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. 2005 Jan;71(1):554-7.
doi: 10.1128/AEM.71.1.554-557.2005.

Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526

Koji Yamazaki  1 , Minako Suzuki, Yuji Kawai, Norio Inoue, Thomas J Montville
Affiliations

Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526

Koji Yamazaki et al. Appl Environ Microbiol. 2005 Jan.

Abstract

The bacteriocin piscicocin CS526 was inactivated by proteolytic enzymes, was stable at 100 degrees C for 30 min, had a pH range of 2 to 8, and was active against Enterococcus, Listeria, Pediococcus, and Leuconostoc. The N-terminal sequence was YGNGL, not the YGNGV consensus motif common in class IIa bacteriocins (alternate residues underlined). The molecular mass of piscicocin CS526, which had a bactericidal mode of action, was approximately 4,430 Da.

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Figures

FIG. 1.
FIG. 1.
Survivor curve of L. monocytogenes IID581 (circles) and E. hirae JCM8729 (triangles) in the presence of piscicocin CS526. The concentrations of the bacteriocin were 0 (open symbols) and 600 (closed symbols) AU/ml.
FIG. 2.
FIG. 2.
Purification of piscicocin CS526 by gel filtration (A), cation-exchange (B) and RP-HPLC (C), and antibacterial detection SDS-PAGE of piscicocin CS526 (D). Purified piscicocin CS526 was analyzed by SDS-PAGE. The gel was removed and cut into two parts. The first half, containing molecular weight markers (lane 1) and the purified piscicocin CS526 (lane 2), was stained with silver. The other half, containing the purified bacteriocin (lane 3), was overlaid with L. monocytogenes IID581 and incubated at 30°C for 24 h. The arrows indicate the bacteriocin activities.
FIG. 3.
FIG. 3.
Electrospray ionization mass spectrometry analysis of purified piscicocin CS526.
See this image and copyright information in PMC

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