Bacteriocin was maximally produced by Pediococcus pentosaceus KC-007 in the late exponential phase in MRS broth. The activity of bacteriocin was completely inactivated by proteinase K, trypsin, chymotrypsin, pepsin, and subtilisin A, but not by catalase, lysozyme, lipase, ribonuclease A, and alpha-amylase. Furthermore, its activity was not affected by pH changes ranging from 2 to 8 and heat treatment at 100 o C for 60 min or autoclaving. The activity of bacteriocin remained after treatment of organic solvents or detergent such as acetone, chloroform, ethanol, hexane, isopropanol, methanol, SDS, or Tween 20. Therefore, the bacteriocin isolated in this study could be used for a food preservative due to its growth inhibition against Bacillus cereus, Escherichia coli O157-H7, and Listeria monocytogenes.