BiPRO: Functional Properties of BiPRO
In their native form, proteins from whey are 100% soluble. During processing, the environment around the whey protein changes. These processing conditions, i.e. heat, pH, ionic strength, etc., can cause the protein to modify its conformation or shape, resulting in varying degrees of denaturation or modification of the whey protein. Denatured whey proteins behave differently than native-state whey proteins. Some of the differences are manifested in their ability to gel, bind water, thicken, foam, emulsify, form films, etc. Depending on the application, it is possible to exploit these functional properties by controlling the modification of the whey proteins in what is called a "controlled denaturation" of the whey protein. The properties that result from a controlled denaturation of whey protein can enhance functional properties in a variety of applications, particularly as they relate to rheology and flavor.
Whey proteins in their native form are 100% soluble. BiPRO is fully soluble over the pH range 2.0 to 9.0. Solubility of protein is critical for beverage application development.
Gelation occurs when native globular whey proteins are denatured (unfolded) in the presence of heat. The denatured proteins aggregate and form three-dimensional matrices that entrap and hold water. Heat induced gelation depends on many factors: composition of the protein, extent of denaturation, pH, temperature of heat treatment, protein concentration, heating rate, ionic strength and presence of specific ions. Beta-lactoglobulin is the primary gelling protein in whey protein, and a major portion of the protein present in BiPRO.
Whey protein has two functions in the formation of foams. It acts as a surfactant to reduce the tension at the air/liquid interface, and it forms a continuous cohesive film at the interface, which stabilizes the foam bubbles. BiPRO has excellent foaming properties (foam overrun and foam stability).