Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension

Autores
Bacigalupe, Alejandro; Poliszuk, Andrea K.; Eisenberg, Patricia; Escobar, Mariano Martin
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The goal of this work is to study the rheological properties of based-modified soy protein concentrate (SPC) adhesives and the relationship between viscoelastic properties and bonding performance. Chemical modification of SPC with sodium hydroxide was made to evaluate the effect of alkali on the viscoelastic properties. Viscosity and solubility depends directly of the 3D structure and the isoelectric point (pI) of the protein. Results show that viscosity is strongly pH dependant due to the protein unfolding. Solubility profiles exhibit the typical U-shaped curve, being higher on either side of isoelectric point. Fourier transformed infrared analysis was used to analyze Amide I (1720-1600 cm-1) and Amide III (1400-1200cm-1) band patterns which reflect the different secondary structures in proteins. The intensity of the band at 1250 cm-1 increases with respect to that at 1235 cm-1 for higher pH values. This could be associated with the destruction, at least partially, of the β-sheet structure. Bonding performance was measured in dry conditions and the wetting properties were analyzed by scanning electron microscopy. The bonding performance improves when the SPC is stabilized at pH 12 due to the protein unfolding, revealing a strong interaction between the secondary structure and the wood surface. As part of an ongoing project it was concluded that alkali modification is a suitable procedure to modify a protein suspension, improving application conditions and mechanical properties of bioadhesives of a semistructural type.
Fil: Bacigalupe, Alejandro. Instituto Nacional de Tecnología Industrial; Argentina
Fil: Poliszuk, Andrea K.. Instituto Nacional de Tecnología Industrial; Argentina
Fil: Eisenberg, Patricia. Instituto Nacional de Tecnología Industrial; Argentina
Fil: Escobar, Mariano Martin. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Industrial; Argentina
Materia
Wood Adhesives
Biodegradable
Rheology
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:11336/41504
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/41504
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspensionBacigalupe, AlejandroPoliszuk, Andrea K.Eisenberg, PatriciaEscobar, Mariano MartinWood AdhesivesBiodegradableRheologyhttps://purl.org/becyt/ford/2.5https://purl.org/becyt/ford/2The goal of this work is to study the rheological properties of based-modified soy protein concentrate (SPC) adhesives and the relationship between viscoelastic properties and bonding performance. Chemical modification of SPC with sodium hydroxide was made to evaluate the effect of alkali on the viscoelastic properties. Viscosity and solubility depends directly of the 3D structure and the isoelectric point (pI) of the protein. Results show that viscosity is strongly pH dependant due to the protein unfolding. Solubility profiles exhibit the typical U-shaped curve, being higher on either side of isoelectric point. Fourier transformed infrared analysis was used to analyze Amide I (1720-1600 cm-1) and Amide III (1400-1200cm-1) band patterns which reflect the different secondary structures in proteins. The intensity of the band at 1250 cm-1 increases with respect to that at 1235 cm-1 for higher pH values. This could be associated with the destruction, at least partially, of the β-sheet structure. Bonding performance was measured in dry conditions and the wetting properties were analyzed by scanning electron microscopy. The bonding performance improves when the SPC is stabilized at pH 12 due to the protein unfolding, revealing a strong interaction between the secondary structure and the wood surface. As part of an ongoing project it was concluded that alkali modification is a suitable procedure to modify a protein suspension, improving application conditions and mechanical properties of bioadhesives of a semistructural type.Fil: Bacigalupe, Alejandro. Instituto Nacional de Tecnología Industrial; ArgentinaFil: Poliszuk, Andrea K.. Instituto Nacional de Tecnología Industrial; ArgentinaFil: Eisenberg, Patricia. Instituto Nacional de Tecnología Industrial; ArgentinaFil: Escobar, Mariano Martin. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Industrial; ArgentinaElsevier2015-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41504Bacigalupe, Alejandro; Poliszuk, Andrea K.; Eisenberg, Patricia; Escobar, Mariano Martin; Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension; Elsevier; International Journal Of Adhesion And Adhesives; 62; 6-2015; 1-60143-7496CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijadhadh.2015.06.004info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0143749615000834info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:26:17Zoai:ri.conicet.gov.ar:11336/41504instacron: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 14:26:17.501CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
title Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
spellingShingle Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
Bacigalupe, Alejandro
Wood Adhesives
Biodegradable
Rheology
title_short Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
title_full Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
title_fullStr Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
title_full_unstemmed Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
title_sort Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension
dc.creator.none.fl_str_mv Bacigalupe, Alejandro
Poliszuk, Andrea K.
Eisenberg, Patricia
Escobar, Mariano Martin
author Bacigalupe, Alejandro
author_facet Bacigalupe, Alejandro
Poliszuk, Andrea K.
Eisenberg, Patricia
Escobar, Mariano Martin
author_role author
author2 Poliszuk, Andrea K.
Eisenberg, Patricia
Escobar, Mariano Martin
author2_role author
author
author
dc.subject.none.fl_str_mv Wood Adhesives
Biodegradable
Rheology
topic Wood Adhesives
Biodegradable
Rheology
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.5
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The goal of this work is to study the rheological properties of based-modified soy protein concentrate (SPC) adhesives and the relationship between viscoelastic properties and bonding performance. Chemical modification of SPC with sodium hydroxide was made to evaluate the effect of alkali on the viscoelastic properties. Viscosity and solubility depends directly of the 3D structure and the isoelectric point (pI) of the protein. Results show that viscosity is strongly pH dependant due to the protein unfolding. Solubility profiles exhibit the typical U-shaped curve, being higher on either side of isoelectric point. Fourier transformed infrared analysis was used to analyze Amide I (1720-1600 cm-1) and Amide III (1400-1200cm-1) band patterns which reflect the different secondary structures in proteins. The intensity of the band at 1250 cm-1 increases with respect to that at 1235 cm-1 for higher pH values. This could be associated with the destruction, at least partially, of the β-sheet structure. Bonding performance was measured in dry conditions and the wetting properties were analyzed by scanning electron microscopy. The bonding performance improves when the SPC is stabilized at pH 12 due to the protein unfolding, revealing a strong interaction between the secondary structure and the wood surface. As part of an ongoing project it was concluded that alkali modification is a suitable procedure to modify a protein suspension, improving application conditions and mechanical properties of bioadhesives of a semistructural type.
Fil: Bacigalupe, Alejandro. Instituto Nacional de Tecnología Industrial; Argentina
Fil: Poliszuk, Andrea K.. Instituto Nacional de Tecnología Industrial; Argentina
Fil: Eisenberg, Patricia. Instituto Nacional de Tecnología Industrial; Argentina
Fil: Escobar, Mariano Martin. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Industrial; Argentina
description The goal of this work is to study the rheological properties of based-modified soy protein concentrate (SPC) adhesives and the relationship between viscoelastic properties and bonding performance. Chemical modification of SPC with sodium hydroxide was made to evaluate the effect of alkali on the viscoelastic properties. Viscosity and solubility depends directly of the 3D structure and the isoelectric point (pI) of the protein. Results show that viscosity is strongly pH dependant due to the protein unfolding. Solubility profiles exhibit the typical U-shaped curve, being higher on either side of isoelectric point. Fourier transformed infrared analysis was used to analyze Amide I (1720-1600 cm-1) and Amide III (1400-1200cm-1) band patterns which reflect the different secondary structures in proteins. The intensity of the band at 1250 cm-1 increases with respect to that at 1235 cm-1 for higher pH values. This could be associated with the destruction, at least partially, of the β-sheet structure. Bonding performance was measured in dry conditions and the wetting properties were analyzed by scanning electron microscopy. The bonding performance improves when the SPC is stabilized at pH 12 due to the protein unfolding, revealing a strong interaction between the secondary structure and the wood surface. As part of an ongoing project it was concluded that alkali modification is a suitable procedure to modify a protein suspension, improving application conditions and mechanical properties of bioadhesives of a semistructural type.
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/11336/41504
Bacigalupe, Alejandro; Poliszuk, Andrea K.; Eisenberg, Patricia; Escobar, Mariano Martin; Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension; Elsevier; International Journal Of Adhesion And Adhesives; 62; 6-2015; 1-6
0143-7496
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41504
identifier_str_mv Bacigalupe, Alejandro; Poliszuk, Andrea K.; Eisenberg, Patricia; Escobar, Mariano Martin; Rheological behaviorandbondingperformanceofanalkalinesoy proteinsuspension; Elsevier; International Journal Of Adhesion And Adhesives; 62; 6-2015; 1-6
0143-7496
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijadhadh.2015.06.004
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0143749615000834
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
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 13.22299

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