TY  - JOUR
A1  - Vargas-Ruiz, Salome
A1  - Schulreich, Christoph
A1  - Kostevic, Angelika
A1  - Tiersch, Brigitte
A1  - Koetz, Joachim
A1  - Kakorin, Sergej
A1  - von Klitzing, Regine
A1  - Jung, Martin
A1  - Hellweg, Thomas
A1  - Wellert, Stefan
T1  - Extraction of model contaminants from solid surfaces by environmentally compatible microemulsions
JF  - Journal of colloid and interface science
N2  - In the present contribution, we evaluate the efficiency of eco-friendly microemulsions to decontaminate solid surfaces by monitoring the extraction of non-toxic simulants of sulfur mustard out of model surfaces. The extraction process of the non-toxic simulants has been monitored by means of spectroscopic and chromatographic techniques. The kinetics of the removal process was analyzed by different empirical models. Based on the analysis of the kinetics, we can assess the influence of the amounts of oil and water and the microemulsion structure on the extraction process. (C) 2016 Elsevier Inc. All rights reserved.
KW  - Microemulsions
KW  - Decontamination
KW  - Surface removal
KW  - Kinetic analysis
KW  - Extraction
Y1  - 2016
U6  - https://doi.org/10.1016/j.jcis.2016.03.006
SN  - 0021-9797
SN  - 1095-7103
VL  - 471
SP  - 118
EP  - 126
PB  - Elsevier
CY  - San Diego
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  -