TY  - JOUR
A1  - Rojas, Oscar
A1  - Tiersch, Brigitte
A1  - Rabe, Christian
A1  - Stehle, Ralf
A1  - Hoell, Armin
A1  - Arlt, Bastian
A1  - Koetz, Joachim
T1  - Nonaqueous Microemulsions Based on N,N '-Alkylimidazolium Alkylsulfate Ionic Liquids
JF  - Langmuir
N2  - The ternary system composed of the ionic liquid surfactant (IL-S) 1-butyl-3-methylimidazolium dodecylsulfate ([Bmim][DodSO(4)]), the room temperature ionic liquid (RTIL) 1-ethyl-3-methylimidazolium ethylsulfate ([Emim][EtSO4]), and toluene has been investigated. Three major mechanisms guiding the structure of the isotropic phase were identified by means of conductometric experiments, which have been correlated to the presence of oil-in-IL, bicontinuous, and IL-in-oil microemulsions. IL-S forms micelles in toluene, which swell by adding RTIL as to be shown by dynamic light scattering (DLS) and small-angle X-ray scattering (SAXS) experiments. Therefore, it is possible to form water free IL-in-oil reverse microemulsions <= 10 nm in size as a new type of nanoreactor.
Y1  - 2013
U6  - https://doi.org/10.1021/la401080q
SN  - 0743-7463
VL  - 29
IS  - 23
SP  - 6833
EP  - 6839
PB  - American Chemical Society
CY  - Washington
ER  - 
TY  - JOUR
A1  - Wellert, Stefan
A1  - Tiersch, Brigitte
A1  - Koetz, Joachim
A1  - Richardt, Andre
A1  - Lapp, Alain
A1  - Holderer, Olaf
A1  - Gaeb, Juergen
A1  - Blum, Marc-Michael
A1  - Schulreich, Christoph
A1  - Stehle, Ralf
A1  - Hellweg, Thomas
T1  - The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions  structure, dynamics, and enzyme activity
JF  - European biophysics journal : with biophysics letters ; an international journal of biophysics
N2  - The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris is of great interest because of its ability to catalyze the hydrolysis of highly toxic organophosphates. In this work, the enzyme structure in solution (native state) was studied by use of different scattering methods. The results are compared with those from hydrodynamic model calculations based on the DFPase crystal structure. Bicontinuous microemulsions made of sugar surfactants are discussed as host systems for the DFPase. The microemulsion remains stable in the presence of the enzyme, which is shown by means of scattering experiments. Moreover, activity assays reveal that the DFPase still has high activity in this complex reaction medium. To complement the scattering experiments cryo-SEM was also employed to study the microemulsion structure.
KW  - Dynamic light scattering
KW  - Neutron spin echo
KW  - Microemulsion
KW  - Enzyme catalysis
KW  - SANS
KW  - Protein structure
Y1  - 2011
U6  - https://doi.org/10.1007/s00249-011-0689-0
SN  - 0175-7571
VL  - 40
IS  - 6
SP  - 761
EP  - 774
PB  - Springer
CY  - New York
ER  -