Research partners:


ILVO - research partner of Smartflow


Smartflow research partner of Smartflow




Milk contains both water, minerals, fat and protein and hence is extremely sensitive to the subtle changes resulting from the exposure to the correct electromagnetic field which subtly alters the hydrogen bonding networks in the water and protein as well as the hydrated mineral ion complexes and the electrostatic stabilization of the hydrophobic fat globules in the water suspension.


When milk is subject to heating in the industrial treatment of milk such as in milk pasteurization, sterilization and evaporation, the whey proteins, in particular Beta Lactoglobulin, are subject to thermal denaturation and aggregation, which leads to the formation of fouling in the heat exchangers and evaporators at the contact surfaces. This leads to a loss of optimum functioning of the heat exchanger, which over a very short time in just hours becomes very significant. The Industry is forced to compensate for this by running Clean In Place (CIP) programs several times per day using aggressive chemicals (NaOH) to purge out and remove the deposits in the heat exchangers.


Treatment of the milk with a suitably designed electromagnetic field has the subtle effect on the hydrogen bonding in the water, protein, mineral hydrated complexes and effect on the stabilization of the fat globules. Most important in this application is the effect that the altered hydrogen bonding has on the thermal denaturation of the beta lactoglobulin. In the absence of the electromagnetic field exposure the beta lactoglobulin is well known to denature above 65 degrees with the quarternary structure unwrapping to expose the thiol groups which then react to cross link with other exposed proteins both beta lactoglobulin and alpha lactoalbumin to form chains or aggregates of proteins. It is these aggregates that are responsible for adhering to the walls of the heat exchangers during the pasteurization of the milk.


When the milk is exposed to the field the rearrangement of the hydrogen bonding structures in the proteins means that the thermal denaturation unwrapping of the beta lactoglobulin chains is altered. The resultant exposure of the thiol groups on unwrapping the protein chains is effected and hence the resultant formation of the protein aggregates is reduced with the resultant effect that the denatured proteins remain dissolved in the milk solution and do not therefore give rise to fouling of the internal surfaces of the heat exchangers.

  • Read more about liquid foods applications in our application secton.


Contact information

Newtec Water Systems NV
Zandvoortstraat 12c
2800 Mechelen

Tel: 015 28 84 10
Fax: 015 28 84 19