Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions

Autores
Drago, Silvina Rosa; González, Rolando J.; Añon, Maria Cristina
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
BACKGROUND: The aim of this work was to optimize the hydrolysis experimental conditions to obtain wheat gluten hydrolysates and to characterize fractions from hydrolysates with different hydrolysis degrees in order to develop protein functional ingredients. Surface response methodology was used to analyze the effect of reaction factors on the degree of hydrolysis to assess the conditions for maximum fungal protease enzyme activity. Hydrolysates having three different trichloroacetic acid indices (TCAI) were prepared. Soluble fractions at pH 4, 6.5 and 9 from these hydrolysates were characterized by electrophoresis, reverse-phase high-performance liquid chromatography, free amino group content and peptide chain length. RESULTS: Temperature and pH ranges for highest enzyme activity at 2.5 h were 54–58 ◦C and 4.2–4.4, respectively. Hydrolysate fraction composition differs according to the hydrolysis degree and extracting pH, the difference being more pronounced at low TCAI. Hydrolysate having 32% TCAI is composed of peptides whose size is lower than 18.5 kDa, with an average peptide chain length of 14 amino acid residues. CONCLUSION: The combination of hydrolysis degree and pH of extraction allows fractions of different peptide composition to be obtained, which could be taken into account when trying to find a defined composition related to determined functional characteristics.
Fil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: González, Rolando J.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Materia
ENZYMES
EXPERIMENTAL DESIGN
HYDROLYSIS
SURFACE RESPONSE METHODOLOGY
WHEAT GLUTEN
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:11336/160882
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/160882
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractionsDrago, Silvina RosaGonzález, Rolando J.Añon, Maria CristinaENZYMESEXPERIMENTAL DESIGNHYDROLYSISSURFACE RESPONSE METHODOLOGYWHEAT GLUTENhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2BACKGROUND: The aim of this work was to optimize the hydrolysis experimental conditions to obtain wheat gluten hydrolysates and to characterize fractions from hydrolysates with different hydrolysis degrees in order to develop protein functional ingredients. Surface response methodology was used to analyze the effect of reaction factors on the degree of hydrolysis to assess the conditions for maximum fungal protease enzyme activity. Hydrolysates having three different trichloroacetic acid indices (TCAI) were prepared. Soluble fractions at pH 4, 6.5 and 9 from these hydrolysates were characterized by electrophoresis, reverse-phase high-performance liquid chromatography, free amino group content and peptide chain length. RESULTS: Temperature and pH ranges for highest enzyme activity at 2.5 h were 54–58 ◦C and 4.2–4.4, respectively. Hydrolysate fraction composition differs according to the hydrolysis degree and extracting pH, the difference being more pronounced at low TCAI. Hydrolysate having 32% TCAI is composed of peptides whose size is lower than 18.5 kDa, with an average peptide chain length of 14 amino acid residues. CONCLUSION: The combination of hydrolysis degree and pH of extraction allows fractions of different peptide composition to be obtained, which could be taken into account when trying to find a defined composition related to determined functional characteristics.Fil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: González, Rolando J.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaJohn Wiley & Sons Ltd2008-06info: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/11336/160882Drago, Silvina Rosa; González, Rolando J.; Añon, Maria Cristina; Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 88; 8; 6-2008; 1415-14220022-5142CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.3233info:eu-repo/semantics/altIdentifier/doi/10.1002/jsfa.3233info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:17:08Zoai:ri.conicet.gov.ar:11336/160882instacron: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:34982025-10-22 12:17:09.054CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
title Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
spellingShingle Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
Drago, Silvina Rosa
ENZYMES
EXPERIMENTAL DESIGN
HYDROLYSIS
SURFACE RESPONSE METHODOLOGY
WHEAT GLUTEN
title_short Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
title_full Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
title_fullStr Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
title_full_unstemmed Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
title_sort Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions
dc.creator.none.fl_str_mv Drago, Silvina Rosa
González, Rolando J.
Añon, Maria Cristina
author Drago, Silvina Rosa
author_facet Drago, Silvina Rosa
González, Rolando J.
Añon, Maria Cristina
author_role author
author2 González, Rolando J.
Añon, Maria Cristina
author2_role author
author
dc.subject.none.fl_str_mv ENZYMES
EXPERIMENTAL DESIGN
HYDROLYSIS
SURFACE RESPONSE METHODOLOGY
WHEAT GLUTEN
topic ENZYMES
EXPERIMENTAL DESIGN
HYDROLYSIS
SURFACE RESPONSE METHODOLOGY
WHEAT GLUTEN
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv BACKGROUND: The aim of this work was to optimize the hydrolysis experimental conditions to obtain wheat gluten hydrolysates and to characterize fractions from hydrolysates with different hydrolysis degrees in order to develop protein functional ingredients. Surface response methodology was used to analyze the effect of reaction factors on the degree of hydrolysis to assess the conditions for maximum fungal protease enzyme activity. Hydrolysates having three different trichloroacetic acid indices (TCAI) were prepared. Soluble fractions at pH 4, 6.5 and 9 from these hydrolysates were characterized by electrophoresis, reverse-phase high-performance liquid chromatography, free amino group content and peptide chain length. RESULTS: Temperature and pH ranges for highest enzyme activity at 2.5 h were 54–58 ◦C and 4.2–4.4, respectively. Hydrolysate fraction composition differs according to the hydrolysis degree and extracting pH, the difference being more pronounced at low TCAI. Hydrolysate having 32% TCAI is composed of peptides whose size is lower than 18.5 kDa, with an average peptide chain length of 14 amino acid residues. CONCLUSION: The combination of hydrolysis degree and pH of extraction allows fractions of different peptide composition to be obtained, which could be taken into account when trying to find a defined composition related to determined functional characteristics.
Fil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: González, Rolando J.. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
description BACKGROUND: The aim of this work was to optimize the hydrolysis experimental conditions to obtain wheat gluten hydrolysates and to characterize fractions from hydrolysates with different hydrolysis degrees in order to develop protein functional ingredients. Surface response methodology was used to analyze the effect of reaction factors on the degree of hydrolysis to assess the conditions for maximum fungal protease enzyme activity. Hydrolysates having three different trichloroacetic acid indices (TCAI) were prepared. Soluble fractions at pH 4, 6.5 and 9 from these hydrolysates were characterized by electrophoresis, reverse-phase high-performance liquid chromatography, free amino group content and peptide chain length. RESULTS: Temperature and pH ranges for highest enzyme activity at 2.5 h were 54–58 ◦C and 4.2–4.4, respectively. Hydrolysate fraction composition differs according to the hydrolysis degree and extracting pH, the difference being more pronounced at low TCAI. Hydrolysate having 32% TCAI is composed of peptides whose size is lower than 18.5 kDa, with an average peptide chain length of 14 amino acid residues. CONCLUSION: The combination of hydrolysis degree and pH of extraction allows fractions of different peptide composition to be obtained, which could be taken into account when trying to find a defined composition related to determined functional characteristics.
publishDate 2008
dc.date.none.fl_str_mv 2008-06
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/11336/160882
Drago, Silvina Rosa; González, Rolando J.; Añon, Maria Cristina; Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 88; 8; 6-2008; 1415-1422
0022-5142
CONICET Digital
CONICET
url http://hdl.handle.net/11336/160882
identifier_str_mv Drago, Silvina Rosa; González, Rolando J.; Añon, Maria Cristina; Application of surface response methodology to optimize hydrolysis of wheat gluten and characterization of selected hydrolysate fractions; John Wiley & Sons Ltd; Journal of the Science of Food and Agriculture; 88; 8; 6-2008; 1415-1422
0022-5142
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/jsfa.3233
info:eu-repo/semantics/altIdentifier/doi/10.1002/jsfa.3233
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
application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons Ltd
publisher.none.fl_str_mv John Wiley & Sons 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
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score 12.982451

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