Emulsifying properties of Hydrolysates isolated from soybean protein
- Autores
- Panizzolo, Luis Alberto; Añón, María Cristina
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- We have developed new surfactant agents based on hydrolyzed soybean proteins using papain, and we have studied their ability to form and stabilize emulsions. The interfacial behavior and the emulsifying properties were correlated to the structural changes that the proteins underwent. The hydrolysis reaction was stopped by dropping to pH 2 in one case, or rapidly dropping the temperature to -18ºC in the other. The structural and functional properties of the obtained products depended on the way the papain hydrolysis of the soy proteins was stopped. Hydrolysis did not have a beneficial effect on the emulsifying properties of those hydrolysates that were stopped by freezing. For all the degrees of hydrolysis we studied, the emulsifying properties of the isolates were significantly improved when the hydrolysis reaction was stopped by dropping to pH 2.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos - Materia
-
Química
Soy proteins
Enzymatic hydrolysis
Emulsion properties - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/98492
Ver los metadatos del registro completo
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Emulsifying properties of Hydrolysates isolated from soybean proteinPanizzolo, Luis AlbertoAñón, María CristinaQuímicaSoy proteinsEnzymatic hydrolysisEmulsion propertiesWe have developed new surfactant agents based on hydrolyzed soybean proteins using papain, and we have studied their ability to form and stabilize emulsions. The interfacial behavior and the emulsifying properties were correlated to the structural changes that the proteins underwent. The hydrolysis reaction was stopped by dropping to pH 2 in one case, or rapidly dropping the temperature to -18ºC in the other. The structural and functional properties of the obtained products depended on the way the papain hydrolysis of the soy proteins was stopped. Hydrolysis did not have a beneficial effect on the emulsifying properties of those hydrolysates that were stopped by freezing. For all the degrees of hydrolysis we studied, the emulsifying properties of the isolates were significantly improved when the hydrolysis reaction was stopped by dropping to pH 2.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2015-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf223-233http://sedici.unlp.edu.ar/handle/10915/98492enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/10567info:eu-repo/semantics/altIdentifier/url/http://www.sciencepublishinggroup.com/journal/paperinfo.aspx?journalid=153&doi=10.11648/j.ijnfs.20150402.24info:eu-repo/semantics/altIdentifier/issn/2327-2716info:eu-repo/semantics/altIdentifier/doi/10.11648/j.ijnfs.20150402.24info:eu-repo/semantics/altIdentifier/hdl/11336/10567info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:52:06Zoai:sedici.unlp.edu.ar:10915/98492Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:52:06.501SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Emulsifying properties of Hydrolysates isolated from soybean protein |
title |
Emulsifying properties of Hydrolysates isolated from soybean protein |
spellingShingle |
Emulsifying properties of Hydrolysates isolated from soybean protein Panizzolo, Luis Alberto Química Soy proteins Enzymatic hydrolysis Emulsion properties |
title_short |
Emulsifying properties of Hydrolysates isolated from soybean protein |
title_full |
Emulsifying properties of Hydrolysates isolated from soybean protein |
title_fullStr |
Emulsifying properties of Hydrolysates isolated from soybean protein |
title_full_unstemmed |
Emulsifying properties of Hydrolysates isolated from soybean protein |
title_sort |
Emulsifying properties of Hydrolysates isolated from soybean protein |
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 Emulsion properties |
topic |
Química Soy proteins Enzymatic hydrolysis Emulsion properties |
dc.description.none.fl_txt_mv |
We have developed new surfactant agents based on hydrolyzed soybean proteins using papain, and we have studied their ability to form and stabilize emulsions. The interfacial behavior and the emulsifying properties were correlated to the structural changes that the proteins underwent. The hydrolysis reaction was stopped by dropping to pH 2 in one case, or rapidly dropping the temperature to -18ºC in the other. The structural and functional properties of the obtained products depended on the way the papain hydrolysis of the soy proteins was stopped. Hydrolysis did not have a beneficial effect on the emulsifying properties of those hydrolysates that were stopped by freezing. For all the degrees of hydrolysis we studied, the emulsifying properties of the isolates were significantly improved when the hydrolysis reaction was stopped by dropping to pH 2. Centro de Investigación y Desarrollo en Criotecnología de Alimentos |
description |
We have developed new surfactant agents based on hydrolyzed soybean proteins using papain, and we have studied their ability to form and stabilize emulsions. The interfacial behavior and the emulsifying properties were correlated to the structural changes that the proteins underwent. The hydrolysis reaction was stopped by dropping to pH 2 in one case, or rapidly dropping the temperature to -18ºC in the other. The structural and functional properties of the obtained products depended on the way the papain hydrolysis of the soy proteins was stopped. Hydrolysis did not have a beneficial effect on the emulsifying properties of those hydrolysates that were stopped by freezing. For all the degrees of hydrolysis we studied, the emulsifying properties of the isolates were significantly improved when the hydrolysis reaction was stopped by dropping to pH 2. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-03 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo 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://sedici.unlp.edu.ar/handle/10915/98492 |
url |
http://sedici.unlp.edu.ar/handle/10915/98492 |
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/11336/10567 info:eu-repo/semantics/altIdentifier/url/http://www.sciencepublishinggroup.com/journal/paperinfo.aspx?journalid=153&doi=10.11648/j.ijnfs.20150402.24 info:eu-repo/semantics/altIdentifier/issn/2327-2716 info:eu-repo/semantics/altIdentifier/doi/10.11648/j.ijnfs.20150402.24 info:eu-repo/semantics/altIdentifier/hdl/11336/10567 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 223-233 |
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