Heating the cheese mixture causes separation of the fats and protein of the cheese emulsion from destabilization. Emulsifying agents are made up of amphiphilic molecules that act as an interface to reduce the surface tension between hydrophilic and hydrophobic molecules of the product to result in a uniform cheese spread that does not separate during storage. Cheese proteins that have denatured during processing are reestablished using melting salts. Sodium citrate and sodium phosphate are the main emulsifiers used in Easy Cheese to sequester calcium in cheddar cheese. This occurrence hydrates and solubilizes the casein, causing it to swell with water. The addition of these salts contributes to the uniformly creamy consistency of Easy Cheese. The key role of emulsifying agents in Easy Cheese is to create a uniform cheese spread by altering the structure of casein micelles in the cheese. Casein micelles have a diameter ranging from 15 to 20 nanometers and are composed of flexible aggregates alpha-, beta-, and kappa-casein. The alpha- and beta-casein are kept in place by “colloidal calcium phosphate-mediated cross links” covered with a kappa-casein outer layer. The outer layer on the casein's surface has glycosylated hydrophilic tails that are negatively charged and is stable in solution due to Van der Waals interactions. All of the negative charges causes the casein micelles to initially repel each other and provides stability to the matrix by protecting the alpha- and beta-caseins. When the group of casein micelles are exposed to heat and shearing forces, kappa-casein is cleaved causing the displacement of the glycosylated hydrophilic tails. The casein micelle becomes destabilized as alpha and beta-casein are now exposed to the environment. Emulsifying agents such as sodium phosphate play an important role in stabilizing the newly destabilized structure. The hydrophilic portion of sodium phosphate removes calcium from the calcium paracaseinate from ion exchange reactions. This action causes “hydration and partial dispersion of the calcium-paracaseinate phosphate network." The hydration process increases the solubility of the protein. Sodium phosphate removes calcium from the Ca-paracaseinate cheese complex due to ion exchange interactions, where positive calcium ions bind to the negative phosphate groups. Phosphate and citrate anions can then bind to the protein structure, converting calcium-paracaseinate converts to water-soluble sodium-paracaseinate. Upon cooling, the partially dispersed matrix forms a gel-like network that gives rise to the textural properties of the final product. Viscosity The interactions between proteins and carbohydrates play an important role in the