INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Relation between solubility and surface hydrophobicity as an indicator of modification during preparation processes of commercial and laboratory prepared soy proteins isolates
Autor/es:
WAGNER, J.R; SORGENTINI, D.A; AÑÓN, M.C
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 2000 vol. 48 p. 3159 - 3165
ISSN:
0021-8561
Resumen:
Because water solubility is the main hydration property of proteins, solubility values of commercial
and laboratory soy protein isolates, prepared under different conditions, were comparatively
analyzed. In contrast, the surface hydrophobicity manifested by proteins is a physicochemical
property that determines, to a great extent, the tendency of protein molecules to aggregate and so
to lose solubility. On these grounds, the solubility of isolates was analyzed as a function of the
surface hydrophobicity of their proteins, and, as a result, three well-defined groups of laboratory
isolates were identified: (A) native, (B) partially or totally denatured with high solubility and surface
hydrophobicity, and (C) totally denatured with low solubility and surface hydrophobicity. Commercial
isolates could not be included in any of these groups; they were grouped as (A¢) partially native and
(C¢) totally denatured. Solubility values in these two groups were similar to those of group C, but
the surface hydrophobicity levels were much lower. The different processes leading to the groups
mentioned above are discussed, along with the way the soy proteins are influenced by the specific
preparation conditions, namely, protein concentration, chemical or thermal treatments, presence
of salts, drying, and phospholipid addition, among others¢) partially native and
(C¢) totally denatured. Solubility values in these two groups were similar to those of group C, but
the surface hydrophobicity levels were much lower. The different processes leading to the groups
mentioned above are discussed, along with the way the soy proteins are influenced by the specific
preparation conditions, namely, protein concentration, chemical or thermal treatments, presence
of salts, drying, and phospholipid addition, among others¢) totally denatured. Solubility values in these two groups were similar to those of group C, but
the surface hydrophobicity levels were much lower. The different processes leading to the groups
mentioned above are discussed, along with the way the soy proteins are influenced by the specific
preparation conditions, namely, protein concentration, chemical or thermal treatments, presence
of salts, drying, and phospholipid addition, among others