Thermodynamic stability and retinol binding property of [beta]-lactoglobulin in the presence of cationic surfactants

In this work the stability parameters of bovine [beta]-lactoglobulin, variant A (BLG-A), with regard to their transition curves induced by dodecyltrimethylammonium bromide (C sub(12TAB), tetradecyltrimethylammonium bromide (C) sub(1)4TAB) and hexadecyltrimethylammonium bromide (C sub(16TAB) as catio...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of chemical thermodynamics 2011-08, Vol.43 (8), p.1185-1191
Main Authors: Sahihi, M, Bordbar, A K, Ghayeb, Y
Format: Article
Language:English
Subjects:
Affinity
Binding
Bromides
Cationic
Stability
Surfactants
Thermodynamics
Titration
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In this work the stability parameters of bovine [beta]-lactoglobulin, variant A (BLG-A), with regard to their transition curves induced by dodecyltrimethylammonium bromide (C sub(12TAB), tetradecyltrimethylammonium bromide (C) sub(1)4TAB) and hexadecyltrimethylammonium bromide (C sub(16TAB) as cationic surfactants, were determined at 298 K. For each transition curve, the conventional method of analysis which assumes a linear concentration dependence of the pre- and post-transition base lines, gave the most realistic values for [detla]G) sub(D)(H sub(2O). The results represent the increase in the denaturating power of surfactants with an increase in hydrocarbon chain length. The value of about 22.27 kJ ) super(.) mol[super]-1 was obtained for [detla]G sub(D(H) sub(2)O) from transition curves. Subsequently, the retinol binding property of BLG as its functional indicator was investigated in the presence of these surfactants using the spectrofluorimeter titration method. The results represent the substantial enhancement of retinol binding affinity of BLG in the presence of these surfactants.
ISSN:0021-9614
DOI:10.1016/j.jct.2011.03.004