T. Kabuki et al., PRODUCTION, PURIFICATION AND CHARACTERIZATION OF REUTERICIN-6, A BACTERIOCIN WITH LYTIC ACTIVITY PRODUCED BY LACTOBACILLUS-REUTERI LA6, International journal of food microbiology, 34(2), 1997, pp. 145-156
A bacteriocin (Reutericin 6) produced by Lactobacillis reuteri LA6, wa
s purified by hydrophobic chromatography from the modified MRS broth (
D'-MRS) with 6180-fold increase in specific activity with 14% recovery
. The molecular weight of reutericin 6 was determined to be 2.7 kDa by
SDS-PAGE and ESI-MS. By amino acid analysis, reutericin 6 comprised o
f 67% hydrophobic and polar neutral amino acids. Lanthionine was not d
etected. The lytic activity against Lactobacillus delbruekii subsp. bu
lgaricus JCM 1002(T) and NIAI B6 was detected by the decrease of both
turbidity and the number of viable cells, and by leaking of beta-galac
tosidase.