Properties of serum albumin in electrolyzed water

Introduction. Electrochemical activation of water controls the physicochemical parameters of aquatic food environment without any reagents. Electrolyzed water affects the properties of macronutrient solutions. The present research studied the effect of anodic and cathodic fractions of electrochemically activated water on protein molecules and their interaction patterns. Study objects and methods. The study featured bovine serum albumin and its properties in electrochemically activated water with nonstandard redox and acidity values. The aqueous solution of bovine serum albumin was studied by viscometry, UV spectrometry, time-of-flight secondary ion mass spectrometry, and electrophoresis. Results and discussion. By knowing the interaction patterns of electrochemically activated water and protein molecules, food producers can control the properties of biological raw materials. Bovine serum albumin was studied in metastable fractions of electrochemically activated water obtained in the anode or cathode chamber of an electrochemical reactor. Both fractions of electrochemically activated water appeared to modify the properties of bovine serum albumin. The oxidized fraction of electrochemically activated water (anolyte) converted the protein solution into a more homogeneous molecular composition. The solution of bovine serum albumin in the reduced fraction of electrochemically activated water (catholyte) had an abnormally negative redox potential (–800 mV). The aqueous solution of bovine serum albumin in catholyte retained its initial viscosity for a long time, and its level was lower than in the control sample. This effect was consistent with other physicochemical characteristics of the solution. Conclusion. The research revealed some patterns that make it possible to apply reagent-free viscosity regulation to protein media in the food industry.