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Purification and cloning of piscicolin 61, a bacteriocin fromCarnobacterium piscicola LV61

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Abstract

Piscicolin 61, a bacteriocin produced byCarnobacterium piscicola LV61, inhibits the growth of strains ofCarnobacterium, Lactobacillus, andEnterococcus. The bacteriocin was purified to homogeneity by ammonium sulfate precipitation and sequential hydrophobic interaction and reversed-phase chromatography. The N-terminal amino acid sequence of piscicolin 61 was determined by Edman degradation. The plasmid-located structural gene encoding piscicolin (psc61) was cloned and sequenced. It encoded a primary translation product of 71 amino acid residues, which is cleaved between amino acid residues 18 and 19 to yield the active bacteriocin. The calculatedM r from the deduced protein sequence, 5052.6, agreed with that obtained by mass spectrometry. Piscicolin 61 did not show any sequence similarities to other known bacteriocins. However, the leader sequence resembled those of the pediocin-like bacteriocins. Piscicolin 61 may be able to form amphiphilic helices and may thus act on the membrane of sensitive cells.

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Holck, A.L., Axelsson, L. & Schillinger, U. Purification and cloning of piscicolin 61, a bacteriocin fromCarnobacterium piscicola LV61. Current Microbiology 29, 63–68 (1994). https://doi.org/10.1007/BF01575750

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