Proteolytic characterization of a novel enzymatic extract from Bromelia serra leaves

Detalhes bibliográficos
Autor(a) principal: HERRERA,MELANIE D. GÓMEZ
Data de Publicação: 2022
Outros Autores: LUACES,PAULA ALAYÓN, LIGGIERI,CONSTANZA, BRUNO,MARIELA, AVANZA,MARÍA VICTORIA
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Anais da Academia Brasileira de Ciências (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501
Resumo: Abstract 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.
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spelling Proteolytic characterization of a novel enzymatic extract from Bromelia serra leavesAcidic proteaseBromelia serra leavesenzymatic extractsize-exclusion chromatographythermal stabilityAbstract 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.Academia Brasileira de Ciências2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501Anais da Academia Brasileira de Ciências v.94 n.4 2022reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765202220201871info:eu-repo/semantics/openAccessHERRERA,MELANIE D. GÓMEZLUACES,PAULA ALAYÓNLIGGIERI,CONSTANZABRUNO,MARIELAAVANZA,MARÍA VICTORIAeng2022-08-02T00:00:00Zoai:scielo:S0001-37652022000600501Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2022-08-02T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false
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
HERRERA,MELANIE D. GÓMEZ
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
author HERRERA,MELANIE D. GÓMEZ
author_facet HERRERA,MELANIE D. GÓMEZ
LUACES,PAULA ALAYÓN
LIGGIERI,CONSTANZA
BRUNO,MARIELA
AVANZA,MARÍA VICTORIA
author_role author
author2 LUACES,PAULA ALAYÓN
LIGGIERI,CONSTANZA
BRUNO,MARIELA
AVANZA,MARÍA VICTORIA
author2_role author
author
author
author
dc.contributor.author.fl_str_mv HERRERA,MELANIE D. GÓMEZ
LUACES,PAULA ALAYÓN
LIGGIERI,CONSTANZA
BRUNO,MARIELA
AVANZA,MARÍA VICTORIA
dc.subject.por.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
description Abstract 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 2022-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652022000600501
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0001-3765202220201871
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Academia Brasileira de Ciências
publisher.none.fl_str_mv Academia Brasileira de Ciências
dc.source.none.fl_str_mv Anais da Academia Brasileira de Ciências v.94 n.4 2022
reponame:Anais da Academia Brasileira de Ciências (Online)
instname:Academia Brasileira de Ciências (ABC)
instacron:ABC
instname_str Academia Brasileira de Ciências (ABC)
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reponame_str Anais da Academia Brasileira de Ciências (Online)
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repository.name.fl_str_mv Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)
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