| Summary: | <i>Pantoea dispersa</i> W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including <i>Mycobacterium tuberculosis</i>, an important human pathogen. Here, the anti-mycobacterial compound produced by <i>Pantoea dispersa</i> W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from <i>Pantoea dispersa</i> W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2−12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of <i>Pantoea dispersa</i>.
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