INTRODUCTIONEconomical and environmentally friendly methodsof food processing require novel technological solutionsto maintain the high quality of finished products [1–3].Food science helps understand the impact of innovativeapproaches on the properties of substances in theproduction chain, from raw materials and by-products tofinished products and waste disposal issues [4–6].The structure and properties of food ingredientsdepend on such physical conditions as temperature,pressure, stirring speed, etc., as well as on chemicalinteractions with other nutrients, e.g. water [7–9].A targeted effect on the water base can develop thedesired characteristics of the semi-finished or finishedproduct [10, 11]. The food industry uses electrochemicalactivation as a relevant method of reagent-free control ofphysicochemical and rheological properties.Electrochemical activation, or electrolysis, isa unipolar electrochemical processing of water oraqueous electrolyte solutions. It occurs in the anodeor cathode chamber of a diaphragm or membraneelectrochemical reactor [12, 13]. Electrolysis happensas a result of electrochemical and electrical processesin water in a double electric layer of electrodeswith a non-equilibrium electric charge transfer.Water is treated with a constant electric current,118Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126and electric potentials exceed its decompositionvoltage (+1.25 V). As a result, water passes intoa metastable state with non-standard electronactivity, redox potential, and other physicochemicalparameters. Electrochemically activated water isable to retain this metastable state for a long timeand resists the thermodynamic equilibrium with theenvironment [12].Metastable compounds with a high oxidizing(anolyte) or reducing (catholyte) ability undergoa series of spontaneous structural, energetic, andchemical transformations and gradually stabilizeduring storage. They are highly reactive to chemicalsand biological objects. Metastable compounds enhanceacidic and oxidizing properties of anolyte, as well asthe alkaline and reducing properties of catholyte [14–17]. Electrochemical nonequilibrium leads to multiplechanges in the reactivity of ions but does not affect theirconcentration. In electrochemically activated water, thepH values of catholyte and anolyte correspond to theequilibrium concentrations of alkali and acid that exceedthe content of salts in this water. The redox values alsogo beyond the chemical control capabilities for a givenelectrical conductivity [12].Electrochemically activated water and its solutionsowe their chemical activity to electrically activemicrobubbles of electrolysis gases. These microbubblesare 0.2–5.0 μm in size, and their concentration can reach106–107 mL−1. They are stabilized by uncompensatedelectric charges at the interface of gas and liquid phases[12, 14, 18].Electrochemically activated water and its solutionshave non-standard physicochemical parameters of pHand redox potential, which makes them biologicallyactive [13, 18, 19]. Electrochemically activated watersolutions of both low and high molecular weightcompounds differ from similar solutions of nonelectrolyzedwater [12, 16].Electrochemically activated water and its solutionsbehave differently in technological processes. Forinstance, electrochemically activated water andultrapure water are known to affect apricot proteinextraction [20]. At the same pH = 9.5, electrochemicallyactivated water had a better extraction efficiencythan ultrapure water. Foaming ability and stabilityof the electrochemically activated water emulsionswere 11.17% and 36.33 min, whereas in the ultrapurewater samples they were 4.75% and 23.88 min,respectively. Electrochemically activated water hada more ordered secondary structure than ultrapurewater. The ordered structures of α-helix and β-sheetwere 7.5 and 60.2%, while the disordered structuresand random turns were 8.4 and 23.8%, respectively.The extraction method increased the yield of theproduct, minimized the structural degradation,and improved the functional properties of apricotprotein [20].Electrochemical activation proved an effectivemeans of extracting protein from canola meal [21].Under the electric field, the cathode chamber producedan alkaline solution from a sodium chloride (NaCl)solution. The alkaline solution had better extractiveproperties compared to the samples subjected tochemical alkalization. The extracted proteins hada better extractability, composition, and secondarystructure. The concentration of NaCl was 0.01–1 M,electroactivation time – 10–60 min, current – 0.2 and0.3A. The experiment was conducted in a three-chambercell separated by ion-exchange membranes.The resulting solutions underwent an extractionprocedure. The maximal protein extract of 34.32 ± 1.21%occurred when the electrolyzed solution was generatedat 0.3A, regardless of the activation time. Thestandard extraction (pH 7–10) yielded 31.18 ± 1.89%proteins under the same conditions. The SodiumDodecyl Sulphate Polyacrylamide Gel Electrophoresis(SDS-PAGE) showed that the electrophoretic profilesof electrolyzed protein concentrates and isolatesdiffered from those obtained with the conventionalmethod. The Fourier Transform Infrared Spectroscopy(FTIR) showed significant differences in the secondarystructures of proteins depending on the pH and saltconcentration. The electrochemically activated sampleshad a lower denaturation [21].Electric field can change the properties of aqueousprotein solutions due to their electrical conductivityand the chemical structure of polyampholyticpolyelectrolytes. Their amino acid units have ionogenicside groups, and their acidic groups alternate withbasic ones, which provides macromolecules withspecific electric, configuration, and hydrodynamicproperties [22]. Molecular conformation, volume,and rheology depend on the concentration of thepolyelectrolyte in the solution, e.g. temperature,pressure, low molecular weight substances,pH value, etc. [23–27].Animal blood proteins can serve as an exampleof such relationships. Serum proteins have a lot ofbeneficial nutritional properties, which makes thempart of many food formulations. A globular moleculeof bovine serum albumin consists of several hundredamino acid residues. Its three-dimensional structure islabile, mobile, and sensitive to exogenous factors [23, 26,28]. A bovine serum albumin solution contains proteinfragments of different dimensions. Its monomers andaggregates are in a state of dynamic equilibrium, andthe weight of polypeptides increases as the albuminconcentration in the solution rises [26].The dissolution of crystalline albumin dependson the contact time of the phases: it can change itsconformation, develop intermolecular bonds, or destroythem. The structure of albumin solutions and theirsurface properties depend on the pH of the solution andthe pH value of the isoelectric point. The closer to theisoelectric point, the more turbid the solutions are andthe lower their viscosity gets. This phenomenon canbe explained by the minimal energy of electrostaticrepulsion between the side chains of albumin molecules119Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126and the molecules themselves. The resulting aggregatesare denser, more compact, and larger in size. They haveless effect on the flow and increase light scattering.During structuring, the turbidity and viscosity of thesolutions change nonlinearly, depending on the proteinconcentration [24, 27].The surface activity of albumin increases togetherwith proton concentration. In an acidic environment,more non-polar groups emerge on the surface ofthe molecule than in a neutral or slightly alkalineenvironment. Obviously, the surface activity of albuminmolecules is minimal at physiological pH values [27].Denaturation and aggregation of serum proteinisolates depend on the pH of the medium. This effectis widely used in food technology. When acidity pHdrops to 1, it leads to the denaturation of bovine serumalbumin with a conformational transition. This processis caused by the loss of the tertiary structure, whichoccurs as the polypeptide chain of the bovine serumalbumin molecule unfolds and the aggregates increase insize [26].A strong alkaline environment has a morepronounced texturing effect, e.g. 2N NaOH solution witha pH of 12.4 ± 0.4 or alkaline electrolyzed water with apH of 11.5 ± 0.4. In an acidic environment, the effect isless pronounced, e.g. 2N HCl with a pH of 2.0 ± 0.2 oracidic electrolysis water with pH 2.5 ± 0.2 [29]. Albuminis a polyelectrolyte with a high conformational mobility.In an electrochemically activated solution, it should besensitive both to the acidity of the solution and its redoxpotential. The present research objective was to studythe effect of electrochemically activated water on theproperties of serum albumin in protein solutions.STUDY OBJECTS AND METHODSSample preparation. The research featured bovineserum albumin BSA 100 (Merck, Sigma-Aldrich).Preparations with casein proteins and instant foodgelatin were used as control (Dr. Oetker, OOO Oetker,Russia, TU 20.59.60-011-42450906-2018).The research involved UV spectrometry, time-offlightsecondary ion mass spectrometry (ToF-SIMS),and electrophoresis of an 1% protein aqueous solution,which was then diluted with water or electrochemicallyactivated water at a ratio of 1:4. Fractions of electrolyzedwater, catholyte (pH 8.2, redox –800 mV), andanolyte (pH 2.2, redox +800 mV) were obtained ina fresh drinking water purification unit by means ofdirect electrochemical action in diaphragm modularelectrochemical cells (LLC Delfin Aqua, Russia).Artesian water (pH 7.2, redox +360 mV) from the citywater supply served as control. In the viscosity test,electrolyzed water with a negative redox value wasobtained using an Izumrud-K1 installation (NPO EkranOJSC, Russia). Tap water passed through a number ofstages:1. Anode chamber of a flow-type electrochemicalmodule. Here the water was disinfected due to peroxideand chlorine-oxygen compounds, then saturated withoxygen and ozone to kill microorganisms and oxidizeorganic impurities;2. Reaction-flotation reactor. It removed coagulatedproducts of anodic treatment from electrolyticallyobtained microbubbles of oxygen and ozone;3. Heterophase catalytic reactor. The procedureremoved active chlorine compounds and produced activeoxygen compounds;4. Cathode chamber. Here the residual ions of iron,copper, magnesium, etc. were converted into insolublehydroxides, which were then removed in the flotationand electrokinetic reactors. During the cathodictreatment, molecular hydrogen and free hydroxyl groupsentered the water and gave it a negative redox value andantioxidant properties.The electrochemically activated water had pH 7.3and redox –223 mV, while for the initial water thesevalues were 7.3 and +190 mV, respectively. The acidity(pH) and redox potential of the solution were measuredusing a SevenExellence S470 multivariable device(METTLER TOLEDO, Switzerland) with a pH electrode(Inlab Routine Pro, Mettler Toledo, Switzerland) anda redox electrode (Inlab Redox Pro, Mettler Toledo,Switzerland). Depending on the concentration ofbovine serum albumin, its pH value ranged 7.2–7.6 forelectrolyzed water and 7.9–8.6 for tap water.UV spectrometry. Spectrometry was used todefine the effect of electrolyzed water on aqueousprotein solutions. Its optical density was recorded inthe absorption spectrum of the sample in the ultravioletregion at a wavelength of 235 and 280 nm using aShimadzu UV-2401PC spectrophotometer (Japan).Time-of-flight secondary ion mass spectrometry(ToF-SIMS). To obtain samples for mass spectrometry,2 μL of bovine serum albumin solution in water or waterfractions were applied to a clean glass substrate. Itssurface was covered with a conductive ITO-indium tinoxide film (Sigma-Aldrich). After drying in an stream,the sample was transferred to the chamber of a ToFSIMS5 secondary ion mass spectrometer (ION-ToFGmbH, Germany). The preparation was ionized with a200 nm beam of primary Bi3+ ions at 30 keV. After 70 nsof exposure, secondary ions were registered (~ 80 μs)and the beam moved to the next point. The primaryion irradiation did not exceed 5 × 1012 ions/cm2. Theprincipal component analysis helped to assess thedifferences between the obtained mass spectra [30, 31].Measuring the kinematic viscosity of proteinsolutions. This parameter was measured using anOstwald VPZh-4m capillary viscometer (VPZh-4mviscometer, LABTECH LLC, Russia) at 20°C. Theviscosity value was calculated as follows:( * * )9,8g K tV = (1)where V is the kinematic viscosity of the liquid, mm2/s;K is the constant of the viscometer, mm2/s2; t is the flowtime, sec; g is the gravity acceleration, 9.8 m/s2.120Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126The protein content in the diluted solution was 0.01,0.05, 0.1, and 0.2%; in the concentrated solution – 1, 3, 5,and 10%.Protein electrophoresis. This parameter wasmeasured using standard methods and the followingingredients. Acrylamide 8% separating gel contained0.375 M Tris HCl (pH 8.8), 0.1% PSA (ammoniumpersulfate 0, 0.1% DS-Na (Dodecylsulfat Na-salz),and 0.01% TEMED (tetramethylethylenediamine).Acrylamide 5% focusing gel included 0.125 M Tris HCl(pH 6.8), 0.1% PSA, 0.1% DS-Na, and 0.01% TEMED.The electrode buffer included 0.025 M Tris HCl (pH 8.3)and 0.19 M glycine.The protein was diluted in buffer: 2% DS-Na, 10%glycerin, 5% 2-mercaptoethanol, 0.004% bromophenolblue, 0.063 M Tris HCl, pH 6.8. After that, it was boiledin a 100% water bath for 5 min. The solution wasapplied to the gel, where electrophoresis was carried outat 20 mA for 2 h. The resulting preparation was stainedwith Cumassi R 250.RESULTS AND DISCUSSIONUV spectrometry. The method of UV spectrometryof aqueous solutions was used to study the effect ofelectrochemically activated water on protein. The UVspectrum was not specific for biomolecule solutions, butit made it possible to perform a comparative analysis ofintegral changes in the sample. The UV spectrometrytest featured bovine serum albumin, food gelatin, andcasein (Fig. 1).Figure 1 demonstrates that the obtained absorptionspectra were identical for all the proteins in theexperiment. Unlike the conventional water solutions,the solutions of electrochemically activated waterfractions had a lower optical density, and theirabsorption peak was in 235–280 nm. All the samples ofelectrochemically activated water had a slightly higherabsorption level of the protein solution in catholyte.These changes were more obvious in the solution ofbiochemically pure albumin (Fig. 1a) than in the samplesof food gelatin (Fig. 1b) and casein (Fig. 1c). The UVspectrometry demonstrated the modification of theprotein in the solution of electrolyzed water fractions.The time-of-flight molecular mass spectrometry (ToFSIMS)provided additional data on the state of albuminin the solutions.Time-of-flight secondary ion mass spectrometr(ToF-SIMS). This method was used to perform themolecular analysis of protein samples. A droplet ofeach solution was dried on a cover glass in a streamof clean air. ToF-SIMS provided information aboutchemical composition, molecular orientation, surfaceorder, chemical bonding, and purity. Mass spectra ofeach preparation were compared using various dataclassification techniques. The principal componentanalysis is one of the most popular techniques usedin mass spectrometry. It features the most intensepeaks in mass spectra and provides a 95% confidenceinterval [30, 31].Briefly, the program received 20 principalcomponents: the higher the component number, themore variation in the data it reflected. Such a numberof coordinates was unnecessary, so the space ofthe first two components was used to analyze thesimilarity of the samples. All the samples of biologicalmacromolecules in this research underwent the sameToF-SIMS preparation procedure and the same principalcomponent analysis. Figure 2 shows the results of themolecular mass spectrometry.Figure 2a illustrates a typical mass spectrum ofbovine serum albumin dissolved in water or electrolyzedwater fractions. Figure 2b clearly demonstrates asignificant difference between all three samples.The catholyte-treated protein showed significantheterogeneity compared to the control and especiallythe anolyte-treated sample. Anolyte treatment had afocusing effect on the protein samples, if compared tothe heterogeneous group of samples obtained from thealbumin solution in catholyte or water. The change in themass spectrum may be due to the development of newFigure 1 Nonspecific UV absorption spectra of 0.20% solutions of bovine serum albumin (a), food gelatin (b),and casein (c) in water or electrochemically activated water fractions (catholyte, anolyte)watercatholyteanolytewatercatholyteanolytewatercatholyteanolytea b с121Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126peaks and/or a change in the intensity of similar peaks.The results of molecular analysis statistically confirmedthe UV spectrometry data (Fig. 1a): electrochemicallyactivated water fractions really modified the albumin.The total change in the physicochemical propertiesof protein could change in the rheological properties(viscosity) of the solution.Kinematic viscosity of bovine serum albumin.The viscosity of aqueous solutions of hydrocolloidsis an important characteristic of food systems. Forinstance, the viscosity of protein solutions is one ofthe most serious problems when highly concentratedprotein formulations or milk powder. The viscosity offood systems is controlled both by physical methodsand by additives. A small amount of such low molecularweight additives as salt reduces the viscosity that resultsfrom electrostatic repulsion and attraction. Argininehydrochloride (ArgHCl) is known to act as a chaotropicagent. It destroys the network of hydrogen bondsbetween water molecules, thus suppressing hydrophobicFigure 2 ToF-SIMS analysis of bovine serum albumin samples in conventional water (control) and electrochemically activatedfractions (anolyte, catholyte): (a) ranges of molecular weights: bottom mass spectrum – control (water), medium – after catholytetreatment, upper – after anolyte treatment; (b) ellipses – 95% confidence areas for n = 6 measurements for each groupwatercatholyteanolytecatholyteanolytewaterаb122Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126attraction and clustering, which can reduce the viscosityof the solution [32].Hydrodynamic cavitation served as a technologicaltool to reduce the viscosity of serum protein concentratebefore spray drying. Whey protein concentrate(31% dry matter) underwent various hydrodynamiccavitation treatments. The samples were tested forviscosity during 14 days of storage. The enthalpy ofdenaturation was estimated using differential scanningcalorimetry, while the particle size was measuredusing dynamic light scattering. The hydrodynamiccavitation treatment appeared to reduce the viscosity by7–8%, and this effect remained constant for 14 days ofstorage. According to the particle size distribution, thedestruction of aggregates decreased the number of largeparticles and thus caused the drop in viscosity [33].The viscosity of protein solution depends not onlyon the size, but also on the shape, morphology, andstructure of the particles. For instance, flow behaviorof partially denatured serum protein aggregatesshowed a complex dependence on the microstructuralmorphology of particles, their concentration, andshear rate [24]. Even though the protein content in thesolution was the same, particles with an open fibrillar/tubular structure had a higher viscosity than compactaggregates. Rough and uneven particles appeared toform solutions of higher viscosity than smooth particlesof the same size. Serum proteins of various sizes anddenaturation degrees produced solutions of differentviscosity, probably, as a result of interactions betweenprotein aggregates. Partial denaturation technologycould control the structure of serum protein aggregatesto achieve specific viscosity characteristics [24].Protein is a biopolymer. Hence, the viscosity ofits solution depends not only on its properties andconcentration, but also on the solvent. Temperature,pH, impurities, and dissolved gases affect the viscosityof solutions. For example, negative redox potential canaffect the quality and interaction efficiency of dissolvedmacromolecules [34, 35].This part of the experiment featured electrolyzedwater with a standard acidity value (pH ~ 7.3) butextremely low redox potential (–223 mV) at the startingpoint. The redox potential value of tap water in thecontrol sample remained constant (+190 mV) at 20°Cduring 24 h. However, the redox potential value ofelectrolyzed water (–223 mV) gradually increased asthe metastable state relaxed. The highest relaxation rateoccurred in the first 6 h after treatment, and then theprocess slowed down. After 24 h, the redox potentialreached +69 mV, which was much lower than in thecontrol sample. As the concentration of albumin keptgrowing from 0.01 to 0.2%, the relaxation rate increasedgradually. After bovine serum albumin dissolved, theredox potential index increased from –194 to –162 mV.When the albumin concentration reached 1–3%, theeffect intensified abruptly and reached plateau at–90 mV. Adding bovine serum albumin speeded upthe recovery of the redox potential of the electrolyzedwater. The kinetics of the process depended on theconcentration. After 24 h, the maximal value was+125 mV at 0.2% of bovine serum albumin, whichwas much lower than the redox potential of the controlsample (+190 mV).The results clearly showed the dependence of theredox potential of electrochemically activated watersolutions on albumin concentration. Such interactionsmay affect the kinematic viscosity of the solution: themolecular conformation change and/or intermolecularbonds are distorted. The structure of water in theelectrochemical reactor changes, thus resulting in anegative redox potential of the water. These changescan also affect the behavior of macromolecules, i.e.solubility, interaction, conformation, repulsion orattraction, as hydrogen, hydrophobic, or electrostaticnon-covalent bonds get stronger or weaker [36, 37].Figure 3 shows the changes in the kinematicviscosity of the solutions of tap water and electrolyzedwater at different concentrations of bovine serumalbumin from 1 to 10%.Electrochemical treatment of tap water decreasedthe viscosity of the solution at all the concentrations ofbovine serum albumin (Fig. 3). The tap water solutionbecame more viscous over time, while the electrolyzedwater with the same concentration of albumin remainedalmost the same. The viscosity of the solution usuallyFigure 3 Kinematic viscosity of water solutionvs. electrochemically activated water solutionat different concentrations of bovine serum albumin, %Kinematic viscosity, mm2/sStorage time, hElectrolyzed water solutionElectrolyzed water solutionElectrolyzed water solution Electrolyzed water solution123Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126increases together with the increase in the proteincontent, but electrolyzed water reduced the initial valueof this parameter, especially in the 10% solutions ofbovine serum albumin. This effect might have resultedfrom the increased electrostatic repulsion betweenalbumin molecules. At an isoelectric point of pl 4.9and pH 7.3–8.6, the total charge of the protein becamenegative due to additional dissociation of carboxylgroups caused by albumin molecular conformation.Both the protein monoproduct sample (albumin)and the food protein composition samples (gelatin andcasein) changed when dissolved in the electrolyzedwater fractions. The observed effects might be aconsequence of changes in the structure of the proteinand/or its fragmentation. Figure 4 shows the results ofgel electrophoresis.Protein electrophoreses differed (Fig. 4), but thesolutions of the same protein in water or electrolyzedwater fractions showed no significant differences.A high performance liquid chromatography(HPLC) confirmed this observation. The data of gelelectrophoresis differed from the results of molecularanalysis (ToF-SIMS) because these two methods arebased on different physical principles. Electrophoresisfeatures proteins and their large fragments in an electricfield while mass spectrometry registers amino acid ionsand small peptides. The decrease in molecular weightunder the action of electrolyzed water was insignificant,but it could still affect the peptide structure both in theoxidized (pH 2.2, redox +800 mV) and reduced (pH 8.2,redox –800 mV) fractions of electrolyzed water. Whenproteins dissolved in the anodic and cathodic fractions ofpurified drinking water, they got neither fragmented norstructurally changed.The effect of the anodic and cathodic fractionsof electrolyzed water on the properties of serumalbumin confirmed the prospects of the targeted useof electrochemical activation in the food industry as ameans of condition monitoring.The research results correlated with other studiesthat state the importance of water for reagent-freecontrol of protein quality in the food industry. Accordingto [38], polyphosphate (50%) can be partially replacedwith alkaline electrolyzed water (1.25 g/L sodiumtripolyphosphate, 0.3 g/L sodium metapolyphosphate,0.4 g/L sodium polyphosphate, pH = 11.4). Thereplacement improved the quality of catfish fillet: itsweight and water retention capacity increased. A higherphosphate content had a similar result (2.5 g/L sodiumtripolyphosphate, 0.6 g/L sodium metapolyphosphate,0.8 g/L sodium polyphosphate, pH = 9.0). However,the experiment established no change in hardnessand elasticity. The test samples improved in color andoxidation resistance, though [38].Electrochemical activation proved to be an effectivesustainable technology to produce acidic and alkaline(anolyte and catholyte) extraction solutions that couldreplace hydrochloric acid and sodium hydroxide.For example, a combination of electrolyzed waterand ultrasonic treatment improved the efficiencyof extracting proteins from sea krill [39]. Unlike asimilar combined method with deionized water, theelectrolyzed water method reduced NaOH consumptionby 30.9% w/w. Electrochemically activated water witha negative redox potential –(800–900 mV) showedgood antioxidant properties, which protected the activegroups of proteins (carbonyl, sulfhydryl) from oxidation.Ultrasonic treatment provided an additional increase inthe extraction yield, raised the solubility, reduced theparticle size, changed the structure, and improved thefunctional properties of krill proteins, e.g. emulsifyingand foaming capacity, foam stability, etc. [39].A combination of electrochemically activatedwater, isoelectric precipitation, as well as isoelectronicprecipitation and electrochemically activated watertreatment (IP-EWT) provided a high recovery rate(≥ 50%) of protein concentrate from heat stabilizeddefatted rice bran [40]. The protein fraction contained65.1 wt% protein and had a high amino acid value(76.6%). A Sodium Dodecyl Sulphate PolyacrylamideGel Electrophoresis and an immunoblotting analysisshowed no signs of allergenic rice protein or heavymetals in the protein fractions. The combined IP-EWTprocess was environmentally friendly. It yielded highlyconcentrated and safe protein from plant materialswithout enzymes or chemicals, e.g. organic solvents,buffering agents, surfactants, etc.Electrochemically activated water proved effectivein the extraction of dry material from soybeanmeal [41]. Solutions of anolyte and catholyte had aFigure 4 Gel electrophoresis of protein solutions in wateror in the fraction of electrochemically activated fractions(catholyte, anolyte): (a) albumin, (b) gelatin, (c) caseinkDA water catholyte anolytealbumingelatinkDA water catholyte anolytecazeinkDA water catholyte anolytea bс124Pogorelov A.G. et al. Foods and Raw Materials, 2022, vol. 10, no. 1, pp. 117–126high ability to extract proteins, carbohydrates, andespecially minerals. The extracted proteins had a wellbalancedamino acid composition, which meant theycould serve as ingredients in various functional foods.Electrochemically activated water gives the foodindustry an important alternative to chemical reagents.In future, it can become an effective tool for functionalmodification of proteins [41, 42].CONCLUSIONThe present research involved viscometry, UVspectrometry, time-of-flight mass spectrometry ofsecondary ions, and electrophoresis of bovine serumalbumin. All the methods confirmed a multifacetedeffect of the anodic and cathodic fractions ofelectrochemically activated water on the structureand properties of protein in aqueous solutions. Theprotein monoproduct (serum albumin) was subjectto modification when interacting with fractionsof electrolyzed water. The oxidized fraction ofelectrochemically activated water (anolyte) madethe protein solution more homogeneous in termsof molecular composition. The research registereda significant unified effect of anolyte with a highconcentration of hydrogen peroxide on the disulfidebond of amino acid residues, e.g. cysteine.However, the mechanism of action of the reducedfraction of electrochemically activated water (catholyte)still remains unclear. The catholyte has a pronouncedantioxidant activity, but the activity of antioxidantsin biological systems can be studied only by thecompensation of oxidative stress to the normal levelof the redox potential of the medium (~ 360 mV). Thecatholyte-based solutions of bovine serum albumin hadan abnormally negative potential (–800 mV), whichwas not induced under physiological conditions orpathological changes. Unlike the control samples, theexperimental samples with electrochemically activatedwater retained the initial viscosity for a long time. Theirviscosity was lower than that of the protein solution innon-electrochemically activated water. This effect wasconsistent with other physicochemical changes.The obtained patterns revealed good prospectsfor reagent-free control of protein food media intechnological processes. Less food additives andtechnological aids during processing means thepossibility to modify the functional properties ofprotein food ingredients, e.g. texturing isolates.Electrochemically activated water can serve as a waterbase for liquid protein-fortified products. The methodhelps maintain the desirable viscosity, consistency, andsensory properties of functional foods.CONTRIBUTIONA.G. Pogorelov supervised the project and proofreadthe final manuscript. L.G. Ipatova wrote and improvedthe manuscript. M.A. Pogorelova obtained andanalyzed the data. A.L. Kuznetsov interpreted the data.O.A. Suvorov designed the research concept.CONFLICT OF INTERESTThe authors claim there is no conflict or interestsregarding the publication of this article.