Plastein Reaction And Functional Changes Of Soy Protein Isolate

In this study,the single factor experiments and quadratic regression design were used to determine the parameters of soybean peptides prepared by enzymatic hydrolysis of soy protein isolate.The prepared soybean peptides were subjected to protein-like reaction.Single factor and response surface analysis were performed to determine the recombinant preparation The optimum process parameters and the characterization of the recombinant.The optimal conditions of digesting the Alkaline protease(Alcalase)on soybean defatted soybean meal were: Time span of 8 hours,Soybean defatted soybean meal concentration of 5%(m/v),alkaline protease dosage of 5%,Reaction temperature of 50 ?,Solution pH ? of 8.5,Hydrolysis degree reached 40.29%,Nitrogen yield is 72.18%.The optimal parameters of soybean peptide reorganization were: The substrate concentration 31%(m/v),Temperature of 47 ?,p H ? 4.4,The protein yield was 39.43%.The recombinant was characterized by SDS-PAGE and amino acid composition analysis.The infrared spectroscopy showed that the soybean peptide has reorganized under the action of pepsin;there was also new bond formation.The contents of arginine,histidine,tyrosine,methionine and lysine in synthetic protein were improved.In functional assays,compared to the soybean protein isolate and hydrolysis products,the emulsion stability,foaming properties of plastein protein,and most of the gel properties showed their advantages,whereas the solubility lied between the two.