[ Objective] This study aimed to characterize the structure of soybean glycinin affected by limited enzymatic hydrolysis. [ Method ] The glycinin was limitedly hydrolyzed by alkaline protease; then the SDS-polyacrylam...[ Objective] This study aimed to characterize the structure of soybean glycinin affected by limited enzymatic hydrolysis. [ Method ] The glycinin was limitedly hydrolyzed by 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 glyeinin structure changing during the hydrolysis process. [ Result] SDS-PAGE analysis showed that the subunit contem of glycinin significantly decreased after hydrolysis, and acidic subunits were more susceptible to hydrolysis than alkaline subunits. The scanning electron microscopy revealed that the structure of glycinin powder changed greatly after hydrolysis. The I^TIR results showed that the propor- tions of all conformations of glycinin 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 conformations of glyeinin, and the change was dependent on the degree of hy- drolysis.展开更多
基金Supported by 863 Program(2006AA10Z330)New Century High-level Talent Project in Hubei Province[(2003)31]
文摘[ Objective] This study aimed to characterize the structure of soybean glycinin affected by limited enzymatic hydrolysis. [ Method ] The glycinin was limitedly hydrolyzed by 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 glyeinin structure changing during the hydrolysis process. [ Result] SDS-PAGE analysis showed that the subunit contem of glycinin significantly decreased after hydrolysis, and acidic subunits were more susceptible to hydrolysis than alkaline subunits. The scanning electron microscopy revealed that the structure of glycinin powder changed greatly after hydrolysis. The I^TIR results showed that the propor- tions of all conformations of glycinin 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 conformations of glyeinin, and the change was dependent on the degree of hy- drolysis.
