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Purification and characterization of plantaricin Y,a novel bacteriocin produced by Lactobacillus plantarum 510 |
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| Authors: | Yi-sheng Chen Yan-chong Wang Yiou-shing Chow Fujitoshi Yanagida Chen-chung Liao Chi-ming Chiu |
| Institution: | 1. Department of Biotechnology, Ming Chuan University, No. 5 De-Ming Rd., Gui-Shan Township, Taoyuan, 333, Taiwan 2. The Institute of Enology and Viticulture, University of Yamanashi, 1-13-1 Kitashin, Kofu, Yamanashi, 400-0005, Japan 3. Proteomics Research Center, National Yang-Ming University, Taipei, 11221, Taiwan |
| Abstract: | Lactobacillus plantarum 510, previously isolated from a koshu vineyard in Japan, was found to produce a bacteriocin-like inhibitory substance which was purified and characterized. Mass spectrometry analysis showed that the mass of this bacteriocin is 4,296.65 Da. A partial sequence, NH2- SSSLLNTAWRKFG, was obtained by N-terminal amino acid sequence analysis. A BLAST search revealed that this is a unique sequence; this peptide is thus a novel bacteriocin produced by Lactobacillus plantarum 510 and was termed plantaricin Y. Plantaricin Y shows strong inhibitory activity against Listeria monocytogenes BCRC 14845, but no activity against other pathogens tested. Bacteriocin activity decreased slightly after autoclaving (121 °C for 15 min), but was completely inactivated by protease K. Furthermore, trypsin-digested bacteriocin product fragments retained activity against L. monocytogenes BCRC 14845 and exhibited a different inhibitory spectrum. |
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