Unexpected high pressure effects on the structural properties of condensed whey protein systems

Abstract

We show that application of high hydrostatic pressure (600 MPa for 15 min) on condensed whey protein (WP) systems (e.g., 80% w/w solids content) results in unexpected structure-function behavior when compared with conventional thermal treatment. Unraveling the relaxation properties in first-order thermodynamic transitions, the manifestation of glass transition phenomena and the preservation of native conformation in condensed preparations were recorded using small-deformation dynamic oscillation in shear, modulated differential scanning calorimetry, and infrared spectroscopy. Informed temperature application results in the formation of continuous networks at the denaturation temperature, whi..