Artículo
Structural characterization of amaranth protein gels
Fecha de publicación:
04/2005
Editorial:
Wiley Blackwell Publishing, Inc
Revista:
Journal of Food Science
ISSN:
0022-1147
e-ISSN:
1750-3841
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Gelation capacity of a native amaranth protein isolate was studied. Structural properties of gels prepared at different protein concentration and heating conditions were analyzed. Proteins present in amaranth isolates obtained by water extraction at pH 9.0 and subsequent isoelectric precipitation are able to form gels of yellowish appearance. Gel color intensity increased while luminosity decreased with increasing protein concentrations. High protein concentration allowed the formation of matrices with high water-holding capacity. In addition, increasing the heating temperature resulted in gels of high luminosity and low water-holding capacity. The increase of protein concentration (10% to 20% w/v) as well as the increase of heating temperature (70°C to 95°C) and heating time (10 to 30 min) resulted in the formation of a more ordered matrix with smaller pores, mainly stabilized by disulfide bonds and, at a lower extent, by noncovalent interactions (specially hydrogen bonds and hydrophobic interactions). Both amaranth globulin (11S globulin and P globulin) participated in gel structure via high-molecular-weight aggregates (>100 kD). Gel structure was stabilized via noncovalent bonds by monomer species of 42 kD and those of molecular mass lower than 20 kD localized in the interstitial spaces of gel matrix.
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Articulos(CIDCA)
Articulos de CENTRO DE INV EN CRIOTECNOLOGIA DE ALIMENTOS (I)
Articulos de CENTRO DE INV EN CRIOTECNOLOGIA DE ALIMENTOS (I)
Citación
Avanza, María Victoria; Puppo, Maria Cecilia; Añon, Maria Cristina; Structural characterization of amaranth protein gels; Wiley Blackwell Publishing, Inc; Journal of Food Science; 70; 3; 4-2005; 1-7
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