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. Practical application: Proteolytic enzymes are employed in the food industry in a wide variety of processes since they modify the properties of proteins causing beneficial effects such as improvement digestibility, diminution of allergenicity, and release of bioactive peptides. Fruits from Bromelia serra possess cysteine peptidases that could be used in food biotechnology because they are capable to hydrolyze soybean and milk proteins by mild working conditions and to provoke the release of bioactive peptides. These hydrolysates containing antioxidative and ACE-inhibitor activities would be useful as ingredients for functional foods or as nutraceuticals, which are nowadays two products highly required by consumers.
Fil: Salese, Lucía. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Liggieri, Constanza Silvina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Bernik, Delia Leticia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina - Materia
-
BIOACTIVE PEPTIDE
BROMELIA SERRA
CYSTEINE PLANT PEPTIDASE
FOOD PROTEIN HYDROLYSATE
FUNCTIONAL FOOD - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/150898
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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 AnahíBIOACTIVE PEPTIDEBROMELIA SERRACYSTEINE PLANT PEPTIDASEFOOD PROTEIN HYDROLYSATEFUNCTIONAL FOODhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2A 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. Practical application: Proteolytic enzymes are employed in the food industry in a wide variety of processes since they modify the properties of proteins causing beneficial effects such as improvement digestibility, diminution of allergenicity, and release of bioactive peptides. Fruits from Bromelia serra possess cysteine peptidases that could be used in food biotechnology because they are capable to hydrolyze soybean and milk proteins by mild working conditions and to provoke the release of bioactive peptides. These hydrolysates containing antioxidative and ACE-inhibitor activities would be useful as ingredients for functional foods or as nutraceuticals, which are nowadays two products highly required by consumers.Fil: Salese, Lucía. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Liggieri, Constanza Silvina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Bernik, Delia Leticia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaWiley Blackwell Publishing, Inc2022-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/150898Salese, Lucía; Liggieri, Constanza Silvina; Bernik, Delia Leticia; Bruno, Mariela Anahí; Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release; Wiley Blackwell Publishing, Inc; Journal Of Food Biochemistry; 46; 1; 1-2022; 1-130145-8884CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/jfbc.14016info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/jfbc.14016info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:38Zoai:ri.conicet.gov.ar:11336/150898instacron: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:34982025-09-03 10:04:38.834CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
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 BIOACTIVE PEPTIDE BROMELIA SERRA CYSTEINE PLANT PEPTIDASE FOOD PROTEIN HYDROLYSATE 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 |
BIOACTIVE PEPTIDE BROMELIA SERRA CYSTEINE PLANT PEPTIDASE FOOD PROTEIN HYDROLYSATE FUNCTIONAL FOOD |
topic |
BIOACTIVE PEPTIDE BROMELIA SERRA CYSTEINE PLANT PEPTIDASE FOOD PROTEIN HYDROLYSATE FUNCTIONAL FOOD |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
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. Practical application: Proteolytic enzymes are employed in the food industry in a wide variety of processes since they modify the properties of proteins causing beneficial effects such as improvement digestibility, diminution of allergenicity, and release of bioactive peptides. Fruits from Bromelia serra possess cysteine peptidases that could be used in food biotechnology because they are capable to hydrolyze soybean and milk proteins by mild working conditions and to provoke the release of bioactive peptides. These hydrolysates containing antioxidative and ACE-inhibitor activities would be useful as ingredients for functional foods or as nutraceuticals, which are nowadays two products highly required by consumers. Fil: Salese, Lucía. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Liggieri, Constanza Silvina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina Fil: Bernik, Delia Leticia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina |
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. Practical application: Proteolytic enzymes are employed in the food industry in a wide variety of processes since they modify the properties of proteins causing beneficial effects such as improvement digestibility, diminution of allergenicity, and release of bioactive peptides. Fruits from Bromelia serra possess cysteine peptidases that could be used in food biotechnology because they are capable to hydrolyze soybean and milk proteins by mild working conditions and to provoke the release of bioactive peptides. These hydrolysates containing antioxidative and ACE-inhibitor activities would be useful as ingredients for functional foods or as nutraceuticals, which are nowadays two products highly required by consumers. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-01 |
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/11336/150898 Salese, Lucía; Liggieri, Constanza Silvina; Bernik, Delia Leticia; Bruno, Mariela Anahí; Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release; Wiley Blackwell Publishing, Inc; Journal Of Food Biochemistry; 46; 1; 1-2022; 1-13 0145-8884 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/150898 |
identifier_str_mv |
Salese, Lucía; Liggieri, Constanza Silvina; Bernik, Delia Leticia; Bruno, Mariela Anahí; Characterization of the fruit proteolytic system of Bromelia serra Griseb. (Bromeliaceae) and its application in bioactive peptides release; Wiley Blackwell Publishing, Inc; Journal Of Food Biochemistry; 46; 1; 1-2022; 1-13 0145-8884 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1111/jfbc.14016 info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/jfbc.14016 |
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 |
dc.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
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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1842269867003084800 |
score |
13.13397 |