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J Gen Microbiol. 1992 Dec;138(12):2715-20.

Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706.

Author information

1
MATFORSK, Norwegian Food Research Institute, As.

Abstract

Sakacin A, a bacteriocin produced by Lactobacillus sake Lb706 and which inhibits the growth of Listeria monocytogenes, was purified to homogeneity by ammonium sulphate precipitation and ion-exchange, hydrophobic-interaction and reversed-phase chromatography. The complete amino acid sequence of sakacin A was determined by Edman degradation. The bacteriocin consisted of 41 amino acid residues and had a calculated M(r) of 4308.7, which is in good agreement with the value determined by mass spectrometry. The structural gene encoding sakacin A (sakA) was cloned and sequenced. The gene encoded a primary translation product of 59 amino acid residues which was cleaved between amino acids 18 and 19 to yield the active sakacin A. Sakacin A shared some sequence similarities with other bacteriocins.

PMID:
1487735
DOI:
10.1099/00221287-138-12-2715
[Indexed for MEDLINE]

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