Structural characterization of amaranth protein gels

Autores
Avanza, María Victoria; Puppo, Maria Cecilia; Añon, Maria Cristina
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Avanza, María Victoria. Universidad Nacional del Nordeste; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Puppo, Maria Cecilia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Materia
AMARANTH PROTEINS
GEL COLOR
GEL MICROSTRUCTURE
GELATION
WATER IMBIBING CAPACITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/151362
Acceder
id CONICETDig_8b87062e4a00def71e01a2c22abf4402
oai_identifier_str oai:ri.conicet.gov.ar:11336/151362
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structural characterization of amaranth protein gelsAvanza, María VictoriaPuppo, Maria CeciliaAñon, Maria CristinaAMARANTH PROTEINSGEL COLORGEL MICROSTRUCTUREGELATIONWATER IMBIBING CAPACITYhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Gelation 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.Fil: Avanza, María Victoria. Universidad Nacional del Nordeste; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Puppo, Maria Cecilia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaWiley Blackwell Publishing, Inc2005-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/151362Avanza, 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; 1-70022-11471750-3841CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://ift.onlinelibrary.wiley.com/doi/10.1111/j.1365-2621.2005.tb07139.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2621.2005.tb07139.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:05:00Zoai:ri.conicet.gov.ar:11336/151362instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:05:00.965CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structural characterization of amaranth protein gels
title Structural characterization of amaranth protein gels
spellingShingle Structural characterization of amaranth protein gels
Avanza, María Victoria
AMARANTH PROTEINS
GEL COLOR
GEL MICROSTRUCTURE
GELATION
WATER IMBIBING CAPACITY
title_short Structural characterization of amaranth protein gels
title_full Structural characterization of amaranth protein gels
title_fullStr Structural characterization of amaranth protein gels
title_full_unstemmed Structural characterization of amaranth protein gels
title_sort Structural characterization of amaranth protein gels
dc.creator.none.fl_str_mv Avanza, María Victoria
Puppo, Maria Cecilia
Añon, Maria Cristina
author Avanza, María Victoria
author_facet Avanza, María Victoria
Puppo, Maria Cecilia
Añon, Maria Cristina
author_role author
author2 Puppo, Maria Cecilia
Añon, Maria Cristina
author2_role author
author
dc.subject.none.fl_str_mv AMARANTH PROTEINS
GEL COLOR
GEL MICROSTRUCTURE
GELATION
WATER IMBIBING CAPACITY
topic AMARANTH PROTEINS
GEL COLOR
GEL MICROSTRUCTURE
GELATION
WATER IMBIBING CAPACITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv 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.
Fil: Avanza, María Victoria. Universidad Nacional del Nordeste; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Puppo, Maria Cecilia. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
description 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.
publishDate 2005
dc.date.none.fl_str_mv 2005-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/151362
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
0022-1147
1750-3841
CONICET Digital
CONICET
url http://hdl.handle.net/11336/151362
identifier_str_mv 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
0022-1147
1750-3841
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ift.onlinelibrary.wiley.com/doi/10.1111/j.1365-2621.2005.tb07139.x
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2621.2005.tb07139.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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