Isolation and Partial Amino Add Sequence of Bacteriocins Produced by Lactobacillus acidophilus | Zendy

Takatsugu Tahara | Zendy; Kazuo Kanatani | Zendy

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Isolation and Partial Amino Add Sequence of Bacteriocins Produced by Lactobacillus acidophilus

Author(s) -

Takatsugu Tahara,

Kazuo Kanatani

Publication year - 1997

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.61.884

Subject(s) - bacteriocin , lactobacillus acidophilus , microbiology and biotechnology , isolation (microbiology) , bacteria , peptide , molecular mass , peptide sequence , biology , chemistry , biochemistry , probiotic , antimicrobial , enzyme , gene , genetics

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.

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