Effect of the Limited Enzymatic Hydrolysis on the Structure Characterization of Glycinin

[Objective] This study aimed to characterize the structure of glycinin affected by limited enzymatic hydrolysis.[Mehtod] The glycinin was hydrolyzed with alkaline protease;then the SDS-polyacrylamide gel electrophoresis(SDS-PAGE),scanning electron microscopy(SEM),Fourier transform infrared spectroscopy(FTIR) and other means were performed to characterize the structure of glycinin changing during the hydrolysis process.[Result] SDS-PAGE analysis showed that subunit content of glycinin significantly decreased after hydrolysis,and acidic subunits was more susceptible to hydrolysis than alkaline subunits.The scanning electron microscopy revealed that the glycinin powder structure changed greatly after hydrolysis.The FTIR results showed that the proportions of all the glycinin conformations changed greatly during hydrolysis process.In addition,the protein hydrophobicity and sulfhydryl content were also significantly influenced by hydrolysis.[Conclusion] The enzymatic hydrolysis greatly changed the conformation of glycinin,and the change was dependent on the degree of hydrolysis.