Effect Of Hydrodynamic Cavitation On The Aggregation Behavior Of Soybean Globulin Under Different Conditions

Soy protein is often used as a food ingredient in food systems because of its good nutritional value and superior functional properties.The functional properties of protein are closely related to its aggregation behavior.Ultrasonic cavitation is an effective physical modification method,and the modification effect is largely related to the degree of protein aggregation and denaturation.Hydrodynamic cavitation has the same cavitation effect as ultrasonic cavitation and is more suitable for amplification treatment.To study the effect of hydraulic cavitation on the aggregation behavior of soybean globulin under different conditions,the results will provide a basis for hydrodynamic cavitation to regulate the aggregation behavior of soybean protein and improve the functional properties of soybean protein.The main findings are as follows:(1)The effect of hydrodynamic cavitation treatment on the aggregation behavior of glycinin after different heat treatments(70?,80?,and 90?)is shown.The results show that the hydrodynamic cavitation treatment promotes the aggregation of glycinin macromolecular protein after different heat treatments,And aggregate content increased;the maximum absorption peak of the endogenous fluorescence spectrum of all samples was blue shifted,the exposed thiol content,disulfide bond content and solubility were reduced,the emulsion stability was increased,and the effect on emulsification activity and surface hydrophobicity and soybean The heat treatment temperature of globulin is related.The surface hydrophobicity and emulsification activity of the protein heat-treated at 70?increase,and the protein after heat treatment at 80?and 90?shows the opposite change trend;the content of glycinin?-fold after heat treatment at 70?and 80?decrease,Secondary structure was changed.(2)The effect of hydrodynamic cavitation treatment on the aggregation behavior of glycinin under different pH(2,4,6,8,10)conditions was studied.The results showed that the effect of hydrodynamic cavitation treatment on the aggregation behavior of glycinin is related to the pH of the protein solution and cavitation treatment time.After all the samples of glycinin were treated by hydrodynamic cavitation for 30 minutes,when the pH of the protein solution was 4,glycinin aggregated and other proteins depolymerized;When the pH was 4,the average particle size of the protein increased,and the other four The average particle size of the protein samples decreases;the?_max of the glycinin solution at pH 2 and 10 is blue-shifted,and the?_maxof the other three protein samples is red-shifted;when the pH is 6,8,and 10,the surface hydrophobicity increases,while the pH is 2 and 4,the surface hydrophobicity is reduced,except for the absolute value of Zeta potential of glycinin at pH 6,the absolute value of Zeta potential of other soybean protein samples has no significant change;the exposed thiol content of glycinin at pH 8 increases,while the rest content of exposed sulfhydryl groups of glycinin samples after hydrodynamic cavitation treatment is reduced;The solubility of glycinin at pH 6 is increased after hydraulic cavitation treatment,and the solubility of other protein samples after cavitation treatment is reduced and emulsified;After the hydraulic cavitation treatment,the stability of the soybean globulin at pH 2,6 and 10 is increased,while the emulsion stability of the soybean globulin at pH 4 and 8 is reduced after the hydraulic cavitation treatment.When the pH is 6,the effect of hydraulic cavitation treatment on its physical and chemical structure and functional properties is the most obvious.(3)The effect of hydraulic cavitation treatment on the aggregation behavior of glycinin under different ionic strengths(0.06,0.2,0.6)was studied.The results showed that the effect of hydraulic cavitation treatment on the aggregation behavior of glycinin and the ionic strength of the protein solution It is related to the cavitation time.After 30minutes of hydrodynamic cavitation treatment of the three protein samples,when the ionic strength of the protein solution is 0.06,the protein aggregates and the average particle size of the protein increases.When the ionic strength is 0.2 and 0.6,glycinin depolymerization,the average particle size decreases,when the ionic strength is 0.06 and 0.6,the surface hydrophobicity increases,the disulfide bond content decreases,and when the ionic strength is 0.2,the surface hydrophobicity decreases,the disulfide bond content increases;the ionic strength is 0.06 When?_max is basically unchanged,when ionic strength is 0.2,?_max is blue-shifted,while ionic strength is 0.6,?_max is red-shifted;the absolute value of Zeta potential is increased;the exposed thiol content and solubility are decreased.When the ionic strength is 0.2,the hydraulic cavitation treatment has the most obvious effect on its physical and chemical properties.