Lactobacillus buchneri LB isolated from a commercially fermented vegetable product produced a bacteriocin-designated buchnericin LB. It was found that buchnericin LB was heat-stable (90-121oC for 15 min) and hydrolyzed by proteases, a-chymotrypsin, trypsin, papain, proteinase K and pepsin. However, it was observed that it was resistant to catalase, peroxidase, lipase, amylases and organic solvents. Also, it was found that it retained its biological activity after exposure to pH 2.0-9.0 and after storage at -20o and -70oC. It was determined that buchnericin LB had a wide inhibitory spectrum, being inhibitory to the Listeria, Bacillus, Enterococcus, Micrococcus, Lactobacillus, Leuconostoc, Pediococcus, and Streptococcus species tested, and its molecular weight was determined to be about 3.5-4.5 kDa by tricine-SDS-PAGE.

Lactobacillus buchneri LB isolated from a commercially fermented vegetable product produced a bacteriocin-designated buchnericin LB. It was found that buchnericin LB was heat-stable (90-121oC for 15 min) and hydrolyzed by proteases, a-chymotrypsin, trypsin, papain, proteinase K and pepsin. However, it was observed that it was resistant to catalase, peroxidase, lipase, amylases and organic solvents. Also, it was found that it retained its biological activity after exposure to pH 2.0-9.0 and after storage at -20o and -70oC. It was determined that buchnericin LB had a wide inhibitory spectrum, being inhibitory to the Listeria, Bacillus, Enterococcus, Micrococcus, Lactobacillus, Leuconostoc, Pediococcus, and Streptococcus species tested, and its molecular weight was determined to be about 3.5-4.5 kDa by tricine-SDS-PAGE.