Satisfactory separation and MS-MS spectrometry of six surfactins isolated from Bacillus subtilis natto.

Oka, Kitaro; Hirano, Toshihiko; Homma, Masato; Ishii, Hiromitsu; Murakami, Kiyotaka; Mogami, Satoru; Motizuki, Akinori; Morita, Hiroshi; Takeya, Koichi; Itokawa, Hideji

doi:10.1248/cpb.41.1000

Cited by 50 publications

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“…Successive loss of aminoacids has been observed as reported previously (Oka et al 1993;Kim et al 2010; De Faria et al 2011). Moreover, common peaks ions as the internal protonated fragment ion [(H)Leu 2 -Leu 3 -Val 4 -Asp 5 -Leu 6 -Leu/Ile 7 (OH) ?H] ?…”

Section: Discussionsupporting

confidence: 59%

Bacillus subtilis subsp. subtilis CBMDC3f with antimicrobial activity against Gram-positive foodborne pathogenic bacteria: UV-MALDI-TOF MS analysis of its bioactive compounds

Torres

Petroselli

Daz

et al. 2015

World J Microbiol Biotechnol

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In this work a new Bacillus sp. strain, isolated from honey, was characterized phylogenetically. Its antibacterial activity against three relevant foodborne pathogenic bacteria was studied; the main bioactive metabolites were analyzed using ultraviolet matrix assisted laser desorption-ionization mass spectrometry (UV-MALDI MS). Bacillus CBMDC3f was phylogenetically characterized as Bacillus subtilis subsp. subtilis after rRNA analysis of the 16S subunit and the gyrA gene (access codes Genbank JX120508 and JX120516, respectively). Its antibacterial potential was evaluated against Listeria monocytogenes (9 strains), B. cereus (3 strains) and Staphylococcus aureus ATCC29213. Its cell suspension and cell-free supernatant (CFS) exerted significant anti-Listeria and anti-S. aureus activities, while the lipopeptides fraction (LF) also showed anti-B. cereus effect. The UV-MALDI-MS analysis revealed surfactin, iturin and fengycin in the CFS, whereas surfactin predominated in the LF. The CFS from CBMDC3f contained surfactin, iturin and fengycin with four, two and four homologues per family, respectively, whereas four surfactin, one iturin and one fengycin homologues were identified in the LF. For some surfactin homologues, their UV-MALDI-TOF/TOF (MS/MS; Laser Induced Decomposition method, LID) spectra were also obtained. Mass spectrometry analysis contributed with relevant information about the type of lipopeptides that Bacillus strains can synthesize. From our results, surfactin would be the main metabolite responsible for the antibacterial effect.

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Section: Discussionsupporting

confidence: 59%

Bacillus subtilis subsp. subtilis CBMDC3f with antimicrobial activity against Gram-positive foodborne pathogenic bacteria: UV-MALDI-TOF MS analysis of its bioactive compounds

Torres

Petroselli

Daz

et al. 2015

World J Microbiol Biotechnol

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“…Several natural amino acid substitutions within the peptide chains of surfactin, as well as other non-ribosomally synthesized peptide antibiotics, have been described, which are due to a reduction in the substrate speci®city of certain modules (Peypoux et al 1994). In particular, the natural occurrence of a Val to Ala substitution at position 4 (Peypoux et al 1994) and a Leu to Ile or Val exchange at position 7 (Baumgart et al 1991;Peypoux et al 1991, Oka et al 1993 indicate that these positions are not essential for the topology of surfactin Fig. 6 Determination of [2, 3-3 H]Orn incorporation.…”

Section: Discussionmentioning

confidence: 99%

Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping

1998

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Analysis of the primary structure of peptide synthetases involved in the non-ribosomal synthesis of peptide antibiotics has revealed a highly conserved and ordered modular arrangement. A module contains at least two domains, involved in ATP-dependent substrate activation and thioester formation. The occurrence and arrangement of these functional building blocks is associated with the number and order of the amino acids incorporated in the peptide product. In this study, we present data on the targeted exchange of the leucine-activating module within the three-module surfactin synthetase 1 (SrfA-A) of Bacillus subtilis. This was achieved by engineering several hybrid srfA-A genes, which were introduced into the surfactin biosynthesis operon by in vivo recombination. We examined the hybrid genes for expression and investigated the enzymatic activities of the resulting recombinant peptide synthetases. For the first time, we demonstrate directly that an individual minimal module, of bacterial or fungal origin, confers its amino acid-specific activity on a multi-modular peptide synthetase. Furthermore, it is shown that directed incorporation of ornithine at the second position of the peptide chain induces a global alteration in the conformation of surfactin and may result in premature cyclization or a branched cyclic structure.

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“…The complex nature of B. subtilis ATCC 21332 culture broth makes identification and quantification of surfactin difficult. Furthermore, surfactin has different isoforms, which vary in carbon chain length and the peptide sequence (Oka et al 1993) and depend on the bacterial strain, nutritional supply and environmental conditions applied during fermentation (Oka et al 1993). …”

Section: Sensitivitymentioning

confidence: 99%

A Simple and Effective Isocratic HPLC Method for Fast Identification and Quantification of Surfactin

Mubarak

Hassan

Hamid³

et al. 2015

JSM

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Satisfactory separation and MS-MS spectrometry of six surfactins isolated from Bacillus subtilis natto.

Cited by 50 publications

References 0 publications

Bacillus subtilis subsp. subtilis CBMDC3f with antimicrobial activity against Gram-positive foodborne pathogenic bacteria: UV-MALDI-TOF MS analysis of its bioactive compounds

Bacillus subtilis subsp. subtilis CBMDC3f with antimicrobial activity against Gram-positive foodborne pathogenic bacteria: UV-MALDI-TOF MS analysis of its bioactive compounds

Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping

A Simple and Effective Isocratic HPLC Method for Fast Identification and Quantification of Surfactin

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