Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
- Autores
- Hidalgo, María Eugenia; Folmer Correa, Ana Paula; Mancilla Canales, Manuel Arturo; Joner Daroit, Daniel; Brandelli, Adriano; Risso, Patricia Hilda
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-delta-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels.
Fil: Hidalgo, María Eugenia. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); Argentina
Fil: Folmer Correa, Ana Paula. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Mancilla Canales, Manuel Arturo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); Argentina
Fil: Joner Daroit, Daniel. Universidade Federal da Fronteira Sul; Brasil
Fil: Brandelli, Adriano. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); Argentina - Materia
-
Bacillus Sp.P7
Bovine Sodium Caseinate
Hydrolysates
Bioactivity
Acid Agreggation And Gelation
Microstructure - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/6194
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Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparationHidalgo, María EugeniaFolmer Correa, Ana PaulaMancilla Canales, Manuel ArturoJoner Daroit, DanielBrandelli, AdrianoRisso, Patricia HildaBacillus Sp.P7Bovine Sodium CaseinateHydrolysatesBioactivityAcid Agreggation And GelationMicrostructurehttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-delta-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels.Fil: Hidalgo, María Eugenia. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); ArgentinaFil: Folmer Correa, Ana Paula. Universidade Federal do Rio Grande do Sul; BrasilFil: Mancilla Canales, Manuel Arturo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); ArgentinaFil: Joner Daroit, Daniel. Universidade Federal da Fronteira Sul; BrasilFil: Brandelli, Adriano. Universidade Federal do Rio Grande do Sul; BrasilFil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); ArgentinaElsevier2014-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/6194Hidalgo, María Eugenia; Folmer Correa, Ana Paula; Mancilla Canales, Manuel Arturo; Joner Daroit, Daniel; Brandelli, Adriano; et al.; Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation; Elsevier; Food Hydrocolloids; 43; 7-2014; 510-5200268-005Xenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X14002525info:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2014.07.009info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:29:23Zoai:ri.conicet.gov.ar:11336/6194instacron: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 14:29:24.116CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
title |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
spellingShingle |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation Hidalgo, María Eugenia Bacillus Sp.P7 Bovine Sodium Caseinate Hydrolysates Bioactivity Acid Agreggation And Gelation Microstructure |
title_short |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
title_full |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
title_fullStr |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
title_full_unstemmed |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
title_sort |
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation |
dc.creator.none.fl_str_mv |
Hidalgo, María Eugenia Folmer Correa, Ana Paula Mancilla Canales, Manuel Arturo Joner Daroit, Daniel Brandelli, Adriano Risso, Patricia Hilda |
author |
Hidalgo, María Eugenia |
author_facet |
Hidalgo, María Eugenia Folmer Correa, Ana Paula Mancilla Canales, Manuel Arturo Joner Daroit, Daniel Brandelli, Adriano Risso, Patricia Hilda |
author_role |
author |
author2 |
Folmer Correa, Ana Paula Mancilla Canales, Manuel Arturo Joner Daroit, Daniel Brandelli, Adriano Risso, Patricia Hilda |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Bacillus Sp.P7 Bovine Sodium Caseinate Hydrolysates Bioactivity Acid Agreggation And Gelation Microstructure |
topic |
Bacillus Sp.P7 Bovine Sodium Caseinate Hydrolysates Bioactivity Acid Agreggation And Gelation Microstructure |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-delta-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels. Fil: Hidalgo, María Eugenia. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); Argentina Fil: Folmer Correa, Ana Paula. Universidade Federal do Rio Grande do Sul; Brasil Fil: Mancilla Canales, Manuel Arturo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); Argentina Fil: Joner Daroit, Daniel. Universidade Federal da Fronteira Sul; Brasil Fil: Brandelli, Adriano. Universidade Federal do Rio Grande do Sul; Brasil Fil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Física de Rosario (i); Argentina |
description |
In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-delta-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-07 |
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/11336/6194 Hidalgo, María Eugenia; Folmer Correa, Ana Paula; Mancilla Canales, Manuel Arturo; Joner Daroit, Daniel; Brandelli, Adriano; et al.; Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation; Elsevier; Food Hydrocolloids; 43; 7-2014; 510-520 0268-005X |
url |
http://hdl.handle.net/11336/6194 |
identifier_str_mv |
Hidalgo, María Eugenia; Folmer Correa, Ana Paula; Mancilla Canales, Manuel Arturo; Joner Daroit, Daniel; Brandelli, Adriano; et al.; Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation; Elsevier; Food Hydrocolloids; 43; 7-2014; 510-520 0268-005X |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0268005X14002525 info:eu-repo/semantics/altIdentifier/doi/ info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodhyd.2014.07.009 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf application/pdf 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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.22299 |