Influence of high hydrostatic pressure on the optical properties of minced fish proteins

In the functioning of various biological systems, an extremely important role is played by the dynamic properties of optically anisotropic protein macromolecules, such as translational movements, temporal correlations, and transfer processes, which are determined by the surface charge, molecular weight, molecular shape, and the nature of intermolecular interactions. An experimental study of the influence of high hydrostatic pressure on the optical properties of pike perch minced fish proteins at room temperature was carried out in this work. The intensities of the radiation transmitted through a thin plane-parallel layer of minced fish were measured, which was subjected to hydrostatic compression at a rate of ≈3 MPa/s and ≈17 MPa/s. It was found that with increasing pressure, the intensity of the transmitted light decreases nonmonotonically; in this case, the experimental plots of the I(P) dependence show the presence of broad attenuation bands of the intensity of the radiation transmitted through the sample, located at pressures of about 150, 300, and 700 MPa. The observed attenuation bands are associated with the appearance of scattering centers formed as a result of denaturation of macromolecules of proteins of various types with different functional purposes contained in the muscle tissue of pike perch.