FOOD USE OF SOYBEAN 7s AND 11s PROTEINS Extraction and Functional Properties of Their Fractions

Contribution of Disulfide Bonding to Viscoelastic Properties and Microstructures of 11S Globulin Gels from Soybeans: Magnesium Chloride-Induced Gels

“…These viscoelastic data indicate that 11S formed stiffer and more solid gels than SPI. These results are consistent with previous reports that of all the soybean proteins, 11S has the greatest ability to form heat-induced gels (Saio et al, 1973;van Kleef, 1986;Nakamura et al, 1986;Renkema et al, 2001).…”

“…These viscoelastic data indicate that 11S formed stiffer and more solid gels than SPI. These results are consistent with previous reports that of all the soybean proteins, 11S has the greatest ability to form heat-induced gels (Saio et al, 1973;van Kleef, 1986;Nakamura et al, 1986;Renkema et al, 2001).Effect of 2-mercaptoethanol (2-ME) on viscoelastic properties of 11S and SPI gels The reducing agent 2-ME prevents disulfide bond formation between protein molecules during the formation of heat-induced gels (Utsumi and Kinsella, 1985ab). Therefore, to examine the contribution of disulfide bonds to gel structure, the effects of 2-ME on emission was measured at 580 − 690 nm.…”

“…Soybean protein isolate (SPI) is prepared from water-extracted soybean proteins by acidic precipitation and consists mainly of 7S and 11S. Rheological properties of heat-induced 7S, 11S, and SPI gels have been extensively studied (Saio et al, 1973;Hermansson, 1986;van Kleef, 1986;Nakamura et al, 1986;Yamauchi et al, 1991; Nagano et al, 1994ab;Renkema et al, 2001;Lakemond et al, 2003;Renkema, 2004). Most studies have reported that of all the soybean proteins, 11S has the greatest ability to form heatinduced gels.…”

Gel Formation of Soybean 7S and 11S Proteins

“…14 -17 ) Consequently, it may explain the much dye-binding ability of the 7S protein at higher dye concentration. The presence of the reactive carboxyl groups in the 11S protein may be correlated with the facts that the addition of salts suppressed the formation of gel of the lIS protein at this experiment, the 11S protein was easily precipitated by calcium salts 2 ) and the calciuminduced or heat-induced gels of the lIS protein were rigider than that of the 7S protein.! ,2)…”

Effect of soybean aging on the quality of soymilk, firmness of tofu and optimum coagulant concentration

“…The OCC of MgSO 4 Á7H 2 O was determined by the same methodology as described in Section 2.4; however, soymilk temperature was kept at 75°C (average denaturation temperature of globulins 7S and 11S, according to Saio and Watanabe, 1973). This measurement was performed on soymilk from soybean cultivars stored at all AA and NA experimental times, and also the control.…”