Relationship between the Method of Obtention and the Structural

PETRUCCELLI, S; AÑÓN, M.C

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

AMER CHEMICAL SOC

Año: 1994 vol. 42 p. 2170 - 2176

0021-8561

Soy protein isolates exhibit heterogeneous protein subunit compositions; their structural and functional properties are determined by the processing conditions. Drastic thermal conditions at pH 7 and 9 result in protein denaturation and polymerization, as evidenced by increased water retention capacity and lower solubility, surface hydrophobicity, and a higher level of AB-11s aggregates. Treatments of glycinin with urea and Na2S03 at pH 7 incorporated 20% of sulfonate groups, resulted in no solubility losses of 11s protein A and B polypeptides, but increased their surface hydrophobicity. The increase of 7s fraction leads to an increase of aliphatic hydrophobicity. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. surface hydrophobicity. The increase of 7s fraction leads to an increase of aliphatic hydrophobicity. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. surface hydrophobicity. The increase of 7s fraction leads to an increase of aliphatic hydrophobicity. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. 11s protein A and B polypeptides, but increased their surface hydrophobicity. The increase of 7s fraction leads to an increase of aliphatic hydrophobicity. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. to an increase of aliphatic hydrophobicity. Thermal treatments at pH 7 and lower protein content lead to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein. to high solubility and high surface hydrophobicity isolates. 7s globulin was completely denatured, while 11s denaturation depended on the treatment conditions; different proportions of AB-1153, ,8-7S, and B-11s aggregates were formed. Thermal treatments at pH 9 favored dissociation and denaturation of AB-11s protein.