title: Isolation and partial amino acid sequence of bacteriocins produced by Lactobacillus acidophilus.
abstract: Bacteriocins produced by Lactobacillus acidophilus JCM 1023, JCM 1028, JCM 1021, JCM 1229, and JCM 5342 were active against closely related lactobacilli. These bacteriocins were purified and partial sequenced. Bacteriocin activities of L. acidophilus JCM 1023 and JCM 1028 were associated with two components. On the basis of N-terminal amino acid sequencing and the molecular masses, it is interpreted that these two-component bacteriocins are identical to acidocin J1132, a bacteriocin from L. acidophilus JCM 1132 [Tahara et al., Appl. Environ. Microbiol., 62, 892-897 (1996)]. Other bacteriocins were single-peptide bacteriocins.
authors.affiliation: Research Laboratory, Tamon Sake Brewing Co., Ltd., Hyogo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Tahara
authors.forename: K
authors.initials: K
authors.lastname: Kanatani
mesh_terms: D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000737:chemistry / Q000302:isolation & purification*; D007778:Lactobacillus / Q000187:drug effects* / Q000254:growth & development; D007779:Lactobacillus acidophilus / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013045:Species Specificity
chemical_list: D001430:Bacteriocins