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An attempt is made to decouple the effects that occur when different electrolytes are added to proteins, especially enzymes, in buffer solutions. In particular, direct molecular ‘chemical’ interactions between ions and specific sites on the enzyme are distinguished from ‘physical’ interactions due to electrostatic and dispersion forces. The latter are often related to a Hofmeister series. It is shown that bulk effects, usually on the pH via a shift of the buffer equilibria, must be separated from direct enzyme–ion interactions. ABTS oxidation with horseradish peroxidase is taken as an example to show how this separation can be done. The different concentration ranges in which these phenomena occur are also discussed. Finally, the influence of ions on a particular enzyme, the NADH oxidase, is compared to their influence on mixed catanionic micelles. The striking similarities can be associated with the structure-making and -breaking behaviour of the ions and a balanced effect for ‘neutral’ Hofmeister ions.

The transition of ionic micelles to vesicles with added salts is explored in this paper. The catanionic surfactant solution was comprised of sodium dodecylsulfate (SDS) and dodecyltrimethylammonium bromide (DTAB) with an excess of SDS. The micellar size increased with concentration for all salts. No anion specificity was found, probably because of the excess of SDS. However, when the cation of the added salt was varied, large differences were observed in the hydrodynamic radii of the aggregates. A classification of the cations according to their ability to increase the measured hydrodynamic radii follows a Hofmeister series. The change in aggregate size can be explained by modified counterion binding and dehydration of the surfactant headgroups.

In the present work hydrophobic dyes, i.e. disperse red 13 (DR-13; (2-[4-(2-chloro-4-nitrophenylazo)-N-ethylphenylamino]ethanol) and Jaune au gras W1201 (1H-indene-1,3(2H)-dione,2-(2-quinolinyl)), are solubilized in water with the help of different additives: acetone and 1-propanol as typical cosolvents, sodium xylene sulfonate (SXS) as a representative of a classical hydrotrope, sodium dodecyl sulfate (SDS) as a typical surfactant, and finally some "solvosurfactants" [ propylene glycol monoalkyl ether derivatives (CiPOj: i = 1, j = 1 and 3; i = 3, j = 1 and 2; i = 4 and tertio-butyl, j = 1) and 1-propoxy-2-ethanol (C3EO1)]. These solvosurfactants are short amphiphiles that do not form well-defined structures in water such as micelles. For all additives an exponential increase in the solubilizations of the two studied hydrophobic dyes was observed when their concentrations in water were increased. Except for the SDS solution, no difference in the overall shapes of the solubilization curves (dye solubility against additive concentration) was found. All the studied molecules were classified according to their hydrotropic efficiencies, i.e., their abilities to solubilize a hydrophobic, sparingly soluble compound in water. The volume of the hydrophobic parts of the studied additives, roughly evaluated by simple calculations, was found to influence strongly the hydrotropic efficiency; i.e. the larger the hydrophobic part of the additive, the better the hydrotropic efficiency. By contrast, the hydrophilic part carrying a charge or not is of minor importance. Taking the hydrophobic part of the molecules as the key parameter, the water solubilization efficiency of cosolvents, hydrotropes, and solvosurfactants can be described in a coherent way.

In this paper we present the first results of enzymatic activities in a reverse microemulsion medium based on a mixture of an anionic and a cationic surfactant, called catanionic microemulsion. The studied system is composed of sodium dodecyl sulfate (SDS)/dodecyltrimethylammonium bromide (DTAB)/n-hexanol/citrate buffer/n-dodecane, with high SDS/(SDS + DTAB) weight fractions. It turns out that the results are similar to those obtained in classical reverse microemulsions, except that the presence of DTAB exerts an inhibiting effect on the enzyme. Nevertheless, enzymatic superactivities are found even at a DTAB to total surfactant ratio of 15%, corresponding to 3% weight fraction of cationic surfactant in the microemulsion. The influence of pH and hexanol content on the enzymatic activities is also studied.