Interactions of Native and Denatured Whey Proteins with Caseins and Polysaccharides

Abstract

In this review, interactions of native or denatured whey proteins with other proteins and polysaccharides were addressed. Chemical structures of whey proteins and caseins as representatives of proteins and of gum Arabic and dextran as representatives of polysaccharides were explained. Whey protein, as a mixture of different proteins, such as beta-lactoglobulin, alpha-lactalbumin, or bovine serum albumin, has a highly complex nature, and therefore, the main interaction occurs within these proteins upon processing. Structu-re of whey protein includes hydrogen bonds, disulfide bridges and free thiol group, all of which allows whey proteins highly reactive with other polymers. With these properties, whey proteins can be denatured via heating or acidification in a controlled way; and therefore, several functional particles with different sizes and shapes could be obtained. Here we explained the interactions of native and denatured whey proteins with caseins, gum Arabic and dextran in terms of their behaviuor in solutions or dispersions, their functional and rheological properties. Denaturation process includes mainly hydrophobic interacti-ons and is most of the time irreversible, whereas the complex formation of proteins with polysaccharides includes electrostatic and/or steric interactions and complex formation could be reversible or irreversible depending on the type of application. Such interactions are important for the stability of food materials especially during processing and storage, therefore, a deep insight on this subject is important.