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Interfacial properties of surfactin
Surfactin is a lipopeptide produced by various strains of Bacillus subtilis and is a very powerful surfactant. Here we present the first report on the interfacial behavior of surfactin. The adsorption, Γ max, of surfactin at the interface of diluted solutions (5 × 10 −8 to 5 × 10 −7 M) is around 3 ×...
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Published in: | Journal of colloid and interface science 1992-10, Vol.153 (1), p.285-291 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Surfactin is a lipopeptide produced by various strains of
Bacillus subtilis and is a very powerful surfactant. Here we present the first report on the interfacial behavior of surfactin. The adsorption,
Γ
max, of surfactin at the interface of diluted solutions (5 × 10
−8 to 5 × 10
−7
M) is around 3 × 10
18 molecule m
−2, a value indicating that surfactin molecules are in a very packed situation. Surfactin spreads readily at the
air
water
interface: the equilibrium spreading pressure
π
e
≈ 30 mN m
−1 reaches 45 mN m
−1 when electrolytes (KCl or CaCl
2) are dissolved in the alkaline subphase. We have plotted the compression isotherm curves and determined surface parameters. These parameters vary only a little with temperature but are very affected by the pH of the subphase. Plotting the transition pressure value π
t as a function of pH results in a titration curve from which one can deduce the p
K value of surfactin at the interface. This value, p
K
s ≈ 6 is around 2 pH units higher than the p
K of surfactin in solution. The addition of electrolytes (
I = 0.15
M) in the alkaline subphase leads to the neutralization of the surfactin monolayer (protonation of the acidic residues LGlu
1 and LAsp
5 of the peptide cycle). This neutralization is complete in the case of Ca
++ ions but not in the case of monovalent cations (Na
+ or K
+). When surfactin monolayers are subjected to successive compression—expansion cycles we observe a reproducible hysteresis loop. The surface parameters of surfactin are compared to those of iturins, lipopeptides also extracted from
B. subtilis, the structure and properties of which are very similar. |
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ISSN: | 0021-9797 1095-7103 |
DOI: | 10.1016/0021-9797(92)90319-H |