Characterization of β-Conglycinin and Glycinin Soy Protein Fractions from Four Selected Soybean Genotypes

Abstract

The beta-conglycinin and glycinin fractions of soy protein were isolated from Macon, Ohio FG1, Enrei, and IL2 genotypes that were grown under the same environmental conditions. The soy protein fractions were evaluated to determine whether chemical composition and gel-forming properties were related. Amino acid analyses suggested that the hydrophobic residues may be the primary cause of differences in soy protein gel characteristics as the storage moduli increased with higher percentages of hydrophobic residues. Reversed-phase high-performance liquid chromatography profiles revealed variations in the composition of each fraction that corresponded to differences observed among the storage moduli. The gel-forming properties may be related to more than just protein content, such as the amount and type of amino acid in the fraction.

Food protein-stabilized nanoemulsions as potential delivery systems for poorly water-soluble drugs: preparation, in vitro characterization, and pharmacokinetics in rats

“…15 The amount of nonpolar amino acid residues is 62.5% (mol%) and 34.8% for 11S and 7S, respectively. 16 WPI is derived from milk, in which the two most important proteins (β-lg and α-lactalbumin) account for about 65% of the total weight of whey protein. 17,18 α-Lactalbumin is a small, acidic, and Ca 2+ -binding milk protein with a molecular weight of 14.2 kDa and an isoelectric point of 4-5.…”

Variation in genetic and environmental effects of beta-conglycinin (7S) and glycinin (11S) protein fractions in conventional and GM soybean cultivars grown in Southern Brazil

“…Among the cultivars BRS 213 and BRS 257 do not present the lipoxygenases L1, L2 and L3, while BRS 242 RR, BRS 244 RR, BRS 245 RR, BRS 246RR, BRS 255 and BRS 256 RR RR are genetically modified. Studies reveal variations in protein and subunits in cultivars with high levels of 7S and 11S (TAKAHASHI et al, 2001). The effects of environment on protein fractions were reported by Murphy and Ressureccion in 1984, and interaction between genotype and environment for the ratios of 11S/7S proteins was also recorded by Helms et al (1998) …”

“…Studies on characterization and functional properties of the proteins glycinin and β-conglycinin in different soybean cultivars were carried out (MOLINA; PAPADOULOS; LEDWARD, 2001, RIBLETT et al, 2001, KHATIB et al, 2002, CARRÃO-PANIZZI et al, 2008. Both fractions are also capable of stimulating activity receptor for low density cholesterol (LDL), (ANTHONY, 2000;ERDMAN, 2000).…”

Hidrólise enzimática de fibras de cotilédones de soja e caracterização das frações sólidas e solúveis

“…Microscopia eletrônica de varredura das fibras de soja sob a forma de fibra alimenar original (A), micronizada (B) (160x), original hidrolisada com protease (C), micronizada hidrolisada com protease (D), original hidrolisada com carboidrase (E) e micronizada hidrolisada com carboidrase (F) (800x). (Garcia et al, 1997;Riblett et al, 2001). Uma banda de menor intensidade foi verificada em 15 KDa, provavelmente uma subunidade da glicinina, o que também foi verificado por Riblett et al (2001) que, ao avaliar as frações 7S e 11S separadamente, observaram que essa banda foi revelada na eletroforese de glicinina, com baixa intensidade.…”

“…(Garcia et al, 1997;Riblett et al, 2001). Uma banda de menor intensidade foi verificada em 15 KDa, provavelmente uma subunidade da glicinina, o que também foi verificado por Riblett et al (2001) que, ao avaliar as frações 7S e 11S separadamente, observaram que essa banda foi revelada na eletroforese de glicinina, com baixa intensidade. De acordo com a análise visual da eletroforese, a protease hidrolisou as proteínas das fibras de soja a peptídeos com pesos moleculares menores que 10 KDa.…”