MTGase Mediated Polymerization of 11S Globulin to Enhance Its Functionalities and the Proteomics

摘要

In this paper, the effects of the induced polymerization and modification by microbial transglutaminase (MTGase) on solubility and emulsifiability of soybean 11S globulin was studied. The mechanism was also investigated through proteomics. Using SDS-PAGE and optical density scanning to testify MTGase enzymatic polymerization, the optimum conditions showed that: temperature was 45 degrees C, ionic condition I was 0.2, pH was 8.0, the amount of enzyme was 30 U/g. The molecular weight of modified 11S globulin subunits concentrated at 15 kDa. The solublity and emulsifiability were significantly enhanced. There were 268 differential protein spots extracted. Ten protein spots had significant differences in expression which totally focused on seed storage proteins, promoting seed germination and maturation proteins, proteins involved in osmotic regulation and alcohol dehydrogenase, which affect solubility and emulsifiability of 11S globulin.