Enzymatic Hydrolysis of Soy Protein Isolates : DSC study
- Autores
- Molina Ortiz, Sara E.; Añón, María Cristina
- Año de publicación
- 2001
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The aim of this work was to analyze the possible use of differential scanning calorimetry (DSC) as a method to study the process of protein modifications during enzymatic hydrolysis. Results of the enzymatic hydrolysis of soy protein showed significant differences in the values of maximum deflection temperature (Tp), heat of reaction (ΔH), and width at half peak height (ΔT1/2), between DSC curves corresponding to the substrate, or zerotime of hydrolysis, and those of the hydrolysates obtained by the action of cucurbita and pomiferin enzymes. DSC curve changes mentioned were explained by the use of gel-filtration chromatography, denaturing electrophoresis and surface hydrophobicity of the hydrolysis products obtained at 30 min of reaction.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos - Materia
-
Bioquímica
DSC
hydrolysis
soy proteins - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
.jpg)
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/140987
Ver los metadatos del registro completo
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Enzymatic Hydrolysis of Soy Protein Isolates : DSC studyMolina Ortiz, Sara E.Añón, María CristinaBioquímicaDSChydrolysissoy proteinsThe aim of this work was to analyze the possible use of differential scanning calorimetry (DSC) as a method to study the process of protein modifications during enzymatic hydrolysis. Results of the enzymatic hydrolysis of soy protein showed significant differences in the values of maximum deflection temperature (Tp), heat of reaction (ΔH), and width at half peak height (ΔT1/2), between DSC curves corresponding to the substrate, or zerotime of hydrolysis, and those of the hydrolysates obtained by the action of cucurbita and pomiferin enzymes. DSC curve changes mentioned were explained by the use of gel-filtration chromatography, denaturing electrophoresis and surface hydrophobicity of the hydrolysis products obtained at 30 min of reaction.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2001info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf489-499http://sedici.unlp.edu.ar/handle/10915/140987enginfo:eu-repo/semantics/altIdentifier/issn/1418-2874info:eu-repo/semantics/altIdentifier/doi/10.1023/a:1013112900718info: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:UNLP2025-09-03T11:04:13Zoai:sedici.unlp.edu.ar:10915/140987Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:13.601SEDICI (UNLP) - Universidad Nacional de La Platafalse |
| dc.title.none.fl_str_mv |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| title |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| spellingShingle |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study Molina Ortiz, Sara E. Bioquímica DSC hydrolysis soy proteins |
| title_short |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| title_full |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| title_fullStr |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| title_full_unstemmed |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| title_sort |
Enzymatic Hydrolysis of Soy Protein Isolates : DSC study |
| dc.creator.none.fl_str_mv |
Molina Ortiz, Sara E. Añón, María Cristina |
| author |
Molina Ortiz, Sara E. |
| author_facet |
Molina Ortiz, Sara E. Añón, María Cristina |
| author_role |
author |
| author2 |
Añón, María Cristina |
| author2_role |
author |
| dc.subject.none.fl_str_mv |
Bioquímica DSC hydrolysis soy proteins |
| topic |
Bioquímica DSC hydrolysis soy proteins |
| dc.description.none.fl_txt_mv |
The aim of this work was to analyze the possible use of differential scanning calorimetry (DSC) as a method to study the process of protein modifications during enzymatic hydrolysis. Results of the enzymatic hydrolysis of soy protein showed significant differences in the values of maximum deflection temperature (Tp), heat of reaction (ΔH), and width at half peak height (ΔT1/2), between DSC curves corresponding to the substrate, or zerotime of hydrolysis, and those of the hydrolysates obtained by the action of cucurbita and pomiferin enzymes. DSC curve changes mentioned were explained by the use of gel-filtration chromatography, denaturing electrophoresis and surface hydrophobicity of the hydrolysis products obtained at 30 min of reaction. Centro de Investigación y Desarrollo en Criotecnología de Alimentos |
| description |
The aim of this work was to analyze the possible use of differential scanning calorimetry (DSC) as a method to study the process of protein modifications during enzymatic hydrolysis. Results of the enzymatic hydrolysis of soy protein showed significant differences in the values of maximum deflection temperature (Tp), heat of reaction (ΔH), and width at half peak height (ΔT1/2), between DSC curves corresponding to the substrate, or zerotime of hydrolysis, and those of the hydrolysates obtained by the action of cucurbita and pomiferin enzymes. DSC curve changes mentioned were explained by the use of gel-filtration chromatography, denaturing electrophoresis and surface hydrophobicity of the hydrolysis products obtained at 30 min of reaction. |
| publishDate |
2001 |
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2001 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://sedici.unlp.edu.ar/handle/10915/140987 |
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http://sedici.unlp.edu.ar/handle/10915/140987 |
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eng |
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eng |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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