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Applied and Environmental Microbiology, April 2007, p. 2247-2250, Vol. 73, No. 7
0099-2240/07/$08.00+0 doi:10.1128/AEM.02484-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Institute of Enology and Viticulture, University of Yamanashi, 1-13-1, Kitashin, Kofu, Yamanashi 400-0005, Japan,1 National Health Research Institutes, 35 Keyan Rd., Zhunan Town, Miaoli County 350, Taiwan, Republic of China2
Received 24 October 2006/ Accepted 2 February 2007
Weissella cibaria 110, isolated from the Thai fermented fish product plaa-som, was found to produce a bacteriocin active against some gram-positive bacteria. Bacteriocin activity was not eliminated by exposure to high temperatures or catalase but was destroyed by exposure to the proteolytic enzymes proteinase K and trypsin. The bacteriocin from W. cibaria 110 was purified, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the purified bacteriocin contained one protein band that was approximately 2.5 kDa in size. Mass spectrometry analysis showed the mass of the peptide to be approximately 3,487.8 Da. N-terminal amino acid sequence analysis was performed, and 27 amino acids were identified. Because it has no similarity to other known bacteriocins, this bacteriocin was defined as a new bacteriocin and termed weissellicin 110.
Published ahead of print on 9 February 2007.
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