I1774
Iturin A from Bacillus subtilis
≥95% (HPLC), suitable for microbiological culture
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product name
Iturin A from Bacillus subtilis, ≥95% (HPLC)
biological source
Bacillus subtilis
Quality Level
Assay
≥95% (HPLC)
form
powder
technique(s)
microbiological culture: suitable
color
white to yellow
solubility
ethanol: soluble 9.80-10.20 mg/mL
antibiotic activity spectrum
fungi
Mode of action
cell membrane | interferes
storage temp.
2-8°C
Application
Iturin A was used in the study of Bacillomycin D (an iturin with antifungal activity against Aspergillus flavus).
Biochem/physiol Actions
IturinA exhibits strong antifungal activity against pathogenic yeast and fungi. It interacts with the cytoplasmic membrane of the target cell forming ion conducting pores. Its mode of action could be attributed to its interaction with sterols and phospholipids. The compound causes the release of exo-vesicles from human erythrocytes.
Other Notes
A family of lipopeptides characterized by a heptapeptide cyclized with a C13-C17 β-amino fatty acid. Composed mainly of C14-C15 β-amino acids.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Scott W Pryor et al.
Journal of agricultural and food chemistry, 55(23), 9530-9536 (2007-10-24)
Partial least squares (PLS) regression modeling was used to relate the antifungal activity of Bacillus subtilis solid-state fermentation extracts to the individual high-performance liquid chromatography (HPLC) peaks from those extracts. A model was developed that predicted bioassay inhibition based on
M A Klich et al.
Mycopathologia, 127(2), 123-127 (1994-08-01)
The removal of many synthetic fungicides from the market has created a demand for new, environmentally safe fungicides. Iturin A, a cyclic lipopeptide produced by Bacillus subtilis, has strong antifungal properties and low mammalian toxicity. To determine the efficacy of
R Maget-Dana et al.
Toxicology, 87(1-3), 151-174 (1994-02-28)
Iturins are a family of lipopeptides extracted from the culture media of various strains of Bacillus subtilis. These amphiphilic compounds are characterized by a peptide ring of seven amino acid residues including an invariable D-Tyr2, with the constant chiral sequence
Thimon, L., et al.
Cytobios, 79, 96-96 (1994)
Nopporn Thasana et al.
FEBS letters, 584(14), 3209-3214 (2010-06-15)
Subtulene A, a new cyclic lipopeptide, was isolated from the culture broth of Bacillus subtilis SSE4. This antibiotic compound contained the seven common alpha-amino acids, L-Asn-1, D-Tyr-2, D-Asn-3, L-Gln-4, L-Pro-5, D-Asn-6, L-Ser-7 and the unique beta-amino acid-8 present in the
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