Thermal and Electrophoretic Behavior, Hydrophobicity, and Some

WAGNER, J.R., ; SORGENTINI, D.A; AÑÓN, M.C

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

AMER CHEMICAL SOC

Año: 1996 vol. 44 p. 1881 - 1889

0021-8561

In the present work, changes in the structure and functional properties of soy protein isolates caused by mild acid treatment at room temperature were investigated. Different conditions (pH, time, neutralization procedure, and isolate concentration) of acid treatment and consequent salt increase were analyzed. The results obtained show that there is a selective denaturation of 11S protein, which conduces to higher surface hydrophobicity. The solubility of modified isolates decreases with extended storage period of the flour from which they were obtained and with higher isolate concentration during acid treatment. The high water imbibing capacity (WIC) of the resulted insoluble fraction does not produce significant changes in the WIC of the total isolate. The denaturation and dissociation of 11S protein lead to modified isolates with improved capacity to form and to stabilize foams without losing the gel formation capacity.