By Topic

Self-association behaviour of protein:surfactant systems in alcohol/water mixtures

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$31 $31
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

4 Author(s)
Ruiz-Pena, M. ; Dept. of Radiochem., Inst. of Appl. Sci. & Technol., Ciudad De La Habana, Cuba ; Comas-Rojas, H. ; Rodriguez-Calvo, S. ; Perez-Gramatges, A.

The effect of the addition of short-chain monohydric alcohols (ethanol and propan-2-ol) to the protein:surfactant system lysozyme:sodium dodecyl sulfate (Lz:SDS) in aqueous solution was investigated using a conductometric technique. A second protein:surfactant system, bovine serum albumin:SDS (BSA:SDS) was also investigated so that the effect of a different protein conformation and composition could be compared. The critical aggregation concentration (CAC) of the protein forming the complex and the critical micelle concentration (CMC*) of SDS in the presence of protein, at different alcohol concentrations, were determined. It was found in both cases that the addition of alcohol does not produce a significant change in the CAC, whereas the CMC* displays variation with alcohol concentration that shows an inversion in the ranges 0.05-0.06 ethanol mole fraction and 0.02-0.03 propan-2-ol mole fraction. This suggests that, in contrast with the CAC behaviour, the major factor that drives SDS micellisation in the presence of protein is the variation in water structure. Results also suggest that it occurs in the same way for both proteins, where electrostatic interactions are the main force in the formation of the complex. Conversely, hydrophobic interactions play the dominant role at the micellisation stage, and only the extent of the interaction between protein:surfactant aggregates and surfactant species seems to depend on protein nature.

Published in:

Nanobiotechnology, IEE Proceedings -  (Volume:152 ,  Issue: 5 )