Foaming properties of soy protein isolate hydrolysates

Autores
Panizzolo, Luis Alberto; Añón, María Cristina
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Química
Soy proteins
Enzymatic hydrolysis
Foaming properties
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/101387
Acceder
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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Foaming properties of soy protein isolate hydrolysatesPanizzolo, Luis AlbertoAñón, María CristinaQuímicaSoy proteinsEnzymatic hydrolysisFoaming propertiesTensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).Centro de Investigación y Desarrollo en Criotecnología de Alimentos2015-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1-9http://sedici.unlp.edu.ar/handle/10915/101387enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/12083info:eu-repo/semantics/altIdentifier/url/http://www.sciencepublishinggroup.com/journal/paperinfo.aspx?journalid=154&doi=10.11648/j.jfns.20150301.11info:eu-repo/semantics/altIdentifier/issn/2330-7293info:eu-repo/semantics/altIdentifier/doi/10.11648/j.jfns.20150301.11info:eu-repo/semantics/altIdentifier/hdl/11336/12083info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:52:07Zoai:sedici.unlp.edu.ar:10915/101387Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:52:07.307SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Foaming properties of soy protein isolate hydrolysates
title Foaming properties of soy protein isolate hydrolysates
spellingShingle Foaming properties of soy protein isolate hydrolysates
Panizzolo, Luis Alberto
Química
Soy proteins
Enzymatic hydrolysis
Foaming properties
title_short Foaming properties of soy protein isolate hydrolysates
title_full Foaming properties of soy protein isolate hydrolysates
title_fullStr Foaming properties of soy protein isolate hydrolysates
title_full_unstemmed Foaming properties of soy protein isolate hydrolysates
title_sort Foaming properties of soy protein isolate hydrolysates
dc.creator.none.fl_str_mv Panizzolo, Luis Alberto
Añón, María Cristina
author Panizzolo, Luis Alberto
author_facet Panizzolo, Luis Alberto
Añón, María Cristina
author_role author
author2 Añón, María Cristina
author2_role author
dc.subject.none.fl_str_mv Química
Soy proteins
Enzymatic hydrolysis
Foaming properties
topic Química
Soy proteins
Enzymatic hydrolysis
Foaming properties
dc.description.none.fl_txt_mv Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description Tensoactive species obtained by papain hydrolysis of soy protein were characterized structurally and physicochemically, and their foam-forming and -stabilizing capacity studied. Protein structural changes upon reaction ending were correlated with functional and interfacial properties and with the behaviour thereof with varying hydrolysis degree. Two different means of halting hydrolysis -pH reduction (pH=2) and quick freezing (-18ºC), respectively- were studied. Distinct structural changes and associated functional properties were found according to reaction ending conditions. No improvement of foaming properties was found for partially-hydrolyzed isolates subject to freezing at reaction ending - with respect to the starting unhydrolyzed soy protein isolate. In contrast, pH treatment as a means of halting hydrolysis led to a significant enhancement of the foaming properties of soybean protein hydrolysates consistently for all studied hydrolysis degrees (0%, 1.8%, 2.5% and 6%).
publishDate 2015
dc.date.none.fl_str_mv 2015-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:ar-repo/semantics/articulo
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status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/101387
url http://sedici.unlp.edu.ar/handle/10915/101387
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/12083
info:eu-repo/semantics/altIdentifier/url/http://www.sciencepublishinggroup.com/journal/paperinfo.aspx?journalid=154&doi=10.11648/j.jfns.20150301.11
info:eu-repo/semantics/altIdentifier/issn/2330-7293
info:eu-repo/semantics/altIdentifier/doi/10.11648/j.jfns.20150301.11
info:eu-repo/semantics/altIdentifier/hdl/11336/12083
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
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instname_str Universidad Nacional de La Plata
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repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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