Whey protein separation technique improves protein properties.
Reverse micelles are surfactant aggregates that have small polar cores of solubilized water of macromolecular dimensions. Reverse micelles can selectively purify recombinant proteins and their intermediates from fermentation broths. Reverse micelles are able to host proteins in an aqueous environment, effectively shielding them from a nonmiscible apolar environment.
By using reverse micellar (RM) solvents to achieve protein-specific isolations, researchers at the California Dairy Foods Research Center have successfully developed strategies for separating beta-lactoglobulin (p-LG), alphalactalbumin (a-LB) and immunoglobulin (IgG) from whey. What we have here is a cost-effective separation process and an opportunity to separate out whey proteins to create value-added products. In RM separation, not only are protein molecules intact afterwards, but also large scale-up of the necessary solutions is relatively uncomplicated.
The two primary components of whey, p-LG and a-LB, have desirable functional properties when used as food ingredients, including the ability to stabilize food emulsions as foams and to create protein-based gels for confections, soups and sauces. These proteins are also valuable for their nutritional quality. To benefit from the value of whey proteins, manufacturers need an efficient and cost-effective approach for separating proteins from whey, and for purifying the individual elements of the whey protein mixture. Current commercial processes for separating whey proteins are based on ultrafiltration and ion exchange adsorption. The resulting protein mixtures have some valuable functional properties in foods, but their usefulness could be enhanced by creating products with better consistency and individual protein purity.
RM techniques have the potential to continuously extract specific proteins from an aqueous mixture, achieving the simultaneous concentration and purification of specific proteins. The RM solvent contains small droplets of water, stabilized within an organic solvent by a surfactant. Because protein molecules often move from an original water phase into these small, encapsulated water droplets, RM extraction is attractive for separating proteins from an aqueous solution.
Further information. Stephanie Dungan, University of California-Davis, Chemical Engineering and Material Sciences, Department of Food Science and Technology, Davis, CA 95616; phone: 530-752-5447; fax: 530-752-4759; email: firstname.lastname@example.org; URL: www.ucdavis.edu.
|Printer friendly Cite/link Email Feedback|
|Publication:||Emerging Food R&D Report|
|Date:||May 1, 2003|
|Previous Article:||Research carried out by French scientists. (Executives: FYI).|
|Next Article:||Food-canning technique uses enzyme to keep cooked vegetables crispy.|