Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins

Autores
Medrano, A.; Abirached, C.; Araujo, A. C.; Panizzolo, L. A.; Moyna, P.; Añon, Maria Cristina
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A comparative study on the behavior in the air–water interface of b-lactoglobulin, a-lactoalbumin, glycinin and b-conglycinin was performed. The behavior at the interface was evaluated by equilibrium surface tension and surface rheological properties of adsorbed films. There were significant differences (a 0.05) in the values of the constants of adsorption to the interface of the four proteins. The glycinin had the slowest rate of adsorption, due to its low average hydrophobicity, low molecular flexibility and large molecular size. Smaller proteins like b-lactoglobulin and a-lactoalbumin tended to greater equilibrium pressure values than the larger proteins because of its higher rate of adsorption to the interface. The foam capacity of proteins showed a positive correlation with the average hydrophobicity; the maximal retained liquid volume or the initial rate of passage of liquid to foam were significantly lower (a 0.05) when protein was glycinin. The dilatational modulus of glycinin was the lowest, which implies lowest resistance to disruption of the film. Glycinin protein has lower proportion of gravitational drainage and higher disproportionation having perhaps a less resistant film. In conclusion, b-conglycinin and whey proteins showed a similar behavior, so b-conglycinin might be the best soybean protein to replace milk proteins in food formulations.
Fil: Medrano, A.. Universidad de la Republica; Uruguay
Fil: Abirached, C.. Universidad de la Republica; Uruguay
Fil: Araujo, A. C.. Universidad de la Republica; Uruguay
Fil: Panizzolo, L. A.. Universidad de la Republica; Uruguay
Fil: Moyna, P.. Universidad de la Republica; Uruguay
Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata; Argentina
Materia
Soy Proteins
Milk Whey Proteins
Interfacial Rheology
Foams
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:11336/10581
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/10581
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteinsMedrano, A.Abirached, C.Araujo, A. C.Panizzolo, L. A.Moyna, P.Añon, Maria CristinaSoy ProteinsMilk Whey ProteinsInterfacial RheologyFoamshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2A comparative study on the behavior in the air–water interface of b-lactoglobulin, a-lactoalbumin, glycinin and b-conglycinin was performed. The behavior at the interface was evaluated by equilibrium surface tension and surface rheological properties of adsorbed films. There were significant differences (a 0.05) in the values of the constants of adsorption to the interface of the four proteins. The glycinin had the slowest rate of adsorption, due to its low average hydrophobicity, low molecular flexibility and large molecular size. Smaller proteins like b-lactoglobulin and a-lactoalbumin tended to greater equilibrium pressure values than the larger proteins because of its higher rate of adsorption to the interface. The foam capacity of proteins showed a positive correlation with the average hydrophobicity; the maximal retained liquid volume or the initial rate of passage of liquid to foam were significantly lower (a 0.05) when protein was glycinin. The dilatational modulus of glycinin was the lowest, which implies lowest resistance to disruption of the film. Glycinin protein has lower proportion of gravitational drainage and higher disproportionation having perhaps a less resistant film. In conclusion, b-conglycinin and whey proteins showed a similar behavior, so b-conglycinin might be the best soybean protein to replace milk proteins in food formulations.Fil: Medrano, A.. Universidad de la Republica; UruguayFil: Abirached, C.. Universidad de la Republica; UruguayFil: Araujo, A. C.. Universidad de la Republica; UruguayFil: Panizzolo, L. A.. Universidad de la Republica; UruguayFil: Moyna, P.. Universidad de la Republica; UruguayFil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata; ArgentinaSage Publications Ltd2012-03-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10581Medrano, A.; Abirached, C.; Araujo, A. C.; Panizzolo, L. A.; Moyna, P.; et al.; Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins; Sage Publications Ltd; Food Science and Technology International; 18; 2; 13-3-2012; 187-1931082-01321532-1738enginfo:eu-repo/semantics/altIdentifier/doi/10.1177/1082013211415137info:eu-repo/semantics/altIdentifier/url/https://journals.sagepub.com/doi/10.1177/1082013211415137info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:02:05Zoai:ri.conicet.gov.ar:11336/10581instacron: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 13:02:05.326CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
title Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
spellingShingle Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
Medrano, A.
Soy Proteins
Milk Whey Proteins
Interfacial Rheology
Foams
title_short Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
title_full Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
title_fullStr Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
title_full_unstemmed Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
title_sort Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins
dc.creator.none.fl_str_mv Medrano, A.
Abirached, C.
Araujo, A. C.
Panizzolo, L. A.
Moyna, P.
Añon, Maria Cristina
author Medrano, A.
author_facet Medrano, A.
Abirached, C.
Araujo, A. C.
Panizzolo, L. A.
Moyna, P.
Añon, Maria Cristina
author_role author
author2 Abirached, C.
Araujo, A. C.
Panizzolo, L. A.
Moyna, P.
Añon, Maria Cristina
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Soy Proteins
Milk Whey Proteins
Interfacial Rheology
Foams
topic Soy Proteins
Milk Whey Proteins
Interfacial Rheology
Foams
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv A comparative study on the behavior in the air–water interface of b-lactoglobulin, a-lactoalbumin, glycinin and b-conglycinin was performed. The behavior at the interface was evaluated by equilibrium surface tension and surface rheological properties of adsorbed films. There were significant differences (a 0.05) in the values of the constants of adsorption to the interface of the four proteins. The glycinin had the slowest rate of adsorption, due to its low average hydrophobicity, low molecular flexibility and large molecular size. Smaller proteins like b-lactoglobulin and a-lactoalbumin tended to greater equilibrium pressure values than the larger proteins because of its higher rate of adsorption to the interface. The foam capacity of proteins showed a positive correlation with the average hydrophobicity; the maximal retained liquid volume or the initial rate of passage of liquid to foam were significantly lower (a 0.05) when protein was glycinin. The dilatational modulus of glycinin was the lowest, which implies lowest resistance to disruption of the film. Glycinin protein has lower proportion of gravitational drainage and higher disproportionation having perhaps a less resistant film. In conclusion, b-conglycinin and whey proteins showed a similar behavior, so b-conglycinin might be the best soybean protein to replace milk proteins in food formulations.
Fil: Medrano, A.. Universidad de la Republica; Uruguay
Fil: Abirached, C.. Universidad de la Republica; Uruguay
Fil: Araujo, A. C.. Universidad de la Republica; Uruguay
Fil: Panizzolo, L. A.. Universidad de la Republica; Uruguay
Fil: Moyna, P.. Universidad de la Republica; Uruguay
Fil: Añon, Maria Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigaciones en Criotecnología de Alimentos (i); Argentina. Universidad Nacional de La Plata; Argentina
description A comparative study on the behavior in the air–water interface of b-lactoglobulin, a-lactoalbumin, glycinin and b-conglycinin was performed. The behavior at the interface was evaluated by equilibrium surface tension and surface rheological properties of adsorbed films. There were significant differences (a 0.05) in the values of the constants of adsorption to the interface of the four proteins. The glycinin had the slowest rate of adsorption, due to its low average hydrophobicity, low molecular flexibility and large molecular size. Smaller proteins like b-lactoglobulin and a-lactoalbumin tended to greater equilibrium pressure values than the larger proteins because of its higher rate of adsorption to the interface. The foam capacity of proteins showed a positive correlation with the average hydrophobicity; the maximal retained liquid volume or the initial rate of passage of liquid to foam were significantly lower (a 0.05) when protein was glycinin. The dilatational modulus of glycinin was the lowest, which implies lowest resistance to disruption of the film. Glycinin protein has lower proportion of gravitational drainage and higher disproportionation having perhaps a less resistant film. In conclusion, b-conglycinin and whey proteins showed a similar behavior, so b-conglycinin might be the best soybean protein to replace milk proteins in food formulations.
publishDate 2012
dc.date.none.fl_str_mv 2012-03-13
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/11336/10581
Medrano, A.; Abirached, C.; Araujo, A. C.; Panizzolo, L. A.; Moyna, P.; et al.; Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins; Sage Publications Ltd; Food Science and Technology International; 18; 2; 13-3-2012; 187-193
1082-0132
1532-1738
url http://hdl.handle.net/11336/10581
identifier_str_mv Medrano, A.; Abirached, C.; Araujo, A. C.; Panizzolo, L. A.; Moyna, P.; et al.; Correlation of average hydrophobicity, water/air interface surface rheological properties and foaming properties of proteins; Sage Publications Ltd; Food Science and Technology International; 18; 2; 13-3-2012; 187-193
1082-0132
1532-1738
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1177/1082013211415137
info:eu-repo/semantics/altIdentifier/url/https://journals.sagepub.com/doi/10.1177/1082013211415137
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
dc.publisher.none.fl_str_mv Sage Publications Ltd
publisher.none.fl_str_mv Sage Publications Ltd
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_ 1842979992562040832
score 12.993085

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