Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Isolation and Partial Amino Acid Sequence of Bacteriocins Produced by Lactobacillus acidophilus
Takatsugu TAHARAKazuo KANATANI
Author information
JOURNAL FREE ACCESS

1997 Volume 61 Issue 5 Pages 884-886

Details
Abstract

Bacteriocins produced by Lactobacillus acidophilus JCM 1023, JCM 1028, JCM 1021, JCM 1229, and JCM 5342 were active against closely related lattobacilli. 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 tbe 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.

Content from these authors

This article cannot obtain the latest cited-by information.

© Japan Society for Bioscience, Biotechnology, and Agrochemistry
Previous article Next article
feedback
Top