Confirmation of the Structure of Surfactin by Mass Spectrometry

Kakinuma, Atsushi; OUCHIDA, Akira; Shima, Takashi; Sugino, Hiromu; Isono, Masao; Tamura, Gakuzo; Arima, Kei

doi:10.1271/bbb1961.33.1669

Cited by 66 publications

(38 citation statements)

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“…The molecular mass and identities of each fraction, as determined by MALDI-TOF mass spectra analysis, are summarized in Table 3. Comparing the mass data obtained for individual fractions and the mass numbers reported for the lipopeptide complexes from other B. subtilis strains [19,[26][27][28][29][30][31][32], the major lipopeptide products of B. subtilis DM-03 could be identified as iturins (C 16 -C 19 ) and surfactins (C 13 -C 15, ) whereas the major lipopeptide isoforms of B. subtilis DM-04 were iturins (C 17 -C 18 ) and surfactins (C 13 -C 15 ). The isoforms of these CLPs were resolved on the basis of their hydrophobicities, which in turn were determined mainly by the length of the fatty acid chains of lipopeptides [19]; therefore iturin isoforms were eluted first from the C 18 -l Nova pak RP-HPLC column followed by surfactin isoforms.…”

Section: Isolation and Purification Of Biosurfactantsmentioning

confidence: 90%

Correlation between diverse cyclic lipopeptides production and regulation of growth and substrate utilization by Bacillus subtilis strains in a particular habitat

Mukherjee

Das

2005

FEMS Microbiology Ecology

140

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The two Bacillus subtilis strains (DM-03 and DM-04) were isolated from two extremely different habitats; one from the traditional fermented food and another one from a petroleum contaminated soil sample. These strains produced quantitatively and qualitatively different cyclic lipopeptides isoforms under laboratory culture conditions. MALDI-TOF mass spectral analysis revealed that lipopeptide profile varied according to the producing B. subtilis strains; iturins and surfactins isoforms were pre-dominant cyclic lipopeptides produced by B. subtilis DM-03 and DM-04 strains, respectively. A comparative study showed that these strains possessed distinct preferences for the carbon and nitrogen substrates, temperature and pH for optimal growth and biosurfactant production. Our study documented that the cyclic lipopeptide isoforms produced by the respective strains played an important role in the utilization of available hydrophobic substrate(s) from their natural habitats and conferred some kind of competitive advantage to the producing B. subtilis strains in their parent ecological niche.

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Section: Isolation and Purification Of Biosurfactantsmentioning

confidence: 90%

Correlation between diverse cyclic lipopeptides production and regulation of growth and substrate utilization by Bacillus subtilis strains in a particular habitat

Mukherjee

Das

2005

FEMS Microbiology Ecology

140

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“…The asterisks (*) indicate m/z values not detected in our cases. calculations, the chain length of the fatty acid side chains varied in the range of [13][14][15] (Table 1). Interestingly, C15-[Val7] was present in the highest amount among the produced surfactins based on the peak area of the sodiated adducts on the extracted ion current chromatograms (Fig.…”

Section: Characterisation Of the Produced Surfactin Isoformsmentioning

confidence: 99%

**Ion trap mass spectrometry of surfactins produced by Bacillus subtilis SZMC 6179J reveals novel fragmentation features of cyclic lipopeptides**

Bóka

László

Kecskeméti

et al. 2016

Rapid Comm Mass Spectrometry

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The detected new natural lipoheptapeptide compounds with modified structures have significant potential for biotechnological and biocontrol applications. The complementary ITMS(2) data as well as the described internal fragmentation mechanism obtained from the sodiated surfactin molecules may further facilitate the structural elucidation of cyclic lipopeptides in the future. Copyright © 2016 John Wiley & Sons, Ltd.

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“…Among these, iturins are the most widely reported class of lipopeptides produced by multiple strains of Bacillus subtilis (Duitman et al 1999; Isogai et al 1982; Peypoux et al 1986), B . licheniformis (Kakinuma et al 1969; Yakimov et al 1999; Jenny et al 1991; Lin et al 1994) and B . cereus (Nishikiori et al 1986).…”

Section: Introductionmentioning

confidence: 99%

Characterization of two antimicrobial peptides produced by a halotolerant Bacillus subtilis strain SK.DU.4 isolated from a rhizosphere soil sample

et al. 2013

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A bacterial strain producing two antimicrobial peptides was isolated from a rhizosphere soil sample and identified as Bacillus subtilis based on both phenotypic and 16S rRNA gene sequence phylogenetic analysis. It grew optimally up to 14% NaCl and produced antimicrobial peptide within 24 h of growth. The peptides were purified using a combination of chemical extraction and chromatographic techniques. The MALDI-TOF analysis of HPLC purified fractions revealed that the strain SK.DU.4 secreted a bacteriocin-like peptide with molecular mass of 5323.9 Da and a surface-active lipopeptide (m/z 1056 Da). The peptide mass fingerprinting of low-molecular-weight bacteriocin exhibited significant similarity with stretches of secreted lipoprotein of Methylomicrobium album BG8 and displayed 70% sequence coverage. MALDI MS/MS analysis elucidated the lipopeptide as a cyclic lipopeptide with a β-hydroxy fatty acid linked to Ser of a peptide with seven α-amino acids (Asp-Tyr-Asn-Gln-Pro-Asn-Ser) and assigned it to iturin-like group of antimicrobial biosurfactants. However, it differed in amino acid composition with other members of the iturin family. Both peptides were active against Gram-positive bacteria, suggesting that they had an additive effect.

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Confirmation of the Structure of Surfactin by Mass Spectrometry

Cited by 66 publications

References 0 publications

Correlation between diverse cyclic lipopeptides production and regulation of growth and substrate utilization by Bacillus subtilis strains in a particular habitat

Correlation between diverse cyclic lipopeptides production and regulation of growth and substrate utilization by Bacillus subtilis strains in a particular habitat

**Ion trap mass spectrometry of surfactins produced by Bacillus subtilis SZMC 6179J reveals novel fragmentation features of cyclic lipopeptides**

Characterization of two antimicrobial peptides produced by a halotolerant Bacillus subtilis strain SK.DU.4 isolated from a rhizosphere soil sample

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