Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs
- Autores
- Sponton, Osvaldo Ernesto; Perez, Adrián Alejandro; Carrara, Carlos R.; Santiago, Liliana G.
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In this work, OVA heat-induced aggregates were obtained by controlled heat treatment varying temperature (60, 70 and 80ºC), heating time (3, 5 and10 min), aqueous medium pH (5.5, 6.0 and 6.5) and protein concentration (5, 10 and 14.2 g/L). Particle size distribution and surface characteristics derived from fluorescence spectroscopy (both intrinsic and extrinsic) were determined. Evaluation of these physicochemical properties allowed knowing experimental conditions under which nanometric OVA aggregates (OVAn), with suitable surface hydrophobicity, could be produced. OVAn ability to bind polyunsaturated fatty acid (PUFA) was carried out by turbidity measurement. In these experiments, linoleic acid (LA) was used as a PUFA model. In general, OVA aggregate sizes increased with temperature, time and protein concentration, furthermore at higher pH value, OVA aggregate sizes were lower. OVA aggregates surface hydrophobicity increased with rising heating temperature and the pH value indicating, on one hand, larger protein unfolding and on the other hand lower aggregation via hydrophobic interaction at higher pH value, respectively. However, surface hydrophobicity decreased with concentration suggesting greater aggregation. OVAn obtained at 70°C, 10 g/L, pH 6-6.5 and 70°C, 5 g/L, pH 6 were assayed by LA binding ability. This property was 1.4-2.0 folds greater than for native OVA. Information derived from this work could be of practical interest for the development of innovative PUFAs carrier systems.
Fil: Sponton, Osvaldo Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Perez, Adrián Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Carrara, Carlos R.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Santiago, Liliana G.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina - Materia
-
Ovalbumin
Heat-Induced Aggregation
Nanoparticles
Linoleic Acid
Fluorescence
Polyunsaturated Fatty Acids - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/16798
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Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAsSponton, Osvaldo ErnestoPerez, Adrián AlejandroCarrara, Carlos R.Santiago, Liliana G.OvalbuminHeat-Induced AggregationNanoparticlesLinoleic AcidFluorescencePolyunsaturated Fatty Acidshttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2In this work, OVA heat-induced aggregates were obtained by controlled heat treatment varying temperature (60, 70 and 80ºC), heating time (3, 5 and10 min), aqueous medium pH (5.5, 6.0 and 6.5) and protein concentration (5, 10 and 14.2 g/L). Particle size distribution and surface characteristics derived from fluorescence spectroscopy (both intrinsic and extrinsic) were determined. Evaluation of these physicochemical properties allowed knowing experimental conditions under which nanometric OVA aggregates (OVAn), with suitable surface hydrophobicity, could be produced. OVAn ability to bind polyunsaturated fatty acid (PUFA) was carried out by turbidity measurement. In these experiments, linoleic acid (LA) was used as a PUFA model. In general, OVA aggregate sizes increased with temperature, time and protein concentration, furthermore at higher pH value, OVA aggregate sizes were lower. OVA aggregates surface hydrophobicity increased with rising heating temperature and the pH value indicating, on one hand, larger protein unfolding and on the other hand lower aggregation via hydrophobic interaction at higher pH value, respectively. However, surface hydrophobicity decreased with concentration suggesting greater aggregation. OVAn obtained at 70°C, 10 g/L, pH 6-6.5 and 70°C, 5 g/L, pH 6 were assayed by LA binding ability. This property was 1.4-2.0 folds greater than for native OVA. Information derived from this work could be of practical interest for the development of innovative PUFAs carrier systems.Fil: Sponton, Osvaldo Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Perez, Adrián Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Carrara, Carlos R.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Santiago, Liliana G.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaElsevier2015-06info: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/11336/16798Sponton, Osvaldo Ernesto; Perez, Adrián Alejandro; Carrara, Carlos R.; Santiago, Liliana G.; Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs; Elsevier; Food Hydrocolloids; 48; 6-2015; 165-1730268-005Xenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2015.02.011info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X15000727info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:14:47Zoai:ri.conicet.gov.ar:11336/16798instacron: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:34982025-09-10 13:14:48.139CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
title |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
spellingShingle |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs Sponton, Osvaldo Ernesto Ovalbumin Heat-Induced Aggregation Nanoparticles Linoleic Acid Fluorescence Polyunsaturated Fatty Acids |
title_short |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
title_full |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
title_fullStr |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
title_full_unstemmed |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
title_sort |
Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs |
dc.creator.none.fl_str_mv |
Sponton, Osvaldo Ernesto Perez, Adrián Alejandro Carrara, Carlos R. Santiago, Liliana G. |
author |
Sponton, Osvaldo Ernesto |
author_facet |
Sponton, Osvaldo Ernesto Perez, Adrián Alejandro Carrara, Carlos R. Santiago, Liliana G. |
author_role |
author |
author2 |
Perez, Adrián Alejandro Carrara, Carlos R. Santiago, Liliana G. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Ovalbumin Heat-Induced Aggregation Nanoparticles Linoleic Acid Fluorescence Polyunsaturated Fatty Acids |
topic |
Ovalbumin Heat-Induced Aggregation Nanoparticles Linoleic Acid Fluorescence Polyunsaturated Fatty Acids |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.10 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
In this work, OVA heat-induced aggregates were obtained by controlled heat treatment varying temperature (60, 70 and 80ºC), heating time (3, 5 and10 min), aqueous medium pH (5.5, 6.0 and 6.5) and protein concentration (5, 10 and 14.2 g/L). Particle size distribution and surface characteristics derived from fluorescence spectroscopy (both intrinsic and extrinsic) were determined. Evaluation of these physicochemical properties allowed knowing experimental conditions under which nanometric OVA aggregates (OVAn), with suitable surface hydrophobicity, could be produced. OVAn ability to bind polyunsaturated fatty acid (PUFA) was carried out by turbidity measurement. In these experiments, linoleic acid (LA) was used as a PUFA model. In general, OVA aggregate sizes increased with temperature, time and protein concentration, furthermore at higher pH value, OVA aggregate sizes were lower. OVA aggregates surface hydrophobicity increased with rising heating temperature and the pH value indicating, on one hand, larger protein unfolding and on the other hand lower aggregation via hydrophobic interaction at higher pH value, respectively. However, surface hydrophobicity decreased with concentration suggesting greater aggregation. OVAn obtained at 70°C, 10 g/L, pH 6-6.5 and 70°C, 5 g/L, pH 6 were assayed by LA binding ability. This property was 1.4-2.0 folds greater than for native OVA. Information derived from this work could be of practical interest for the development of innovative PUFAs carrier systems. Fil: Sponton, Osvaldo Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina Fil: Perez, Adrián Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina Fil: Carrara, Carlos R.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina Fil: Santiago, Liliana G.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina |
description |
In this work, OVA heat-induced aggregates were obtained by controlled heat treatment varying temperature (60, 70 and 80ºC), heating time (3, 5 and10 min), aqueous medium pH (5.5, 6.0 and 6.5) and protein concentration (5, 10 and 14.2 g/L). Particle size distribution and surface characteristics derived from fluorescence spectroscopy (both intrinsic and extrinsic) were determined. Evaluation of these physicochemical properties allowed knowing experimental conditions under which nanometric OVA aggregates (OVAn), with suitable surface hydrophobicity, could be produced. OVAn ability to bind polyunsaturated fatty acid (PUFA) was carried out by turbidity measurement. In these experiments, linoleic acid (LA) was used as a PUFA model. In general, OVA aggregate sizes increased with temperature, time and protein concentration, furthermore at higher pH value, OVA aggregate sizes were lower. OVA aggregates surface hydrophobicity increased with rising heating temperature and the pH value indicating, on one hand, larger protein unfolding and on the other hand lower aggregation via hydrophobic interaction at higher pH value, respectively. However, surface hydrophobicity decreased with concentration suggesting greater aggregation. OVAn obtained at 70°C, 10 g/L, pH 6-6.5 and 70°C, 5 g/L, pH 6 were assayed by LA binding ability. This property was 1.4-2.0 folds greater than for native OVA. Information derived from this work could be of practical interest for the development of innovative PUFAs carrier systems. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-06 |
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/11336/16798 Sponton, Osvaldo Ernesto; Perez, Adrián Alejandro; Carrara, Carlos R.; Santiago, Liliana G.; Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs; Elsevier; Food Hydrocolloids; 48; 6-2015; 165-173 0268-005X |
url |
http://hdl.handle.net/11336/16798 |
identifier_str_mv |
Sponton, Osvaldo Ernesto; Perez, Adrián Alejandro; Carrara, Carlos R.; Santiago, Liliana G.; Impact of evironment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs; Elsevier; Food Hydrocolloids; 48; 6-2015; 165-173 0268-005X |
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.2015.02.011 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X15000727 |
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 |
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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1842980793432932352 |
score |
12.993085 |