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Applied and Environmental Microbiology, January 2005, p. 554-557, Vol. 71, No. 1
0099-2240/05/$08.00+0 doi:10.1128/AEM.71.1.554-557.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Purification and Characterization of a Novel Class IIa Bacteriocin, Piscicocin CS526, from Surimi-Associated Carnobacterium piscicola CS526
Koji Yamazaki,1*
Minako Suzuki,1
Yuji Kawai,1
Norio Inoue,1 and
Thomas J. Montville2
Laboratory of Marine Food Science, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Japan,1
Department of Food Science, Cook College, Rutgers, The State University of New Jersey, New Brunswick, New Jersey2
Received 3 March 2004/
Accepted 29 August 2004
The bacteriocin piscicocin CS526 was inactivated by proteolytic enzymes, was stable at 100°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
4,430 Da.
* Corresponding author. Mailing address: Laboratory of Marine Food Science, Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato, Hakodate 041-8611, Japan. Phone: 81-138-40-5574. Fax: 81-138-40-5573. E-mail:
yamasaki{at}fish.hokudai.ac.jp.
Applied and Environmental Microbiology, January 2005, p. 554-557, Vol. 71, No. 1
0099-2240/05/$08.00+0 doi:10.1128/AEM.71.1.554-557.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
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