Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems

Autores
Spotti, Maria Julia; Martinez, María Julia; Pilosof, Ana Maria Renata; Candioti, Mario César; Rubiolo, Amelia Catalina; Carrara, Carlos Roberto
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It is well known that protein/polysaccharide conjugates obtained by Maillard reaction (MR) have good emulsifying properties. However, there is little information about the use of these conjugates in gel systems. Structural characteristics and rheological properties of conjugates obtained by MR of whey protein isolate (WPI) and dextrans (DX) of various molecular weight (MW: 6, 40 and 70 kDa) were studied. Conjugation was confirmed by electrophoresis; browning intensity was measured by absorbance at 420 nm; and conformational changes were studied by fluorescence emission of tryptophan (Trp) (λex = 280 nm). Rheological properties were determined by oscillatory rheometry with temperature ramp (25–90 °C). After each measure, a mechanical spectrum (at 25 °C) was obtained. The electrophoresis indicated the presence of WPI/DX conjugates in all systems. Browning intensity increased with decreasing MW of DX. Fluorescence emission of WPI incubated increased, but decreased in WPI/DX incubated systems. The gelation time (obtained by G′–G″ crossover) and G′ value at 25 °C increased in conjugate systems compared with WPI alone. Stability of gel structures were shown by frequency sweeps.
Fil: Spotti, Maria Julia. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Candioti, Mario César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina
Fil: Rubiolo, Amelia Catalina. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Carrara, Carlos Roberto. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Whey Proteins
Dextrans
Maillard Conjugation
Rheological Properties
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:11336/30651
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/30651
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systemsSpotti, Maria JuliaMartinez, María JuliaPilosof, Ana Maria RenataCandioti, Mario CésarRubiolo, Amelia CatalinaCarrara, Carlos RobertoWhey ProteinsDextransMaillard ConjugationRheological Propertieshttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3It is well known that protein/polysaccharide conjugates obtained by Maillard reaction (MR) have good emulsifying properties. However, there is little information about the use of these conjugates in gel systems. Structural characteristics and rheological properties of conjugates obtained by MR of whey protein isolate (WPI) and dextrans (DX) of various molecular weight (MW: 6, 40 and 70 kDa) were studied. Conjugation was confirmed by electrophoresis; browning intensity was measured by absorbance at 420 nm; and conformational changes were studied by fluorescence emission of tryptophan (Trp) (λex = 280 nm). Rheological properties were determined by oscillatory rheometry with temperature ramp (25–90 °C). After each measure, a mechanical spectrum (at 25 °C) was obtained. The electrophoresis indicated the presence of WPI/DX conjugates in all systems. Browning intensity increased with decreasing MW of DX. Fluorescence emission of WPI incubated increased, but decreased in WPI/DX incubated systems. The gelation time (obtained by G′–G″ crossover) and G′ value at 25 °C increased in conjugate systems compared with WPI alone. Stability of gel structures were shown by frequency sweeps.Fil: Spotti, Maria Julia. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Candioti, Mario César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; ArgentinaFil: Rubiolo, Amelia Catalina. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Carrara, Carlos Roberto. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2014-01info: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/11336/30651Spotti, Maria Julia; Martinez, María Julia; Pilosof, Ana Maria Renata; Candioti, Mario César; Rubiolo, Amelia Catalina; et al.; Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems; Elsevier; Food Hydrocolloids; 39; 1-2014; 223-2300268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2014.01.014info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X14000320info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:54:04Zoai:ri.conicet.gov.ar:11336/30651instacron: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 09:54:04.515CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
title Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
spellingShingle Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
Spotti, Maria Julia
Whey Proteins
Dextrans
Maillard Conjugation
Rheological Properties
title_short Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
title_full Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
title_fullStr Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
title_full_unstemmed Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
title_sort Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems
dc.creator.none.fl_str_mv Spotti, Maria Julia
Martinez, María Julia
Pilosof, Ana Maria Renata
Candioti, Mario César
Rubiolo, Amelia Catalina
Carrara, Carlos Roberto
author Spotti, Maria Julia
author_facet Spotti, Maria Julia
Martinez, María Julia
Pilosof, Ana Maria Renata
Candioti, Mario César
Rubiolo, Amelia Catalina
Carrara, Carlos Roberto
author_role author
author2 Martinez, María Julia
Pilosof, Ana Maria Renata
Candioti, Mario César
Rubiolo, Amelia Catalina
Carrara, Carlos Roberto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Whey Proteins
Dextrans
Maillard Conjugation
Rheological Properties
topic Whey Proteins
Dextrans
Maillard Conjugation
Rheological Properties
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv It is well known that protein/polysaccharide conjugates obtained by Maillard reaction (MR) have good emulsifying properties. However, there is little information about the use of these conjugates in gel systems. Structural characteristics and rheological properties of conjugates obtained by MR of whey protein isolate (WPI) and dextrans (DX) of various molecular weight (MW: 6, 40 and 70 kDa) were studied. Conjugation was confirmed by electrophoresis; browning intensity was measured by absorbance at 420 nm; and conformational changes were studied by fluorescence emission of tryptophan (Trp) (λex = 280 nm). Rheological properties were determined by oscillatory rheometry with temperature ramp (25–90 °C). After each measure, a mechanical spectrum (at 25 °C) was obtained. The electrophoresis indicated the presence of WPI/DX conjugates in all systems. Browning intensity increased with decreasing MW of DX. Fluorescence emission of WPI incubated increased, but decreased in WPI/DX incubated systems. The gelation time (obtained by G′–G″ crossover) and G′ value at 25 °C increased in conjugate systems compared with WPI alone. Stability of gel structures were shown by frequency sweeps.
Fil: Spotti, Maria Julia. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Martinez, María Julia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Candioti, Mario César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina
Fil: Rubiolo, Amelia Catalina. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Carrara, Carlos Roberto. Universidad Nacional del Litoral. Facultad de Ingeniería Química; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description It is well known that protein/polysaccharide conjugates obtained by Maillard reaction (MR) have good emulsifying properties. However, there is little information about the use of these conjugates in gel systems. Structural characteristics and rheological properties of conjugates obtained by MR of whey protein isolate (WPI) and dextrans (DX) of various molecular weight (MW: 6, 40 and 70 kDa) were studied. Conjugation was confirmed by electrophoresis; browning intensity was measured by absorbance at 420 nm; and conformational changes were studied by fluorescence emission of tryptophan (Trp) (λex = 280 nm). Rheological properties were determined by oscillatory rheometry with temperature ramp (25–90 °C). After each measure, a mechanical spectrum (at 25 °C) was obtained. The electrophoresis indicated the presence of WPI/DX conjugates in all systems. Browning intensity increased with decreasing MW of DX. Fluorescence emission of WPI incubated increased, but decreased in WPI/DX incubated systems. The gelation time (obtained by G′–G″ crossover) and G′ value at 25 °C increased in conjugate systems compared with WPI alone. Stability of gel structures were shown by frequency sweeps.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
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/11336/30651
Spotti, Maria Julia; Martinez, María Julia; Pilosof, Ana Maria Renata; Candioti, Mario César; Rubiolo, Amelia Catalina; et al.; Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems; Elsevier; Food Hydrocolloids; 39; 1-2014; 223-230
0268-005X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/30651
identifier_str_mv Spotti, Maria Julia; Martinez, María Julia; Pilosof, Ana Maria Renata; Candioti, Mario César; Rubiolo, Amelia Catalina; et al.; Influence of Maillard conjugation on structural characteristics and rheological properties of whey protein/dextran systems; Elsevier; Food Hydrocolloids; 39; 1-2014; 223-230
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/doi/10.1016/j.foodhyd.2014.01.014
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X14000320
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
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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score 13.070432

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