THE PHYSICAL PROPERTIES OF THE CASEIN IN SOLUTION: EFFECT OF ULTRA-HIGH PRESSURE

The aim of this work was to study the effect of pressure (50; 90; 160; 250; 350 MPa) on a physical property of casein micelle: hydrodynamic radius, tyrosine and tryptophan fluorescence and IR spectra characteristics. According to photon-correlation spectroscopy, the average hydrodynamic radius of the casein micelle was 128 nm, increasing at 50 MPa to 467 nm with the formation of conglomerates. Further increase of pressure led to the formation of two fractions of particles, differing in hydrodynamic radius. At a pressure of 350 MPa, an average radius of 75 % of particles was 121 nm. Comparison of hydrodynamic radius and tyrosine fluorescence revealed a decrease in the intensity of the glow with an increase in the proportion of large particles and an increase in the radiation in the solution with a decrease of the micelles size. The increase of casein fluorescence by tryptophan and its decrease by tyrosine indicate a change in the conformation of protein molecules during pressure treatment. FTIR spectroscopy revealed a change in the intensity of the optical density in the range of amide I, amide II and valence bonds of tyrosine, confirming the absence of new bonds. The obtained physical data indicate a change in the structure of casein micelles with an increase in the proportion (25 %) of large particles after the action of high pressure (350mpa), which should be taken into account in milk processing. The fluorescence of casein during pressure treatment is a poorly investigated physical indicator and can be important for the processing of raw milk.