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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/92948
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:05:36Zoai: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:34982025-09-29 10:05:37.067CONICET 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 |
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1844613894378618880 |
score |
13.070432 |