INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Structural properties of heat-induced soy protein gels as affected by ionic strength and pH
Autor/es:
PUPPO, M.C; AÑÓN, M.C
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 1998 vol. 46 p. 3583 - 3589
ISSN:
0021-8561
Resumen:
Hydration properties of acidic soy protein gels, prepared with different salt solutions, were studied.
The type of bonds that stabilize gel structure and the nature of protein species that make up and
stabilize such structure were also investigated. The microstructure of gels was evaluated by scanning
electron microscopy (SEM) and water-holding capacity (WHC) assays. The stability and nature of
protein fractions of gel matrices were analyzed by solubility measurements and sodium dodecyl
sulfate-polyacrylamide gel electrophoresis. The WHC of gels prepared with NaCl and CaCl2-polyacrylamide gel electrophoresis. The WHC of gels prepared with NaCl and CaCl2
decreased with increasing salt concentration. This fact suggested, as was corroborated by gel SEM,
that at high ionic strength a more open matrix was formed. The structure of acidic gels, stabilized
by noncovalent bonds, changed with NaCl addition. Both 7S and 11S globulin subunits participated
via hydrophobic interactions to the stability of pH 2.75 gels. At pH 3.50 the gel matrix was stabilized
by hydrophobic interactions among â-conglycinin subunits, whereas the AB-11S subunit and the
AB-11S polymers, linked by disulfide bonds, would be soluble in the matrix interior due to the
glycinin fraction that remains native after thermal treatment.â-conglycinin subunits, whereas the AB-11S subunit and the
AB-11S polymers, linked by disulfide bonds, would be soluble in the matrix interior due to the
glycinin fraction that remains native after thermal treatment.