INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Thermal and Electrophoretic Behavior, Hydrophobicity, and Some
Autor/es:
WAGNER, J.R., ; SORGENTINI, D.A; AÑÓN, M.C
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 1996 vol. 44 p. 1881 - 1889
ISSN:
0021-8561
Resumen:
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.