Milk proteins play a crucial role in dairy products as they influence various physical, chemical and sensory characteristics.
These proteins can be modified using various physical and chemical methods; however, there is an increasing demand for clean label products, leading to the need for chemical-free processes.
High-pressure homogenization (hydrodynamic cavitation) is a physical process that shows great potential in manipulating the structure and functionality of milk proteins required for various dairy products.
Fresh skimmed milk and reconstituted micellar casein samples were subjected to cavitation, with no changes observed in the size of casein micelles, free casein content and soluble calcium concentration.
There was a slight increase in soluble whey proteins and a corresponding decrease in viscosity, as well as a temporary decrease in pH.
However, cavitation led to the release of proteins from the micellar phase to the whey phase and the rupture of casein micelles in the reconstituted skimmed milk samples.
This suggests a potential application of cavitation in the development of milk with novel functionalities by altering micelle size and redistributing caseins between the micellar and serum phases.
Casein micelles can be partially disrupted by cavitation, particularly at high pH, resulting in an increase in surface area, which may be useful for improving rennet coagulation and acid gelation.
An increase in turbidity and a reduction in particle diameter can occur at any given pH value for the casein solution with increasing potency. A greater reduction in diameter of reassembled micelles is observed at higher pH, suggesting an interaction between cavitation and pH.
