Caseins are amphiphilic proteins with lots of hydrophobic and hydrophilic amino-acid esters [15; 16]. They exhibit numerous positive properties, such as biocompatibility and interfacial activity, they are non-toxic, exhibit a certain stability against temperature and the possibility to form complexes together with other molecules, as well as protective properties for sensitive loads [17]. About 95% of milk casein is suspended in the form of CM, which are of approx. 150 nm in diameter. CM are molecular complexes consisting of different molecules (\(\alpha\)-, \(\beta\)-, \(\kappa\)- and \(\gamma\)-caseins). Spatial structure of CM is determined by properties of casein fractions (e.g., solubility, sensitivity against calcium). A schematic diagram is depicted in Figure 1. The inner core of the micelle mainly consists of more hydrophobic caesins (\(\alpha\)-, \(\beta\)- casein) forming complex structures by using calcium citrate and phosphate bridges with carboxylic groups and phosphoric acid esters of the proteins. More hydrophilic caseinacropeptides, which are part of \(\kappa\)-casein, form a hydration shell around the CM's core and reach into the aqueous phase acting as protective colloid for the CM. The thickness of this hydration shell depends on pH and ion concentration. Furthermore, an electric double layer is formed at the surface of the CM, which is responsible for the stability of CM. Hence, the electric double layer and hydrophilic shell have to be opened or disintegrated in order to incorporate FSBS into CM followed by a subsequent closing or restructuring procedure of CM. CM are not thermally stable. It has been observed that native CM free of whey protein attachments are larger due to thermal changes in casein fractions by ultra-high temperature treatment [4]. Even when cooling down to 2-6 \({}^{\circ}\)C, numerous physico-chemical changes take place, already investigated quite intensively in the 1970s [18; 19]; when milk is refrigerated, a disintegration of the CM due to the release of the strongly hydrophobic \(\beta\)-caseins takes place. This disintegration can be reversed by so-called thermization at 65 \({}^{\circ}\)C. This means that the original properties of the CM are almost completely restored. When pH is lowered, e.g., by adding acid, colloidal calcium phosphate is solubilized, which is intended to bind the casein submicelles together [19]. This can at least lead to a loosening of the CM's substructure. If pH is reduced below 5.2, electrostatic attraction of CM increases and, therefore, intermolecular cohesion. At pH 4.6, caseins precipitate. In principle, acid precipitation is reversible. If pH rises above 5.3, CM are held together due to colloidal calcium phosphate [19]. As a result, the structure of CM can consequently be influenced, e.g., by varying temperature and pH. Besides these known methods to disintegrate CM, a new promising process can be the application of pulsed electric fields (PEF). The technology of PEF is known for the treatment of various food products to affect biological and microbial cells. During this treatment, the product is exposed to high-voltage electrical pulses between two electrodes. The electrical pulses cause the cell to polarize, which induces pore formation in the cell membrane of biological tissue [20; 21]. The working principle is called electroporation. The process is already established in, e.g., the potato industry, to improve chips or French fries processing [21]. Further areas of application of PEF technology are the preservation of fresh juices [22]. The principle of electroporation is based on the effect of the electrical current on a cell. Each cell is surrounded by a protective membrane, which is usually composed of phospholipids and thus represents an insulator. If the cell is exposed to the high-voltage pulses, ions migrate within the cell, which causes the cell to polarize. This polarization leads to an accumulation of charge, in which the ions collect at the membrane and thus exert a kind of compression.