Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves

Autores
Gómez Herrera, Melanie Desirée; Alayón Luaces, Paula; Liggieri, Constanza Silvina; Bruno, Mariela Anahí; Avanza, María Victoria
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst.
Fil: Gómez Herrera, Melanie Desirée. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Alayón Luaces, Paula. Universidad Nacional del Nordeste. Facultad de Ciencias Agrarias. Departamento de Protección Vegetal; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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; Argentina
Fil: Avanza, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Materia
ACIDIC PROTEASE
BROMELIA SERRA LEAVES
ENZYMATIC EXTRACT
SIZE-EXCLUSION CHROMATOGRAPHY
THERMAL STABILITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/202841
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/202841
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Proteolytic characterization of a novel enzymatic extract from Bromelia serra leavesGómez Herrera, Melanie DesiréeAlayón Luaces, PaulaLiggieri, Constanza SilvinaBruno, Mariela AnahíAvanza, María VictoriaACIDIC PROTEASEBROMELIA SERRA LEAVESENZYMATIC EXTRACTSIZE-EXCLUSION CHROMATOGRAPHYTHERMAL STABILITYhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst.Fil: Gómez Herrera, Melanie Desirée. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Alayón Luaces, Paula. Universidad Nacional del Nordeste. Facultad de Ciencias Agrarias. Departamento de Protección Vegetal; ArgentinaFil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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; ArgentinaFil: Avanza, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaAcademia Brasileira de Ciencias2022-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/202841Gómez Herrera, Melanie Desirée; Alayón Luaces, Paula; Liggieri, Constanza Silvina; Bruno, Mariela Anahí; Avanza, María Victoria; Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves; Academia Brasileira de Ciencias; Anais da Academia Brasileira de Ciencias; 94; 4; 8-2022; 1-150001-37651678-2690CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.scielo.br/j/aabc/a/xZccRNzRRbKks9fHCMyFkQn/?lang=eninfo:eu-repo/semantics/altIdentifier/doi/10.1590/0001-3765202220201871info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:04:28Zoai:ri.conicet.gov.ar:11336/202841instacron: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:34982025-09-10 13:04:28.412CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
title Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
spellingShingle Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
Gómez Herrera, Melanie Desirée
ACIDIC PROTEASE
BROMELIA SERRA LEAVES
ENZYMATIC EXTRACT
SIZE-EXCLUSION CHROMATOGRAPHY
THERMAL STABILITY
title_short Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
title_full Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
title_fullStr Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
title_full_unstemmed Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
title_sort Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves
dc.creator.none.fl_str_mv Gómez Herrera, Melanie Desirée
Alayón Luaces, Paula
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
Avanza, María Victoria
author Gómez Herrera, Melanie Desirée
author_facet Gómez Herrera, Melanie Desirée
Alayón Luaces, Paula
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
Avanza, María Victoria
author_role author
author2 Alayón Luaces, Paula
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
Avanza, María Victoria
author2_role author
author
author
author
dc.subject.none.fl_str_mv ACIDIC PROTEASE
BROMELIA SERRA LEAVES
ENZYMATIC EXTRACT
SIZE-EXCLUSION CHROMATOGRAPHY
THERMAL STABILITY
topic ACIDIC PROTEASE
BROMELIA SERRA LEAVES
ENZYMATIC EXTRACT
SIZE-EXCLUSION CHROMATOGRAPHY
THERMAL STABILITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst.
Fil: Gómez Herrera, Melanie Desirée. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Alayón Luaces, Paula. Universidad Nacional del Nordeste. Facultad de Ciencias Agrarias. Departamento de Protección Vegetal; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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; Argentina
Fil: Avanza, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
description Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst.
publishDate 2022
dc.date.none.fl_str_mv 2022-08
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/11336/202841
Gómez Herrera, Melanie Desirée; Alayón Luaces, Paula; Liggieri, Constanza Silvina; Bruno, Mariela Anahí; Avanza, María Victoria; Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves; Academia Brasileira de Ciencias; Anais da Academia Brasileira de Ciencias; 94; 4; 8-2022; 1-15
0001-3765
1678-2690
CONICET Digital
CONICET
url http://hdl.handle.net/11336/202841
identifier_str_mv Gómez Herrera, Melanie Desirée; Alayón Luaces, Paula; Liggieri, Constanza Silvina; Bruno, Mariela Anahí; Avanza, María Victoria; Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves; Academia Brasileira de Ciencias; Anais da Academia Brasileira de Ciencias; 94; 4; 8-2022; 1-15
0001-3765
1678-2690
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.scielo.br/j/aabc/a/xZccRNzRRbKks9fHCMyFkQn/?lang=en
info:eu-repo/semantics/altIdentifier/doi/10.1590/0001-3765202220201871
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
application/pdf
dc.publisher.none.fl_str_mv Academia Brasileira de Ciencias
publisher.none.fl_str_mv Academia Brasileira de Ciencias
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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score 12.993085

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