Effect of thermal treatment on the proteins of amaranth isolates

Autores
Avanza, María Victoria; Añon, Maria Cristina
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effect of thermal treatment of proteins from Amaranthus hypochondriacus was studied. Two protein isolates were obtained from the defatted flour by water extraction at a pH of 9 (A9 isolate) and 11 (A11 isolate), followed by isoelectric precipitation at a pH of 5. Effect of thermal treatment (70 and 90 °C, during 3, 5, 10, 15 and 30 min) on A9 and A11 dispersions were analyzed by differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, UV spectrophotometry, superficial hydrophobicity and solubility in water. Thermal treatment induced the aggregate formation of high molecular mass stabilized by disulfide and non‐covalent bond. Thermal treatment at 70 °C produced a 30% denaturation in both, while at 90 °C A9 was more denatured than A11 (75% and 55% of denaturation, respectively). An increase in thermal stability was also detected by DSC in A9 treated at 90 °C. The denaturation process was accompanied at short heating times by an increase in UV absorbance and changes in superficial hydrophobicity. A decrease in water solubility (35–50%, depending on time–temperature conditions) was also observed for the A9 isolates. The results suggest that the A9 isolates, enriched in a globulin protein fraction, are more sensitive to thermal treatment than isolates A11 enriched in glutelin protein fraction. The changes shown by both isolates, indeed, could affect their functional properties and could definitely limit their use in food products.
Fil: Avanza, María Victoria. Universidad Nacional del Nordeste; 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
Thermal treatment
Protein isolates
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:11336/111466
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/111466
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Effect of thermal treatment on the proteins of amaranth isolatesAvanza, María VictoriaAñon, Maria CristinaAmaranthProteinsThermal treatmentProtein isolateshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The effect of thermal treatment of proteins from Amaranthus hypochondriacus was studied. Two protein isolates were obtained from the defatted flour by water extraction at a pH of 9 (A9 isolate) and 11 (A11 isolate), followed by isoelectric precipitation at a pH of 5. Effect of thermal treatment (70 and 90 °C, during 3, 5, 10, 15 and 30 min) on A9 and A11 dispersions were analyzed by differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, UV spectrophotometry, superficial hydrophobicity and solubility in water. Thermal treatment induced the aggregate formation of high molecular mass stabilized by disulfide and non‐covalent bond. Thermal treatment at 70 °C produced a 30% denaturation in both, while at 90 °C A9 was more denatured than A11 (75% and 55% of denaturation, respectively). An increase in thermal stability was also detected by DSC in A9 treated at 90 °C. The denaturation process was accompanied at short heating times by an increase in UV absorbance and changes in superficial hydrophobicity. A decrease in water solubility (35–50%, depending on time–temperature conditions) was also observed for the A9 isolates. The results suggest that the A9 isolates, enriched in a globulin protein fraction, are more sensitive to thermal treatment than isolates A11 enriched in glutelin protein fraction. The changes shown by both isolates, indeed, could affect their functional properties and could definitely limit their use in food products.Fil: Avanza, María Victoria. Universidad Nacional del Nordeste; 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; ArgentinaJohn Wiley & Sons Ltd2007-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/111466Avanza, María Victoria; Añon, Maria Cristina; Effect of thermal treatment on the proteins of amaranth isolates; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 87; 4; 3-2007; 616-6230022-51421097-0010CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.2751info:eu-repo/semantics/altIdentifier/doi/10.1002/jsfa.2751info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:00:36Zoai:ri.conicet.gov.ar:11336/111466instacron: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:34982025-10-22 11:00:36.737CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of thermal treatment on the proteins of amaranth isolates
title Effect of thermal treatment on the proteins of amaranth isolates
spellingShingle Effect of thermal treatment on the proteins of amaranth isolates
Avanza, María Victoria
Amaranth
Proteins
Thermal treatment
Protein isolates
title_short Effect of thermal treatment on the proteins of amaranth isolates
title_full Effect of thermal treatment on the proteins of amaranth isolates
title_fullStr Effect of thermal treatment on the proteins of amaranth isolates
title_full_unstemmed Effect of thermal treatment on the proteins of amaranth isolates
title_sort Effect of thermal treatment on the proteins of amaranth isolates
dc.creator.none.fl_str_mv Avanza, María Victoria
Añon, Maria Cristina
author Avanza, María Victoria
author_facet Avanza, María Victoria
Añon, Maria Cristina
author_role author
author2 Añon, Maria Cristina
author2_role author
dc.subject.none.fl_str_mv Amaranth
Proteins
Thermal treatment
Protein isolates
topic Amaranth
Proteins
Thermal treatment
Protein isolates
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The effect of thermal treatment of proteins from Amaranthus hypochondriacus was studied. Two protein isolates were obtained from the defatted flour by water extraction at a pH of 9 (A9 isolate) and 11 (A11 isolate), followed by isoelectric precipitation at a pH of 5. Effect of thermal treatment (70 and 90 °C, during 3, 5, 10, 15 and 30 min) on A9 and A11 dispersions were analyzed by differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, UV spectrophotometry, superficial hydrophobicity and solubility in water. Thermal treatment induced the aggregate formation of high molecular mass stabilized by disulfide and non‐covalent bond. Thermal treatment at 70 °C produced a 30% denaturation in both, while at 90 °C A9 was more denatured than A11 (75% and 55% of denaturation, respectively). An increase in thermal stability was also detected by DSC in A9 treated at 90 °C. The denaturation process was accompanied at short heating times by an increase in UV absorbance and changes in superficial hydrophobicity. A decrease in water solubility (35–50%, depending on time–temperature conditions) was also observed for the A9 isolates. The results suggest that the A9 isolates, enriched in a globulin protein fraction, are more sensitive to thermal treatment than isolates A11 enriched in glutelin protein fraction. The changes shown by both isolates, indeed, could affect their functional properties and could definitely limit their use in food products.
Fil: Avanza, María Victoria. Universidad Nacional del Nordeste; 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 The effect of thermal treatment of proteins from Amaranthus hypochondriacus was studied. Two protein isolates were obtained from the defatted flour by water extraction at a pH of 9 (A9 isolate) and 11 (A11 isolate), followed by isoelectric precipitation at a pH of 5. Effect of thermal treatment (70 and 90 °C, during 3, 5, 10, 15 and 30 min) on A9 and A11 dispersions were analyzed by differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, UV spectrophotometry, superficial hydrophobicity and solubility in water. Thermal treatment induced the aggregate formation of high molecular mass stabilized by disulfide and non‐covalent bond. Thermal treatment at 70 °C produced a 30% denaturation in both, while at 90 °C A9 was more denatured than A11 (75% and 55% of denaturation, respectively). An increase in thermal stability was also detected by DSC in A9 treated at 90 °C. The denaturation process was accompanied at short heating times by an increase in UV absorbance and changes in superficial hydrophobicity. A decrease in water solubility (35–50%, depending on time–temperature conditions) was also observed for the A9 isolates. The results suggest that the A9 isolates, enriched in a globulin protein fraction, are more sensitive to thermal treatment than isolates A11 enriched in glutelin protein fraction. The changes shown by both isolates, indeed, could affect their functional properties and could definitely limit their use in food products.
publishDate 2007
dc.date.none.fl_str_mv 2007-03
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/11336/111466
Avanza, María Victoria; Añon, Maria Cristina; Effect of thermal treatment on the proteins of amaranth isolates; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 87; 4; 3-2007; 616-623
0022-5142
1097-0010
CONICET Digital
CONICET
url http://hdl.handle.net/11336/111466
identifier_str_mv Avanza, María Victoria; Añon, Maria Cristina; Effect of thermal treatment on the proteins of amaranth isolates; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 87; 4; 3-2007; 616-623
0022-5142
1097-0010
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://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.2751
info:eu-repo/semantics/altIdentifier/doi/10.1002/jsfa.2751
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
dc.publisher.none.fl_str_mv John Wiley & Sons Ltd
publisher.none.fl_str_mv John Wiley & Sons Ltd
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 12.982451

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