Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526.
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.
Yamazaki
Koji
K
Laboratory of Marine Food Science, Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato, Hakodate 041-8611, Japan. yamasaki@fish.hokudai.ac.jp
Suzuki
Minako
M
Kawai
Yuji
Y
Inoue
Norio
N
Montville
Thomas J
TJ
D000595:Amino Acid Sequence; D000818:Animals; D001430:Bacteriocins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D005396:Fish Products / Q000382:microbiology*; D006094:Gram-Positive Bacteria / Q000302:isolation & purification / Q000378:metabolism*; D006095:Gram-Positive Cocci / Q000187:drug effects; D008087:Listeria / Q000187:drug effects; D008969:Molecular Sequence Data
D001430:Bacteriocins