Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH

Amaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be env...

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Detalles Bibliográficos
Autores principales: Ventureira, Jorge Luis, Bolontrade, Agustín Juan, Speroni Aguirre, Francisco, David Briand, Elisabeth, Scilingo, Adriana Alicia, Ropers, Marie-Hélène, Boury, Frank, Añón, María Cristina, Anton, Marc
Formato: Articulo
Lenguaje:Inglés
Publicado: 2011
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/105696
Aporte de:
id I19-R120-10915-105696
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
spellingShingle Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
Ventureira, Jorge Luis
Bolontrade, Agustín Juan
Speroni Aguirre, Francisco
David Briand, Elisabeth
Scilingo, Adriana Alicia
Ropers, Marie-Hélène
Boury, Frank
Añón, María Cristina
Anton, Marc
Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
topic_facet Química
Amaranth
Interfacial properties
Dilatational interfacial rheology
Langmuir isotherm
Emulsifying properties
description Amaranth proteins have adequate amino acid balance for substituting either partly or completely animal proteins in human nutrition. However, they present poor emulsifying properties in basic conditions corresponding to their extraction medium. Consequently their use in acidic conditions could be envisaged to better exploit their potentialities. To better understand their emulsifying properties we have studied their interfacial activities at pHs 2.0 and 8.0 and tried to make the link between 2D and 3D properties. Our results clearly demonstrate the better properties of AI at pH 2.0 than at pH 8 in terms of protein solubility, spreading, adsorption, viscoelastic properties of interfaces and emulsion stability. These results are in relation with the denaturated state of proteins at pH 2.0 where proteins form a harder interfacial film, as compared to pH 8.0. Thus the potential use of amaranth proteins in emulsifying applications should be oriented towards acidic applications.
format Articulo
Articulo
author Ventureira, Jorge Luis
Bolontrade, Agustín Juan
Speroni Aguirre, Francisco
David Briand, Elisabeth
Scilingo, Adriana Alicia
Ropers, Marie-Hélène
Boury, Frank
Añón, María Cristina
Anton, Marc
author_facet Ventureira, Jorge Luis
Bolontrade, Agustín Juan
Speroni Aguirre, Francisco
David Briand, Elisabeth
Scilingo, Adriana Alicia
Ropers, Marie-Hélène
Boury, Frank
Añón, María Cristina
Anton, Marc
author_sort Ventureira, Jorge Luis
title Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_short Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_full Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_fullStr Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_full_unstemmed Interfacial and emulsifying properties of amaranth (<i>Amaranthus hypochondriacus</i>) protein isolates under different conditions of pH
title_sort interfacial and emulsifying properties of amaranth (<i>amaranthus hypochondriacus</i>) protein isolates under different conditions of ph
publishDate 2011
url http://sedici.unlp.edu.ar/handle/10915/105696
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