CIDCA   05380
CENTRO DE INVESTIGACION Y DESARROLLO EN CRIOTECNOLOGIA DE ALIMENTOS
Unidad Ejecutora - UE
artículos
Título:
Interactions between Isoflavones and Soybean Proteins: Applications in Soybean-Protein-Isolate Production
Autor/es:
FRANCISCO SPERONI; VERÓNICA MILESI; AÑÓN, M.C.
Revista:
LEBENSMITTEL-WISSENSCHAFT UND-TECHNOLOGIE-FOOD SCIENCE AND TECHNOLOGY
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2010
ISSN:
0023-6438
Resumen:
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The
effects of several modifications to soybean protein isolate (SPI) production on
genistein series composition and content were analyzed. Combined variations of
protein extraction pH and protein precipitation pH revealed that the maximum
content of total genistein series was obtained with protein extraction at pH
8.0 and protein precipitation at pH 3.5. When protein extraction was carried
out at pH 11.0, the saponification of malonylgenistin, resulting in genistin
production, led to a decrease in isoflavone content. This fact was attributed
to the low affinity of genistin for b-conglycinin.
Malonylgenistin exhibited a high level of association with both glycinin and b-conglycinin
at precipitation conditions. When temperature was reduced from 20 to 0 °C during protein precipitation,
the genistein series content increased if the b-glucosidase
activity was inhibited. This increase was at the expense of glucosilated forms.
The nature of the interaction between soybean proteins and malonylgenistein and
genistin seemed to be -at least in part- enthalpic in nature. In particular,
malonylgenistin at pH 3.5 establishes another kind of interaction with protein,
besides enthalpic ones. Glycinin exhibited higher affinities for genistein
series components than b-conglycinin, the
interactions being more stable at acidic than at alkaline pHs.