On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers

Autores
Zema, Paula Daniela; Pilosof, Ana Maria Renata
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under conditions of concentration (up to 5% w/w) and pH (3–7) that could have a technological application has been studied. The degree of folic acid binding to the proteins depended on their pH-dependent ζ-potential, indicating the occurrence of ionic bonds. Regardless of FA concentration, the percentage of bound FA to β-lg or G was 100% at pH 3. At pH 3, the size of particles strongly increased by increasing the molar FA/protein ratio. Protein aggregation and further flocculation was observed at higher molar ratios. However, the size of particles could be modulated by high intensity ultrasound application. FA/protein particles formed at pH 3 were totally reversible by shifting back the pH to 7. This pH dependence is strongly favorable for the delivery of FA at the duodene (pH 7) and for the protection of FA at the pH prevailing in the stomach (pH 3).
Fil: Zema, Paula Daniela. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
Materia
AGGREGATION
DELIVERY
FOLIC ACID
GELATIN
PH
Β-LACTOGLOBULIN
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:11336/92948
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling On the binding of folic acid to food proteins performing as vitamin micro/nanocarriersZema, Paula DanielaPilosof, Ana Maria RenataAGGREGATIONDELIVERYFOLIC ACIDGELATINPHΒ-LACTOGLOBULINhttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under conditions of concentration (up to 5% w/w) and pH (3–7) that could have a technological application has been studied. The degree of folic acid binding to the proteins depended on their pH-dependent ζ-potential, indicating the occurrence of ionic bonds. Regardless of FA concentration, the percentage of bound FA to β-lg or G was 100% at pH 3. At pH 3, the size of particles strongly increased by increasing the molar FA/protein ratio. Protein aggregation and further flocculation was observed at higher molar ratios. However, the size of particles could be modulated by high intensity ultrasound application. FA/protein particles formed at pH 3 were totally reversible by shifting back the pH to 7. This pH dependence is strongly favorable for the delivery of FA at the duodene (pH 7) and for the protection of FA at the pH prevailing in the stomach (pH 3).Fil: Zema, Paula Daniela. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; ArgentinaFil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; ArgentinaElsevier2018-06info: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/11336/92948Zema, Paula Daniela; Pilosof, Ana Maria Renata; On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers; Elsevier; Food Hydrocolloids; 79; 6-2018; 509-5170268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0268005X17316120info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2018.01.021info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:02:20Zoai:ri.conicet.gov.ar:11336/92948instacron: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:34982025-10-15 15:02:20.868CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
spellingShingle On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
Zema, Paula Daniela
AGGREGATION
DELIVERY
FOLIC ACID
GELATIN
PH
Β-LACTOGLOBULIN
title_short On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_full On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_fullStr On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_full_unstemmed On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_sort On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
dc.creator.none.fl_str_mv Zema, Paula Daniela
Pilosof, Ana Maria Renata
author Zema, Paula Daniela
author_facet Zema, Paula Daniela
Pilosof, Ana Maria Renata
author_role author
author2 Pilosof, Ana Maria Renata
author2_role author
dc.subject.none.fl_str_mv AGGREGATION
DELIVERY
FOLIC ACID
GELATIN
PH
Β-LACTOGLOBULIN
topic AGGREGATION
DELIVERY
FOLIC ACID
GELATIN
PH
Β-LACTOGLOBULIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.10
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under conditions of concentration (up to 5% w/w) and pH (3–7) that could have a technological application has been studied. The degree of folic acid binding to the proteins depended on their pH-dependent ζ-potential, indicating the occurrence of ionic bonds. Regardless of FA concentration, the percentage of bound FA to β-lg or G was 100% at pH 3. At pH 3, the size of particles strongly increased by increasing the molar FA/protein ratio. Protein aggregation and further flocculation was observed at higher molar ratios. However, the size of particles could be modulated by high intensity ultrasound application. FA/protein particles formed at pH 3 were totally reversible by shifting back the pH to 7. This pH dependence is strongly favorable for the delivery of FA at the duodene (pH 7) and for the protection of FA at the pH prevailing in the stomach (pH 3).
Fil: Zema, Paula Daniela. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
Fil: Pilosof, Ana Maria Renata. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Quimicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Quimicos.; Argentina
description Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under conditions of concentration (up to 5% w/w) and pH (3–7) that could have a technological application has been studied. The degree of folic acid binding to the proteins depended on their pH-dependent ζ-potential, indicating the occurrence of ionic bonds. Regardless of FA concentration, the percentage of bound FA to β-lg or G was 100% at pH 3. At pH 3, the size of particles strongly increased by increasing the molar FA/protein ratio. Protein aggregation and further flocculation was observed at higher molar ratios. However, the size of particles could be modulated by high intensity ultrasound application. FA/protein particles formed at pH 3 were totally reversible by shifting back the pH to 7. This pH dependence is strongly favorable for the delivery of FA at the duodene (pH 7) and for the protection of FA at the pH prevailing in the stomach (pH 3).
publishDate 2018
dc.date.none.fl_str_mv 2018-06
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/11336/92948
Zema, Paula Daniela; Pilosof, Ana Maria Renata; On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers; Elsevier; Food Hydrocolloids; 79; 6-2018; 509-517
0268-005X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/92948
identifier_str_mv Zema, Paula Daniela; Pilosof, Ana Maria Renata; On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers; Elsevier; Food Hydrocolloids; 79; 6-2018; 509-517
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/http://linkinghub.elsevier.com/retrieve/pii/S0268005X17316120
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2018.01.021
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 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
_version_ 1846083164910387200
score 13.22299

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