More specially, chelating salts bind calcium ions to hydrate proteins and create a more uniform spread.

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.

[4] 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.

[9] 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.

Emulsifying agents such as sodium phosphate play an important role in stabilizing the newly destabilized structure.

[7] Easy Cheese exhibits pseudoplastic behaviors during extrusion of the product, which can be represented using the Herschel-Bulkley Model: This power law model represents a type of non-Newtonian fluid relating shear rate and shear stress with viscosity.

Sodium alginate works in conjunction with the destabilization of the casein micelle where calcium ions can interact with guluronic chains.

About 0.05–0.5% weight by volume of sodium alginate at a 5.4–5.7 range must be added to the cheese mixture to exhibit these properties during extrusion.