Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles

Autores
Berino, Romina Paola; Báez, Germán David; Ballerini, Griselda A.; Llopart, Emilce Elina; Busti, Pablo Andres; Moro, Andrea; Delorenzi, Nestor Jorge
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Interaction between vitamin D3 with beta-lactoglobulin (β-LG) was studied by turbidimetric measurements covering vitamin concentrations up to 500 μM, within a wide range of vitamin concentration and at high vitamin/protein ratios, both conditions that have not been assayed in previous studies. Turbidity of vitamin D3 in the absence and presence of β-LG (20, 40 and 100 μM) in 20 mM phosphate buffer at pH 7.0 proved the expected vitamin-protein interaction as well as the effect of protein concentration. In order to estimate the proportion of bound vitamin in the vitamin-protein complex, a binding parameter (BP) was defined and its dependence on protein concentration was analysed. Fluorescence quenching with acrylamide for 100 μM vitamin D3 and 20 μM β-LG in 20 mM phosphate buffer at pH 7.0, suggested vitamin D3 interact in the hydrophobic calix in the protein. Circular dichroism experiments showed the binding of the vitamin causes conformational changes in the secondary protein structure. Particle size and zeta potential determinations were also carried out in order to establish possible conformational models of interaction vitamin-protein. The higher the vitamin concentration, the greater the bound vitamin proportion was; which could be due to a cooperative phenomenon and/or a stacking process. These studies would be useful for a better understanding of the β-LG properties as a carrier of hydrophobic vitamins or other hydrophobic nutraceuticals in order to enrich non-fat foods.
Fil: Berino, Romina Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Báez, Germán David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Llopart, Emilce Elina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Materia
BETA-LACTOGLOBULIN
BINDING SITE
CONFORMATIONAL CHANGE
NANOPARTICLE SIZE
STACKING PROCESS
VITAMIN D3
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:11336/127683
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/127683
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticlesBerino, Romina PaolaBáez, Germán DavidBallerini, Griselda A.Llopart, Emilce ElinaBusti, Pablo AndresMoro, AndreaDelorenzi, Nestor JorgeBETA-LACTOGLOBULINBINDING SITECONFORMATIONAL CHANGENANOPARTICLE SIZESTACKING PROCESSVITAMIN D3https://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Interaction between vitamin D3 with beta-lactoglobulin (β-LG) was studied by turbidimetric measurements covering vitamin concentrations up to 500 μM, within a wide range of vitamin concentration and at high vitamin/protein ratios, both conditions that have not been assayed in previous studies. Turbidity of vitamin D3 in the absence and presence of β-LG (20, 40 and 100 μM) in 20 mM phosphate buffer at pH 7.0 proved the expected vitamin-protein interaction as well as the effect of protein concentration. In order to estimate the proportion of bound vitamin in the vitamin-protein complex, a binding parameter (BP) was defined and its dependence on protein concentration was analysed. Fluorescence quenching with acrylamide for 100 μM vitamin D3 and 20 μM β-LG in 20 mM phosphate buffer at pH 7.0, suggested vitamin D3 interact in the hydrophobic calix in the protein. Circular dichroism experiments showed the binding of the vitamin causes conformational changes in the secondary protein structure. Particle size and zeta potential determinations were also carried out in order to establish possible conformational models of interaction vitamin-protein. The higher the vitamin concentration, the greater the bound vitamin proportion was; which could be due to a cooperative phenomenon and/or a stacking process. These studies would be useful for a better understanding of the β-LG properties as a carrier of hydrophobic vitamins or other hydrophobic nutraceuticals in order to enrich non-fat foods.Fil: Berino, Romina Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Báez, Germán David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; ArgentinaFil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Instituto Nacional de Tecnología Agropecuaria; ArgentinaFil: Llopart, Emilce Elina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; ArgentinaFil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaElsevier2019-05info: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/11336/127683Berino, Romina Paola; Báez, Germán David; Ballerini, Griselda A.; Llopart, Emilce Elina; Busti, Pablo Andres; et al.; Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles; Elsevier; Food Hydrocolloids; 90; 5-2019; 182-1880268-005XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0268005X18311408info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2018.11.027info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-06T12:13:54Zoai:ri.conicet.gov.ar:11336/127683instacron: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:34982026-02-06 12:13:54.59CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
title Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
spellingShingle Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
Berino, Romina Paola
BETA-LACTOGLOBULIN
BINDING SITE
CONFORMATIONAL CHANGE
NANOPARTICLE SIZE
STACKING PROCESS
VITAMIN D3
title_short Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
title_full Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
title_fullStr Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
title_full_unstemmed Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
title_sort Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles
dc.creator.none.fl_str_mv Berino, Romina Paola
Báez, Germán David
Ballerini, Griselda A.
Llopart, Emilce Elina
Busti, Pablo Andres
Moro, Andrea
Delorenzi, Nestor Jorge
author Berino, Romina Paola
author_facet Berino, Romina Paola
Báez, Germán David
Ballerini, Griselda A.
Llopart, Emilce Elina
Busti, Pablo Andres
Moro, Andrea
Delorenzi, Nestor Jorge
author_role author
author2 Báez, Germán David
Ballerini, Griselda A.
Llopart, Emilce Elina
Busti, Pablo Andres
Moro, Andrea
Delorenzi, Nestor Jorge
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv BETA-LACTOGLOBULIN
BINDING SITE
CONFORMATIONAL CHANGE
NANOPARTICLE SIZE
STACKING PROCESS
VITAMIN D3
topic BETA-LACTOGLOBULIN
BINDING SITE
CONFORMATIONAL CHANGE
NANOPARTICLE SIZE
STACKING PROCESS
VITAMIN D3
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Interaction between vitamin D3 with beta-lactoglobulin (β-LG) was studied by turbidimetric measurements covering vitamin concentrations up to 500 μM, within a wide range of vitamin concentration and at high vitamin/protein ratios, both conditions that have not been assayed in previous studies. Turbidity of vitamin D3 in the absence and presence of β-LG (20, 40 and 100 μM) in 20 mM phosphate buffer at pH 7.0 proved the expected vitamin-protein interaction as well as the effect of protein concentration. In order to estimate the proportion of bound vitamin in the vitamin-protein complex, a binding parameter (BP) was defined and its dependence on protein concentration was analysed. Fluorescence quenching with acrylamide for 100 μM vitamin D3 and 20 μM β-LG in 20 mM phosphate buffer at pH 7.0, suggested vitamin D3 interact in the hydrophobic calix in the protein. Circular dichroism experiments showed the binding of the vitamin causes conformational changes in the secondary protein structure. Particle size and zeta potential determinations were also carried out in order to establish possible conformational models of interaction vitamin-protein. The higher the vitamin concentration, the greater the bound vitamin proportion was; which could be due to a cooperative phenomenon and/or a stacking process. These studies would be useful for a better understanding of the β-LG properties as a carrier of hydrophobic vitamins or other hydrophobic nutraceuticals in order to enrich non-fat foods.
Fil: Berino, Romina Paola. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Báez, Germán David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina
Fil: Ballerini, Griselda A.. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Llopart, Emilce Elina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Busti, Pablo Andres. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Moro, Andrea. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Tecnología; Argentina
Fil: Delorenzi, Nestor Jorge. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
description Interaction between vitamin D3 with beta-lactoglobulin (β-LG) was studied by turbidimetric measurements covering vitamin concentrations up to 500 μM, within a wide range of vitamin concentration and at high vitamin/protein ratios, both conditions that have not been assayed in previous studies. Turbidity of vitamin D3 in the absence and presence of β-LG (20, 40 and 100 μM) in 20 mM phosphate buffer at pH 7.0 proved the expected vitamin-protein interaction as well as the effect of protein concentration. In order to estimate the proportion of bound vitamin in the vitamin-protein complex, a binding parameter (BP) was defined and its dependence on protein concentration was analysed. Fluorescence quenching with acrylamide for 100 μM vitamin D3 and 20 μM β-LG in 20 mM phosphate buffer at pH 7.0, suggested vitamin D3 interact in the hydrophobic calix in the protein. Circular dichroism experiments showed the binding of the vitamin causes conformational changes in the secondary protein structure. Particle size and zeta potential determinations were also carried out in order to establish possible conformational models of interaction vitamin-protein. The higher the vitamin concentration, the greater the bound vitamin proportion was; which could be due to a cooperative phenomenon and/or a stacking process. These studies would be useful for a better understanding of the β-LG properties as a carrier of hydrophobic vitamins or other hydrophobic nutraceuticals in order to enrich non-fat foods.
publishDate 2019
dc.date.none.fl_str_mv 2019-05
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/11336/127683
Berino, Romina Paola; Báez, Germán David; Ballerini, Griselda A.; Llopart, Emilce Elina; Busti, Pablo Andres; et al.; Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles; Elsevier; Food Hydrocolloids; 90; 5-2019; 182-188
0268-005X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/127683
identifier_str_mv Berino, Romina Paola; Báez, Germán David; Ballerini, Griselda A.; Llopart, Emilce Elina; Busti, Pablo Andres; et al.; Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles; Elsevier; Food Hydrocolloids; 90; 5-2019; 182-188
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/https://www.sciencedirect.com/science/article/abs/pii/S0268005X18311408
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2018.11.027
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 13.11174

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