Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food
- Autores
- Dos Santos Da Fonseca, Renata Aline; Silva, Carolina Moroni; Fernandes da Rosa, Giordan; Prentice Hernández, Carlos
- Año de publicación
- 2017
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The fish and its by-products from industrial processing are a rich source of protein. For this reason, cobia (Rachycentron canadum), a large and easily adaptable to aquaculture species has emerged as an option for obtaining peptides. Enzymatic proteolysis is able to release inactive biopeptides ? which may have greater activity when separated into their peptide fractions ? from intact proteins. However, as they can be applied in food, they should be evaluated for any possible harm to health. Thus, this study aimed to evaluate the ability of the protein hydrolysates of cobia (muscle and waste), obtained by the action of Alcalase, Flavourzyme and Protamex enzymes (whole and their fractions less and major than 3 kDa) to inhibit the oxidation of meat food and ensure their food security. The hydrolysates studied in this work demonstrated antioxidant activity through chemical methods in vitro. All hydrolysates and their fractions were not cytotoxic to zebrafish (Danio rerio) hepatocytes at the concentrations of 0.1, 1.0, 10 and 100 g/mL at 0, 24, 48 and 72 h. By etermining the 25 inhibition of thiobarbituric acid reactive substances in bacon and ground beef it was found that the majority of the hydrolysates presented this capacity, highlighting the peptide fractions major than 3 kDa of muscle hydrolysates which reduced by around 50% the TBARS (thiobarbituric acid reactive substances) content formed in the ground beef, and by more than 80% in bacon, probably because the bacon has a higher content of lipid. The enzyme Protamex provided hydrolyzed with more antioxidant activity. Therefore, these results indicate that the hydrolysates studied have the potential to be safe physicochemically, not cytotoxic, used in foods as antioxidants.
Fil: Dos Santos Da Fonseca, Renata Aline. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Silva, Carolina Moroni. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Fernandes da Rosa, Giordan. Universidade Federal do Rio Grande do Sul; Brasil
Fil: Prentice Hernández, Carlos. Universidade Federal do Rio Grande do Sul; Brasil - Materia
-
FOOD SAFETY
LIPID PEROXIDATION
ANTIOXIDANT PEPTIDES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/75326
Ver los metadatos del registro completo
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Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for foodDos Santos Da Fonseca, Renata AlineSilva, Carolina MoroniFernandes da Rosa, GiordanPrentice Hernández, CarlosFOOD SAFETYLIPID PEROXIDATIONANTIOXIDANT PEPTIDEShttps://purl.org/becyt/ford/1.7https://purl.org/becyt/ford/1The fish and its by-products from industrial processing are a rich source of protein. For this reason, cobia (Rachycentron canadum), a large and easily adaptable to aquaculture species has emerged as an option for obtaining peptides. Enzymatic proteolysis is able to release inactive biopeptides ? which may have greater activity when separated into their peptide fractions ? from intact proteins. However, as they can be applied in food, they should be evaluated for any possible harm to health. Thus, this study aimed to evaluate the ability of the protein hydrolysates of cobia (muscle and waste), obtained by the action of Alcalase, Flavourzyme and Protamex enzymes (whole and their fractions less and major than 3 kDa) to inhibit the oxidation of meat food and ensure their food security. The hydrolysates studied in this work demonstrated antioxidant activity through chemical methods in vitro. All hydrolysates and their fractions were not cytotoxic to zebrafish (Danio rerio) hepatocytes at the concentrations of 0.1, 1.0, 10 and 100 g/mL at 0, 24, 48 and 72 h. By etermining the 25 inhibition of thiobarbituric acid reactive substances in bacon and ground beef it was found that the majority of the hydrolysates presented this capacity, highlighting the peptide fractions major than 3 kDa of muscle hydrolysates which reduced by around 50% the TBARS (thiobarbituric acid reactive substances) content formed in the ground beef, and by more than 80% in bacon, probably because the bacon has a higher content of lipid. The enzyme Protamex provided hydrolyzed with more antioxidant activity. Therefore, these results indicate that the hydrolysates studied have the potential to be safe physicochemically, not cytotoxic, used in foods as antioxidants.Fil: Dos Santos Da Fonseca, Renata Aline. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidade Federal do Rio Grande do Sul; BrasilFil: Silva, Carolina Moroni. Universidade Federal do Rio Grande do Sul; BrasilFil: Fernandes da Rosa, Giordan. Universidade Federal do Rio Grande do Sul; BrasilFil: Prentice Hernández, Carlos. Universidade Federal do Rio Grande do Sul; BrasilUniversiti Putra Malaysia. Faculty of Food Science & Technology2017-12info: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/11336/75326Dos Santos Da Fonseca, Renata Aline; Silva, Carolina Moroni; Fernandes da Rosa, Giordan; Prentice Hernández, Carlos; Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food; Universiti Putra Malaysia. Faculty of Food Science & Technology; International Food Research Journal; 24; 6; 12-2017; 2500-25081985-46682231-7546CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.ifrj.upm.edu.my/24%20(06)%202017/(31).pdfinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:01:44Zoai:ri.conicet.gov.ar:11336/75326instacron: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 12:01:44.35CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
title |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
spellingShingle |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food Dos Santos Da Fonseca, Renata Aline FOOD SAFETY LIPID PEROXIDATION ANTIOXIDANT PEPTIDES |
title_short |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
title_full |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
title_fullStr |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
title_full_unstemmed |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
title_sort |
Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food |
dc.creator.none.fl_str_mv |
Dos Santos Da Fonseca, Renata Aline Silva, Carolina Moroni Fernandes da Rosa, Giordan Prentice Hernández, Carlos |
author |
Dos Santos Da Fonseca, Renata Aline |
author_facet |
Dos Santos Da Fonseca, Renata Aline Silva, Carolina Moroni Fernandes da Rosa, Giordan Prentice Hernández, Carlos |
author_role |
author |
author2 |
Silva, Carolina Moroni Fernandes da Rosa, Giordan Prentice Hernández, Carlos |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
FOOD SAFETY LIPID PEROXIDATION ANTIOXIDANT PEPTIDES |
topic |
FOOD SAFETY LIPID PEROXIDATION ANTIOXIDANT PEPTIDES |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.7 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The fish and its by-products from industrial processing are a rich source of protein. For this reason, cobia (Rachycentron canadum), a large and easily adaptable to aquaculture species has emerged as an option for obtaining peptides. Enzymatic proteolysis is able to release inactive biopeptides ? which may have greater activity when separated into their peptide fractions ? from intact proteins. However, as they can be applied in food, they should be evaluated for any possible harm to health. Thus, this study aimed to evaluate the ability of the protein hydrolysates of cobia (muscle and waste), obtained by the action of Alcalase, Flavourzyme and Protamex enzymes (whole and their fractions less and major than 3 kDa) to inhibit the oxidation of meat food and ensure their food security. The hydrolysates studied in this work demonstrated antioxidant activity through chemical methods in vitro. All hydrolysates and their fractions were not cytotoxic to zebrafish (Danio rerio) hepatocytes at the concentrations of 0.1, 1.0, 10 and 100 g/mL at 0, 24, 48 and 72 h. By etermining the 25 inhibition of thiobarbituric acid reactive substances in bacon and ground beef it was found that the majority of the hydrolysates presented this capacity, highlighting the peptide fractions major than 3 kDa of muscle hydrolysates which reduced by around 50% the TBARS (thiobarbituric acid reactive substances) content formed in the ground beef, and by more than 80% in bacon, probably because the bacon has a higher content of lipid. The enzyme Protamex provided hydrolyzed with more antioxidant activity. Therefore, these results indicate that the hydrolysates studied have the potential to be safe physicochemically, not cytotoxic, used in foods as antioxidants. Fil: Dos Santos Da Fonseca, Renata Aline. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario; Argentina. Universidade Federal do Rio Grande do Sul; Brasil Fil: Silva, Carolina Moroni. Universidade Federal do Rio Grande do Sul; Brasil Fil: Fernandes da Rosa, Giordan. Universidade Federal do Rio Grande do Sul; Brasil Fil: Prentice Hernández, Carlos. Universidade Federal do Rio Grande do Sul; Brasil |
description |
The fish and its by-products from industrial processing are a rich source of protein. For this reason, cobia (Rachycentron canadum), a large and easily adaptable to aquaculture species has emerged as an option for obtaining peptides. Enzymatic proteolysis is able to release inactive biopeptides ? which may have greater activity when separated into their peptide fractions ? from intact proteins. However, as they can be applied in food, they should be evaluated for any possible harm to health. Thus, this study aimed to evaluate the ability of the protein hydrolysates of cobia (muscle and waste), obtained by the action of Alcalase, Flavourzyme and Protamex enzymes (whole and their fractions less and major than 3 kDa) to inhibit the oxidation of meat food and ensure their food security. The hydrolysates studied in this work demonstrated antioxidant activity through chemical methods in vitro. All hydrolysates and their fractions were not cytotoxic to zebrafish (Danio rerio) hepatocytes at the concentrations of 0.1, 1.0, 10 and 100 g/mL at 0, 24, 48 and 72 h. By etermining the 25 inhibition of thiobarbituric acid reactive substances in bacon and ground beef it was found that the majority of the hydrolysates presented this capacity, highlighting the peptide fractions major than 3 kDa of muscle hydrolysates which reduced by around 50% the TBARS (thiobarbituric acid reactive substances) content formed in the ground beef, and by more than 80% in bacon, probably because the bacon has a higher content of lipid. The enzyme Protamex provided hydrolyzed with more antioxidant activity. Therefore, these results indicate that the hydrolysates studied have the potential to be safe physicochemically, not cytotoxic, used in foods as antioxidants. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-12 |
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/11336/75326 Dos Santos Da Fonseca, Renata Aline; Silva, Carolina Moroni; Fernandes da Rosa, Giordan; Prentice Hernández, Carlos; Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food; Universiti Putra Malaysia. Faculty of Food Science & Technology; International Food Research Journal; 24; 6; 12-2017; 2500-2508 1985-4668 2231-7546 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/75326 |
identifier_str_mv |
Dos Santos Da Fonseca, Renata Aline; Silva, Carolina Moroni; Fernandes da Rosa, Giordan; Prentice Hernández, Carlos; Peptides obtained from proteins of cobia (Rachycentron canadum): a study of potentially safe antioxidants for food; Universiti Putra Malaysia. Faculty of Food Science & Technology; International Food Research Journal; 24; 6; 12-2017; 2500-2508 1985-4668 2231-7546 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.ifrj.upm.edu.my/24%20(06)%202017/(31).pdf |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Universiti Putra Malaysia. Faculty of Food Science & Technology |
publisher.none.fl_str_mv |
Universiti Putra Malaysia. Faculty of Food Science & Technology |
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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1846782350892990464 |
score |
12.982451 |