Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release
- Autores
- Salese, Lucía; Liggieri, Constanza Silvina; Bernik, Delia Leticia; Bruno, Mariela Anahí
- Año de publicación
- 2022
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A crude extract with proteolytic activity was prepared from edible fruits of Bromelia serra, containing cysteine peptidases with molecular masses between 24.1 and 25.9 kDa. The extract presented an optimal pH range of 6.03‒9.05, retained more than 80% of activity after thermal pre-treatments at 23, 37, and 45°C (120 min), but it was rapidly inactivated after 10 min at 75°C. These proteases were employed to hydrolyze soybean proteins, bovine casein and bovine whey, achieving degrees of hydrolysis of 18.3 ± 0.6, 29.1 ± 0.7, and 12.6 ± 0.9% (55°C, 180 min), respectively. The casein 180 min-hydrolysate (55°C) presented the maximum value of antioxidant activity (2.89 ± 0.12 mg/mL Trolox), and the whey protein 180 min-hydrolysate (55°C) showed the highest percentage of angiotensin-converting enzyme inhibition (91.9 ± 1.2%). This low-cost enzymatic preparation would be promising for the food industry because it requires mild working conditions and yields hydrolysates with biological activities useful as ingredients for functional food.
Centro de Investigación de Proteínas Vegetales - Materia
-
Bioquímica
bioactive peptide
Bromelia serra
food protein hydrolysate
cysteine plant peptidase
functional food - 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:10915/159152
Ver los metadatos del registro completo
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Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides releaseSalese, LucíaLiggieri, Constanza SilvinaBernik, Delia LeticiaBruno, Mariela AnahíBioquímicabioactive peptideBromelia serrafood protein hydrolysatecysteine plant peptidasefunctional foodA crude extract with proteolytic activity was prepared from edible fruits of Bromelia serra, containing cysteine peptidases with molecular masses between 24.1 and 25.9 kDa. The extract presented an optimal pH range of 6.03‒9.05, retained more than 80% of activity after thermal pre-treatments at 23, 37, and 45°C (120 min), but it was rapidly inactivated after 10 min at 75°C. These proteases were employed to hydrolyze soybean proteins, bovine casein and bovine whey, achieving degrees of hydrolysis of 18.3 ± 0.6, 29.1 ± 0.7, and 12.6 ± 0.9% (55°C, 180 min), respectively. The casein 180 min-hydrolysate (55°C) presented the maximum value of antioxidant activity (2.89 ± 0.12 mg/mL Trolox), and the whey protein 180 min-hydrolysate (55°C) showed the highest percentage of angiotensin-converting enzyme inhibition (91.9 ± 1.2%). This low-cost enzymatic preparation would be promising for the food industry because it requires mild working conditions and yields hydrolysates with biological activities useful as ingredients for functional food.Centro de Investigación de Proteínas Vegetales2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/159152enginfo:eu-repo/semantics/altIdentifier/issn/1745-4514info:eu-repo/semantics/altIdentifier/issn/0145-8884info:eu-repo/semantics/altIdentifier/doi/10.1111/jfbc.14016info: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:UNLP2025-09-03T11:13:33Zoai:sedici.unlp.edu.ar:10915/159152Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:13:34.141SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
title |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
spellingShingle |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release Salese, Lucía Bioquímica bioactive peptide Bromelia serra food protein hydrolysate cysteine plant peptidase functional food |
title_short |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
title_full |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
title_fullStr |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
title_full_unstemmed |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
title_sort |
Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release |
dc.creator.none.fl_str_mv |
Salese, Lucía Liggieri, Constanza Silvina Bernik, Delia Leticia Bruno, Mariela Anahí |
author |
Salese, Lucía |
author_facet |
Salese, Lucía Liggieri, Constanza Silvina Bernik, Delia Leticia Bruno, Mariela Anahí |
author_role |
author |
author2 |
Liggieri, Constanza Silvina Bernik, Delia Leticia Bruno, Mariela Anahí |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Bioquímica bioactive peptide Bromelia serra food protein hydrolysate cysteine plant peptidase functional food |
topic |
Bioquímica bioactive peptide Bromelia serra food protein hydrolysate cysteine plant peptidase functional food |
dc.description.none.fl_txt_mv |
A crude extract with proteolytic activity was prepared from edible fruits of Bromelia serra, containing cysteine peptidases with molecular masses between 24.1 and 25.9 kDa. The extract presented an optimal pH range of 6.03‒9.05, retained more than 80% of activity after thermal pre-treatments at 23, 37, and 45°C (120 min), but it was rapidly inactivated after 10 min at 75°C. These proteases were employed to hydrolyze soybean proteins, bovine casein and bovine whey, achieving degrees of hydrolysis of 18.3 ± 0.6, 29.1 ± 0.7, and 12.6 ± 0.9% (55°C, 180 min), respectively. The casein 180 min-hydrolysate (55°C) presented the maximum value of antioxidant activity (2.89 ± 0.12 mg/mL Trolox), and the whey protein 180 min-hydrolysate (55°C) showed the highest percentage of angiotensin-converting enzyme inhibition (91.9 ± 1.2%). This low-cost enzymatic preparation would be promising for the food industry because it requires mild working conditions and yields hydrolysates with biological activities useful as ingredients for functional food. Centro de Investigación de Proteínas Vegetales |
description |
A crude extract with proteolytic activity was prepared from edible fruits of Bromelia serra, containing cysteine peptidases with molecular masses between 24.1 and 25.9 kDa. The extract presented an optimal pH range of 6.03‒9.05, retained more than 80% of activity after thermal pre-treatments at 23, 37, and 45°C (120 min), but it was rapidly inactivated after 10 min at 75°C. These proteases were employed to hydrolyze soybean proteins, bovine casein and bovine whey, achieving degrees of hydrolysis of 18.3 ± 0.6, 29.1 ± 0.7, and 12.6 ± 0.9% (55°C, 180 min), respectively. The casein 180 min-hydrolysate (55°C) presented the maximum value of antioxidant activity (2.89 ± 0.12 mg/mL Trolox), and the whey protein 180 min-hydrolysate (55°C) showed the highest percentage of angiotensin-converting enzyme inhibition (91.9 ± 1.2%). This low-cost enzymatic preparation would be promising for the food industry because it requires mild working conditions and yields hydrolysates with biological activities useful as ingredients for functional food. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022 |
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/10915/159152 |
url |
http://sedici.unlp.edu.ar/handle/10915/159152 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/1745-4514 info:eu-repo/semantics/altIdentifier/issn/0145-8884 info:eu-repo/semantics/altIdentifier/doi/10.1111/jfbc.14016 |
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 |
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