Abstract:
A marine bacterium (KMM 1364), identified as Bacillus pumilus, was isolated from the surface of ascidian Halocynthia aurantium. Structural analysis revealed that the strain KMM 1364 produced a mixture of lipopeptide surfactin analogs with major components with molecular masses of 1035, 1049, 1063, and 1077. The variation in molecular weight represents changes in the number of methylene groups in the lipid and/or peptide portions of the compounds. Structurally, these lipopeptides differ from surfactin in the substitution of the valine residue in position 4 by leucine, and have been isolated as two carboxy-terminal variants, with valine or isoleucine in position 7. As constituents of the lipophilic part of the peptides, only β-hydroxy-C15-, β-hydroxy-C16-, and a high amount of β-hydroxy-C17 fatty acid were determined.
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Kalinovskaya, N., Kuznetsova, T., Ivanova, E. et al. Characterization of Surfactin-like Cyclic Depsipeptides Synthesized by Bacillus pumilus from Ascidian Halocynthia aurantium . Mar. Biotechnol. 4, 179–188 (2002). https://doi.org/10.1007/s10126-001-0084-4
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DOI: https://doi.org/10.1007/s10126-001-0084-4