Rheological 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
- Gel forming properties of amaranth proteins at different thermal conditions and protein concentration were studied. Gel point (G′ and G″ crossover) and gelation kinetics (G′ vs. time) were analyzed. The type of gel formed from the rheological point of view was studied analyzing the rheograms obtained from frequency sweeps. Texture properties of cold-set gels were analyzed by TPA assays. Minimum conditions for gelation were 7%, w/v and 70°C. Elasticity of heated dispersions and gels increased with the increase of protein concentration. A high value of the network structure index was observed. This behavior could be related to the great proportion of disulfide bonds formed during amaranth protein gelation. At temperatures above 70°C (80, 90 and 95°C), gelation of dispersions (15%, w/v) took place at times less than 5 min. A first order kinetic gelation process with reaction rate specific constant values that increased with the increase of heating temperature was observed. A rapid denaturation of globulins followed by sulfhydryl/disulfide interchange reactions between protein molecules conduced to a gelation phenomenon enhanced by protein aggregation. Gels prepared over critical conditions (T>70°C, protein concentration >7%, w/v) presented a strong gel-like behavior. These type of gels were elastic in nature (tan δ<0.1), of high hardness, fracturability and cohesiveness, although presented low adhesiveness. Depending on protein and thermal conditions, amaranth proteins were able to form self-supporting gels that could be applied in different gel-like foods.
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 TEXTURE
GEL VISCOELASTICITY
GELATION
KINETIC GELATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/151446
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Rheological characterization of amaranth protein gelsAvanza, María VictoriaPuppo, Maria CeciliaAñon, Maria CristinaAMARANTH PROTEINSGEL TEXTUREGEL VISCOELASTICITYGELATIONKINETIC GELATIONhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Gel forming properties of amaranth proteins at different thermal conditions and protein concentration were studied. Gel point (G′ and G″ crossover) and gelation kinetics (G′ vs. time) were analyzed. The type of gel formed from the rheological point of view was studied analyzing the rheograms obtained from frequency sweeps. Texture properties of cold-set gels were analyzed by TPA assays. Minimum conditions for gelation were 7%, w/v and 70°C. Elasticity of heated dispersions and gels increased with the increase of protein concentration. A high value of the network structure index was observed. This behavior could be related to the great proportion of disulfide bonds formed during amaranth protein gelation. At temperatures above 70°C (80, 90 and 95°C), gelation of dispersions (15%, w/v) took place at times less than 5 min. A first order kinetic gelation process with reaction rate specific constant values that increased with the increase of heating temperature was observed. A rapid denaturation of globulins followed by sulfhydryl/disulfide interchange reactions between protein molecules conduced to a gelation phenomenon enhanced by protein aggregation. Gels prepared over critical conditions (T>70°C, protein concentration >7%, w/v) presented a strong gel-like behavior. These type of gels were elastic in nature (tan δ<0.1), of high hardness, fracturability and cohesiveness, although presented low adhesiveness. Depending on protein and thermal conditions, amaranth proteins were able to form self-supporting gels that could be applied in different gel-like foods.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; ArgentinaElsevier2005-09info: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/11336/151446Avanza, María Victoria; Puppo, Maria Cecilia; Añon, Maria Cristina; Rheological characterization of amaranth protein gels; Elsevier; Food Hydrocolloids; 19; 5; 9-2005; 889-8980268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0268005X05000032info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2004.12.002info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:17:22Zoai:ri.conicet.gov.ar:11336/151446instacron: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:34982025-09-10 13:17:22.845CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Rheological characterization of amaranth protein gels |
title |
Rheological characterization of amaranth protein gels |
spellingShingle |
Rheological characterization of amaranth protein gels Avanza, María Victoria AMARANTH PROTEINS GEL TEXTURE GEL VISCOELASTICITY GELATION KINETIC GELATION |
title_short |
Rheological characterization of amaranth protein gels |
title_full |
Rheological characterization of amaranth protein gels |
title_fullStr |
Rheological characterization of amaranth protein gels |
title_full_unstemmed |
Rheological characterization of amaranth protein gels |
title_sort |
Rheological 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 TEXTURE GEL VISCOELASTICITY GELATION KINETIC GELATION |
topic |
AMARANTH PROTEINS GEL TEXTURE GEL VISCOELASTICITY GELATION KINETIC GELATION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
Gel forming properties of amaranth proteins at different thermal conditions and protein concentration were studied. Gel point (G′ and G″ crossover) and gelation kinetics (G′ vs. time) were analyzed. The type of gel formed from the rheological point of view was studied analyzing the rheograms obtained from frequency sweeps. Texture properties of cold-set gels were analyzed by TPA assays. Minimum conditions for gelation were 7%, w/v and 70°C. Elasticity of heated dispersions and gels increased with the increase of protein concentration. A high value of the network structure index was observed. This behavior could be related to the great proportion of disulfide bonds formed during amaranth protein gelation. At temperatures above 70°C (80, 90 and 95°C), gelation of dispersions (15%, w/v) took place at times less than 5 min. A first order kinetic gelation process with reaction rate specific constant values that increased with the increase of heating temperature was observed. A rapid denaturation of globulins followed by sulfhydryl/disulfide interchange reactions between protein molecules conduced to a gelation phenomenon enhanced by protein aggregation. Gels prepared over critical conditions (T>70°C, protein concentration >7%, w/v) presented a strong gel-like behavior. These type of gels were elastic in nature (tan δ<0.1), of high hardness, fracturability and cohesiveness, although presented low adhesiveness. Depending on protein and thermal conditions, amaranth proteins were able to form self-supporting gels that could be applied in different gel-like foods. 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 |
Gel forming properties of amaranth proteins at different thermal conditions and protein concentration were studied. Gel point (G′ and G″ crossover) and gelation kinetics (G′ vs. time) were analyzed. The type of gel formed from the rheological point of view was studied analyzing the rheograms obtained from frequency sweeps. Texture properties of cold-set gels were analyzed by TPA assays. Minimum conditions for gelation were 7%, w/v and 70°C. Elasticity of heated dispersions and gels increased with the increase of protein concentration. A high value of the network structure index was observed. This behavior could be related to the great proportion of disulfide bonds formed during amaranth protein gelation. At temperatures above 70°C (80, 90 and 95°C), gelation of dispersions (15%, w/v) took place at times less than 5 min. A first order kinetic gelation process with reaction rate specific constant values that increased with the increase of heating temperature was observed. A rapid denaturation of globulins followed by sulfhydryl/disulfide interchange reactions between protein molecules conduced to a gelation phenomenon enhanced by protein aggregation. Gels prepared over critical conditions (T>70°C, protein concentration >7%, w/v) presented a strong gel-like behavior. These type of gels were elastic in nature (tan δ<0.1), of high hardness, fracturability and cohesiveness, although presented low adhesiveness. Depending on protein and thermal conditions, amaranth proteins were able to form self-supporting gels that could be applied in different gel-like foods. |
publishDate |
2005 |
dc.date.none.fl_str_mv |
2005-09 |
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/11336/151446 Avanza, María Victoria; Puppo, Maria Cecilia; Añon, Maria Cristina; Rheological characterization of amaranth protein gels; Elsevier; Food Hydrocolloids; 19; 5; 9-2005; 889-898 0268-005X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/151446 |
identifier_str_mv |
Avanza, María Victoria; Puppo, Maria Cecilia; Añon, Maria Cristina; Rheological characterization of amaranth protein gels; Elsevier; Food Hydrocolloids; 19; 5; 9-2005; 889-898 0268-005X 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://www.sciencedirect.com/science/article/pii/S0268005X05000032 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2004.12.002 |
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 |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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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1842980951111499776 |
score |
12.993085 |