Accessibility navigation


Selective separation of beta-lactoglobulin from sweet whey using CGAs generated from the cationic surfactant CTAB

Fuda, E., Bhatia, D., Pyle, D.L. and Jauregi, P. (2005) Selective separation of beta-lactoglobulin from sweet whey using CGAs generated from the cationic surfactant CTAB. Biotechnology and Bioengineering, 90 (5). pp. 532-542. ISSN 0006-3592

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1002/bit.20412

Abstract/Summary

The selective separation of whey proteins was studied using colloidal gas aphrons generated from the cationic surfactant cetyl trimethyl ammonium bromide (CTAB). From the titration curves obtained by zeta potential measurements of individual whey proteins, it was expected to selectively adsorb the major whey proteins, i.e., bovine serum albumin, alpha-lactalbumin, and beta-lactoglobulin to the aphrons and elute the remaining proteins (lactoferrin and lactoperoxidase) in the liquid phase. A number of process parameters including pH, ionic strength, and mass ratio of surfactant to protein (M-CTAB/M-TP) were varied in order to evaluate their effect on protein separation. Under optimum conditions (2 mmol/l CTAB, M-CTAB/M-TP = 0.26-0.35, pH 8, and ionic strength = 0.018 mol/l), 80-90% beta-lactoglobulin was removed from the liquid phase as a precipitate, while about 75% lactoferrin and lactoperoxidase, 80% bovine serum albumin, 95% immunoglobulin, and 65% alpha-lactalbumin were recovered in the liquid fraction. Mechanistic studies using zeta potential measurements and fluorescence spectroscopy proved that electrostatic interactions modulate only partially the selectivity of protein separation, as proteins with similar surface charges do not separate to the same extent between the two phases. The selectivity of recovery of beta-lactoglobulin probably occurs in two steps: the first being the selective interaction of the protein with opposite-charged surfactant molecules by means of electrostatic interactions, which leads to denaturation of the protein and subsequent formation and precipitation of the CTAB-beta-lactoglobulin complex. This is followed by the separation of CTAB-beta-lactoglobulin aggregates from the bulk liquid by flotation in the aphron phase. In this way, CGAs act as carriers which facilitate the removal of protein precipitate. (c) 2005 Wiley Periodicals, Inc.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13404
Uncontrolled Keywords:microbubbles, CTAB, beta-lactoglobulin, protein-surfactant, interactions, zeta potential, fluorescence quenching, COLLOIDAL GAS APHRONS, ALPHA-LACTALBUMIN, PROTEIN RECOVERY, RECOMBINANT, CUTINASE, ANIONIC SURFACTANT, BOVINE WHEY, CHEESE WHEY, WASTE-WATER, LACTOFERRIN, DISPERSIONS

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation