Purification and characterization of plantaricin Y, a novel bacteriocin produced by Lactobacillus plantarum 510

• Published in: Archives of microbiology Vol. 196; no. 3; pp. 193 - 199
• Main Authors: Chen, Yi-sheng, Wang, Yan-chong, Chow, Yiou-shing, Yanagida, Fujitoshi, Liao, Chen-chung, Chiu, Chi-ming
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.03.2014; Springer Nature B.V
• Subjects: Amino Acid Sequence; Amino acids; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - isolation & purification; Anti-Bacterial Agents - pharmacology; Bacteria; Bacteriocins - chemistry; Bacteriocins - isolation & purification; Bacteriocins - metabolism; Bacteriocins - pharmacology; Biochemistry; Biomedical and Life Sciences; Biotechnology; Cell Biology; Chromatography; Ecology; Endopeptidase K - metabolism; Enzymes; Hot Temperature; Japan; Lactobacillus plantarum; Lactobacillus plantarum - chemistry; Lactobacillus plantarum - genetics; Life Sciences; Listeria; Listeria monocytogenes; Listeria monocytogenes - drug effects; Listeria monocytogenes - metabolism; Mass Spectrometry; Microbial Ecology; Microbiology; Molecular Weight; Original Paper; Peptides; Wineries & vineyards; Japan; United States > US; Taiwan; Plantaricin; Lactic acid bacteria; Bacteriocin
• ISSN: 0302-8933; 1432-072X
• DOI: 10.1007/s00203-014-0958-2

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, NH 2 - 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.