Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes

Autores
Condes, María Cecilia; Scilingo, Adriana Alicia; Añon, Maria Cristina
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Amaranth protein isolates were prepared from Amaranthus hypochondriacus and hydrolyzed using trypsin. Degrees of hydrolysis varied between 2% and 7% with the time of hydrolysis reaction. The structure, solubility and foaming properties of protein isolates were studied. SDS-PAGE analysis demonstrated that polypeptides from 11S-globulin and P globulin were the main targets for the protease, while a polypeptide of 45 kDa from the 7S globulin was more resistant to trypsin action. The FPLC analysis of hydrolyzed proteins showed that the structure is partially conserved, while an increase of the fraction of lower molecular weight is observed. Such structure exhibits a single endotherm of lower denaturation heat than the protein isolate. The solubility and foaming properties of protein isolates and hydrolysates were analyzed, in the later case at two protein concentrations (1 mg and 2.5 mg of solid matter per ml). Protein solubility increased markedly with hydrolysis, while changes in foaming properties were less dramatic. Nevertheless, foams obtained with amaranth protein hydrolysates were more dense and stable than those prepared with non-digested proteins, specially for foams produced with the protein hydrolysate of higher concentration.
Fil: Condes, María 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: Scilingo, Adriana Alicia. 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
FOAM PROPERTIES
HYDROLYSIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/136303
Acceder
id CONICETDig_398763dbd78ab9f17232679e00d35ca6
oai_identifier_str oai:ri.conicet.gov.ar:11336/136303
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changesCondes, María CeciliaScilingo, Adriana AliciaAñon, Maria CristinaAMARANTH PROTEINSFOAM PROPERTIESHYDROLYSIShttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Amaranth protein isolates were prepared from Amaranthus hypochondriacus and hydrolyzed using trypsin. Degrees of hydrolysis varied between 2% and 7% with the time of hydrolysis reaction. The structure, solubility and foaming properties of protein isolates were studied. SDS-PAGE analysis demonstrated that polypeptides from 11S-globulin and P globulin were the main targets for the protease, while a polypeptide of 45 kDa from the 7S globulin was more resistant to trypsin action. The FPLC analysis of hydrolyzed proteins showed that the structure is partially conserved, while an increase of the fraction of lower molecular weight is observed. Such structure exhibits a single endotherm of lower denaturation heat than the protein isolate. The solubility and foaming properties of protein isolates and hydrolysates were analyzed, in the later case at two protein concentrations (1 mg and 2.5 mg of solid matter per ml). Protein solubility increased markedly with hydrolysis, while changes in foaming properties were less dramatic. Nevertheless, foams obtained with amaranth protein hydrolysates were more dense and stable than those prepared with non-digested proteins, specially for foams produced with the protein hydrolysate of higher concentration.Fil: Condes, María 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: Scilingo, Adriana Alicia. 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; ArgentinaElsevier Science2009-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/136303Condes, María Cecilia; Scilingo, Adriana Alicia; Añon, Maria Cristina; Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes; Elsevier Science; LWT - Food Science and Technology; 42; 5; 6-2009; 963-9700023-64381096-1127CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2008.12.008info:eu-repo/semantics/altIdentifier/url/https://bit.ly/36Ds5WDinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:36:08Zoai:ri.conicet.gov.ar:11336/136303instacron: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 10:36:09.196CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
title Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
spellingShingle Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
Condes, María Cecilia
AMARANTH PROTEINS
FOAM PROPERTIES
HYDROLYSIS
title_short Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
title_full Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
title_fullStr Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
title_full_unstemmed Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
title_sort Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes
dc.creator.none.fl_str_mv Condes, María Cecilia
Scilingo, Adriana Alicia
Añon, Maria Cristina
author Condes, María Cecilia
author_facet Condes, María Cecilia
Scilingo, Adriana Alicia
Añon, Maria Cristina
author_role author
author2 Scilingo, Adriana Alicia
Añon, Maria Cristina
author2_role author
author
dc.subject.none.fl_str_mv AMARANTH PROTEINS
FOAM PROPERTIES
HYDROLYSIS
topic AMARANTH PROTEINS
FOAM PROPERTIES
HYDROLYSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Amaranth protein isolates were prepared from Amaranthus hypochondriacus and hydrolyzed using trypsin. Degrees of hydrolysis varied between 2% and 7% with the time of hydrolysis reaction. The structure, solubility and foaming properties of protein isolates were studied. SDS-PAGE analysis demonstrated that polypeptides from 11S-globulin and P globulin were the main targets for the protease, while a polypeptide of 45 kDa from the 7S globulin was more resistant to trypsin action. The FPLC analysis of hydrolyzed proteins showed that the structure is partially conserved, while an increase of the fraction of lower molecular weight is observed. Such structure exhibits a single endotherm of lower denaturation heat than the protein isolate. The solubility and foaming properties of protein isolates and hydrolysates were analyzed, in the later case at two protein concentrations (1 mg and 2.5 mg of solid matter per ml). Protein solubility increased markedly with hydrolysis, while changes in foaming properties were less dramatic. Nevertheless, foams obtained with amaranth protein hydrolysates were more dense and stable than those prepared with non-digested proteins, specially for foams produced with the protein hydrolysate of higher concentration.
Fil: Condes, María 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: Scilingo, Adriana Alicia. 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 Amaranth protein isolates were prepared from Amaranthus hypochondriacus and hydrolyzed using trypsin. Degrees of hydrolysis varied between 2% and 7% with the time of hydrolysis reaction. The structure, solubility and foaming properties of protein isolates were studied. SDS-PAGE analysis demonstrated that polypeptides from 11S-globulin and P globulin were the main targets for the protease, while a polypeptide of 45 kDa from the 7S globulin was more resistant to trypsin action. The FPLC analysis of hydrolyzed proteins showed that the structure is partially conserved, while an increase of the fraction of lower molecular weight is observed. Such structure exhibits a single endotherm of lower denaturation heat than the protein isolate. The solubility and foaming properties of protein isolates and hydrolysates were analyzed, in the later case at two protein concentrations (1 mg and 2.5 mg of solid matter per ml). Protein solubility increased markedly with hydrolysis, while changes in foaming properties were less dramatic. Nevertheless, foams obtained with amaranth protein hydrolysates were more dense and stable than those prepared with non-digested proteins, specially for foams produced with the protein hydrolysate of higher concentration.
publishDate 2009
dc.date.none.fl_str_mv 2009-06
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/11336/136303
Condes, María Cecilia; Scilingo, Adriana Alicia; Añon, Maria Cristina; Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes; Elsevier Science; LWT - Food Science and Technology; 42; 5; 6-2009; 963-970
0023-6438
1096-1127
CONICET Digital
CONICET
url http://hdl.handle.net/11336/136303
identifier_str_mv Condes, María Cecilia; Scilingo, Adriana Alicia; Añon, Maria Cristina; Characterization of amaranth proteins modified by trypsin proteolysis. Structural and functional changes; Elsevier Science; LWT - Food Science and Technology; 42; 5; 6-2009; 963-970
0023-6438
1096-1127
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2008.12.008
info:eu-repo/semantics/altIdentifier/url/https://bit.ly/36Ds5WD
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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
_version_ 1844614381618331648
score 13.070432

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