Open AccessIsolation and partial characterization of bacteriocins produced by Lactobacillus gasseri JCM 2124
Author(s) -
Tahara Takatsugu,
Yoshioka Sachiko,
Utsumi Ryutaro,
Kanatani Kazuo
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10273.x
Subject(s) - bacteriocin , lactobacillus gasseri , peptide , complementation , molecular mass , chemistry , isolation (microbiology) , peptide sequence , lantibiotics , lactobacillus acidophilus , microbiology and biotechnology , amino acid , lactobacillus , biochemistry , mass spectrometry , biology , bacteria , fermentation , chromatography , antimicrobial , probiotic , genetics , gene , enzyme , phenotype
Four antibacterially active peptides (B1 to B4) were purified from the culture broth of L. gasseri JCM 2124. The B2 peptide (gassericin B2) was determined to be 4400 Da by mass spectrometry and partially sequenced. Gassericin B2 did not show any sequence similarities to other known bacteriocins. The B1 and B3 peptides shared identical sequences with two peptides of a two‐component bacteriocin from Lactobacillus acidophilus . However, synergistic activity upon complementation of B1 and B3 was not observed. Based on amino acid sequencing and molecular mass, it is suggested that B1 and B4 peptides were derived from B3 (gassericin B3).