The bacteriocin produced by Lactobacillus sp. GM7311 was purified by sequential steps including n-propanol/acetone treatment, CM-cellulose chromatography, and gel filtration on Sephacryl HR-100. The relative activity of bacteriocin increased 493-fold after final purification step with a recovery of 8.3%. Two protein bands of ca. 8,200 and 2,500 were detected by SDS-PAGE of bacteriocin purified through CM-cellulose and sephacryl HR-100 chromatography and both of them had bacteriocin activity.