacticin Q were found to have distinguished features for further applications as the next generation to nisin.
Zendo
Takeshi
T
Laboratory of Microbial Technology, Division of Applied Molecular Microbiology and Biomass Chemistry, Department of Bioscience and Biotechnology, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, 812-8581, Japan.
Yoneyama
Fuminori
F
Sonomoto
Kenji
K
D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology*; D001430:Bacteriocins / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology*; D002463:Cell Membrane Permeability / Q000187:drug effects*; D015964:Gene Expression Regulation, Bacterial; D017045:Lactococcus / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D010455:Peptides