Soybean ?-conglycinin and glycinin were polymerized by a microbial transglutaminase (MTGase), and some functional properties of these polymers, including solubility, heat stability and emulsifying, foaming, and gelling properties, were investigated. SDS-PAGE showed that the acidic subunits of glycinin and ?, ? subunits of ?-conglycinin were easily susceptible to MTGase than basic subunits and ?-subunits, respectively. Although MTGase treatment led to the decreases in solubility and emulsifying activity of ?-conglycinin and glycinin, the significant improvements in their gelling and heat stability were observed (p < 0.05). In addition, the MTGase polymerization also increased the foaming property and emulsifying stability of glycinin. These results show that MTGase treatment could improve some functional properties of ?-conglycinin and glycinin, which provides a new opportunity to obtain specific functional properties of soy proteins used in various food systems.
Physicochemical changes of myosin and gelling properties of washed tilapia mince as influenced by oxidative stress and microbial transglutaminase
