Quantum-chemical study of dispersion medium influence on the emulsifying ability of milk proteins

Nowadays the products containing milk proteins are widely used in meat industry. Due to these substances application protein-fatty emulsions are stabilized, products consistency, succulence and appearance are made better. To investigate the influence of electrochemically activated water on the emulsifying ability of milk proteins computer molecular modeling and quantum chemical calculations of fragment molecules of αs1-casein in drinking water and catholyte in the presence of linoleic acid triacylglyceride has been conducted. It has been revealed that the negatively charged part of the test protein in the presence of fat molecules in the water is directed toward the polar component, and the nonpolar part is directed toward the hydrophobic component. It has been established that the dipole moment value of αs1-casein molecule fragment being studied in catholyte has been reduced by 10.55 D, the number of hydrogen bonds with molecules of the catholyte has increased by a factor of 1.3 and the number of intramolecular hydrogen bonds of the protein has increased by a factor of 1.7 comparing to the results of the system modeling on the basis of drinking water. On the fragment molecules of αs1-casein in the catholyte the strong electrostatic potential concentration with high electron density center displacement to the phosphoserine amino-acid residue area has been fixed; the protein emulsifying ability increase due to hydrophilic and hydrophobic properties strengthening at the corresponding sections of the peptide chain comparing to drinking water has been established. On the basis of the conducted researches it has been established that protein milk products hydrated with electrochemically activated water (catholyte) are more effective as emulsifiers and water-binding components then when drinking water is used. This allows recommending them for the production of different meat products