Reference : Dynamic And Equilibrium Surface Tensions Of Surfactin Aqueous Solutions
Scientific journals : Article
Physical, chemical, mathematical & earth Sciences : Chemistry
http://hdl.handle.net/2268/61168
Dynamic And Equilibrium Surface Tensions Of Surfactin Aqueous Solutions
English
Razafindralambo, Hary [Université de Liège > > Gembloux Agro-Bio Tech >]
Thonart, Philippe mailto [Université de Liège > > Gembloux Agro-Bio Tech >]
Paquot, Michel mailto [Université de Liège - ULg > Chimie et bio-industries > Chimie biologique industrielle >]
2004
Journal of Surfactants and Detergents
7
1
41-46
Yes (verified by ORBi)
International
1097-3958
1558-9293
[en] Biosurfactant, dynamic surface tension, homologous series, micelles, surfactins
[en] A homologous series of surfactins containing β-hydroxy fatty acids having 13, 14, or 15 carbon atoms were isolated from the supernatant of Bacillus subtilis strain S499 cultures. Their surface-active properties at the air-water interface were then evaluated. Dynamic surface tension data were analyzed by the relaxation function γt=γm+(γo−γm)/[1+(t/t*)n]. Based on various parameters t*, n, vmax, γm calculated from this equation, the dynamic surface properties of surfactin were found to depend on both bulk concentration and hydrophobic character of the alkyl chain. At low concentrations of surfactin, the dynamic surface tension (γd) decreased with increasing carbon atom number of the surfactin alkyl chain (n=13 to 15). However, at high concentrations, the maximum decrease of 41-4 was achieved by surfactin-C14. In contrast, more strongly hydrophobic alkyl chains in surfactins always enhanced their ability in reducing the equilibrium surface tensions and their aptitude in forming micelles.
http://hdl.handle.net/2268/61168
also: http://hdl.handle.net/2268/22476
10.1007/s11743-004-0286-x

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
Razafindralambo-H_2004_JSD.pdfPublisher postprint146.01 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.